Phospholipases a2 secretory. Medical search

A class of enzymes that catalyze the hydrolysis of phosphoglycerides or glycerophosphatidates. EC 3.1.-.

Phospholipases that hydrolyze one of the acyl groups of phosphoglycerides or glycerophosphatidates.

Phospholipases that hydrolyze the acyl group attached to the 2-position of PHOSPHOGLYCERIDES.

A phospholipase that hydrolyzes the acyl group attached to the 1-position of PHOSPHOGLYCERIDES.

A subcategory of secreted phospholipases A2 that includes enzymes isolated from a variety of sources. The creation of this group is based upon similarities in the structural determinants of the enzymes including a negatively charged carboxy-terminal segment.

A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS.

A secreted phospholipase A2 subtype that contains a interfacial-binding region with specificity for PHOSPHATIDYLCHOLINE. This enzyme group may play a role in eliciting ARACHIDONIC ACID release from intact cellular membranes and from LOW DENSITY LIPOPROTEINS. Members of this group bind specifically to PHOSPHOLIPASE A2 RECEPTORS.

A subcategory of phospholipases A2 that are secreted from cells. They are 14 kDa proteins containing multiple disulfide-bonds and access their substrate via an interfacial binding site that interacts with phospholipid membranes. In addition specific PHOSPHOLIPASE A2 RECEPTORS can bind to and internalize the enzymes.

A subcategory of secreted phospholipases A2 that includes enzymes isolated from ELAPID VENOMS and pancreatic sources. The creation of this group is based upon similarities in the structural determinants of the enzymes.

An enzyme that catalyzes the hydrolysis of a single fatty acid ester bond in lysoglycerophosphatidates with the formation of glyceryl phosphatidates and a fatty acid. EC 3.1.1.5.

A subcategory of secreted phospholipases A2 that contains both a negatively charged carboxy-terminal segment and interfacial-binding region specific for PHOSPHATIDYL CHOLINE-containing membranes. This enzyme group may play a role in the release of ARACHIDONIC ACID from phospholipid membranes.

Solutions or mixtures of toxic and nontoxic substances elaborated by snake (Ophidia) salivary glands for the purpose of killing prey or disabling predators and delivered by grooved or hollow fangs. They usually contain enzymes, toxins, and other factors.

An enzyme found mostly in plant tissue. It hydrolyzes glycerophosphatidates with the formation of a phosphatidic acid and a nitrogenous base such as choline. This enzyme also catalyzes transphosphatidylation reactions. EC 3.1.4.4.

Venoms from snakes of the subfamily Crotalinae or pit vipers, found mostly in the Americas. They include the rattlesnake, cottonmouth, fer-de-lance, bushmaster, and American copperhead. Their venoms contain nontoxic proteins, cardio-, hemo-, cyto-, and neurotoxins, and many enzymes, especially phospholipases A. Many of the toxins have been characterized.

Cell surface receptors that bind to and internalize SECRETED PHOSPHOLIPASES A2. Although primarily acting as scavenger receptors, these proteins may also play a role in intracellular signaling. Soluble forms of phospholipase A2 receptors occur through the action of proteases and may a play a role in the inhibition of extracellular phospholipase activity.

A calcium-independent phospholipase A2 group that may play a role in membrane phospholipid remodeling and homeostasis by controling the levels of PHOSPHATIDYLCHOLINE in mammalian cell membranes.

Venoms from snakes of the genus Naja (family Elapidae). They contain many specific proteins that have cytotoxic, hemolytic, neurotoxic, and other properties. Like other elapid venoms, they are rich in enzymes. They include cobramines and cobralysins.

A cytosolic phospholipase A2 group that plays an important role in the release of free ARACHIDONIC ACID, which in turn is metabolized to PROSTAGLANDINS by the CYCLOOXYGENASE pathway and to LEUKOTRIENES by the 5-LIPOXYGENASE pathway.

A family of snakes comprising three subfamilies: Azemiopinae (the mountain viper, the sole member of this subfamily), Viperinae (true vipers), and Crotalinae (pit vipers). They are widespread throughout the world, being found in the United States, Central and South America, Europe, Asia and Africa. Their venoms act on the blood (hemotoxic) as compared to the venom of elapids which act on the nervous system (neurotoxic). (Goin, Goin, and Zug, Introduction to Herpetology, 3d ed, pp333-36)

A genus of poisonous snakes of the VIPERIDAE family. About 50 species are known and all are found in tropical America and southern South America. Bothrops atrox is the fer-de-lance and B. jararaca is the jararaca. (Goin, Goin, and Zug, Introduction to Herpetology, 3d ed, p336)

Proteins obtained from species of REPTILES.

Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.

Venoms from SNAKES of the viperid family. They tend to be less toxic than elapid or hydrophid venoms and act mainly on the vascular system, interfering with coagulation and capillary membrane integrity and are highly cytotoxic. They contain large amounts of several enzymes, other factors, and some toxins.

A specific complex of toxic proteins from the venom of Crotalus durissus terrificus (South American rattlesnake). It can be separated into a phospholipase A and crotapotin fragment; the latter consists of three different amino acid chains, potentiates the enzyme, and is specifically neurotoxic.

A subcategory of secreted phospholipases A2 with specificity for PHOSPHATIDYLETHANOLAMINES and PHOSPHATIDYLCHOLINE. It occurs as a component of VENOMS and as a mammalian secretory phospholipase A2. The creation of this group is based upon similarities in the structural determinants of the enzymes including a long amino-terminal domain, a conserved group III-specific domain, and a long carboxyl-terminal domain.

Venoms from snakes of the family Elapidae, including cobras, kraits, mambas, coral, tiger, and Australian snakes. The venoms contain polypeptide toxins of various kinds, cytolytic, hemolytic, and neurotoxic factors, but fewer enzymes than viper or crotalid venoms. Many of the toxins have been characterized.

Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a choline moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and choline and 2 moles of fatty acids.

A family of extremely venomous snakes, comprising coral snakes, cobras, mambas, kraits, and sea snakes. They are widely distributed, being found in the southern United States, South America, Africa, southern Asia, Australia, and the Pacific Islands. The elapids include three subfamilies: Elapinae, Hydrophiinae, and Lauticaudinae. Like the viperids, they have venom fangs in the front part of the upper jaw. The mambas of Africa are the most dangerous of all snakes by virtue of their size, speed, and highly toxic venom. (Goin, Goin, and Zug, Introduction to Herpetology, 3d ed, p329-33)

An unsaturated, essential fatty acid. It is found in animal and human fat as well as in the liver, brain, and glandular organs, and is a constituent of animal phosphatides. It is formed by the synthesis from dietary linoleic acid and is a precursor in the biosynthesis of prostaglandins, thromboxanes, and leukotrienes.

A subcategory of phospholipases A2 that occur in the CYTOSOL.

A subcategory of structurally-related phospholipases A2 that do not require calcium for activity.

The process of cleaving a chemical compound by the addition of a molecule of water.

Venoms obtained from Apis mellifera (honey bee) and related species. They contain various enzymes, polypeptide toxins, and other substances, some of which are allergenic or immunogenic or both. These venoms were formerly used in rheumatism to stimulate the pituitary-adrenal system.

A subclass of group I phospholipases A2 that includes enzymes isolated from ELAPID VENOMS.

Compounds that inhibit or block the activity of a PHOSPHOLIPASE A2 enzyme.

Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids.

A phosphorus-oxygen lyase found primarily in BACTERIA. The enzyme catalyzes the cleavage of a phosphoester linkage in 1-phosphatidyl-1D-myo-inositol to form 1D-myo-inositol 1,2-cyclic phosphate and diacylglycerol. The enzyme was formerly classified as a phosphoric diester hydrolase (EC 3.1.4.10) and is often referred to as a TYPE C PHOSPHOLIPASES. However it is now known that a cyclic phosphate is the final product of this enzyme and that water does not enter into the reaction.

Limbless REPTILES of the suborder Serpentes.

Fatty acid derivatives of glycerophosphates. They are composed of glycerol bound in ester linkage with 1 mole of phosphoric acid at the terminal 3-hydroxyl group and with 2 moles of fatty acids at the other two hydroxyl groups.

Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.

A species of rod-shaped bacteria that is a common soil saprophyte. Its spores are widespread and multiplication has been observed chiefly in foods. Contamination may lead to food poisoning.

A genus of snakes of the family VIPERIDAE, one of the pit vipers, so-called from the pit hollowing out the maxillary bone, opening between the eye and the nostril. They are distinctively American serpents. Most of the 25 recognized species are found in the southwestern United States and northern Mexico. Several species are found as far north as Canada and east of the Mississippi, including southern Appalachia. They are named for the jointed rattle (Greek krotalon) at the tip of their tail. (Goin, Goin, and Zug: Introduction to Herpetology, 3d ed; Moore: Poisonous Snakes of the World, 1980, p335)

Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to an ethanolamine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and ethanolamine and 2 moles of fatty acids.

A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.

The rate dynamics in chemical or physical systems.

An acridine derivative formerly widely used as an antimalarial but superseded by chloroquine in recent years. It has also been used as an anthelmintic and in the treatment of giardiasis and malignant effusions. It is used in cell biological experiments as an inhibitor of phospholipase A2.

Lipids, predominantly phospholipids, cholesterol and small amounts of glycolipids found in membranes including cellular and intracellular membranes. These lipids may be arranged in bilayers in the membranes with integral proteins between the layers and peripheral proteins attached to the outside. Membrane lipids are required for active transport, several enzymatic activities and membrane formation.

A genus of snakes of the family VIPERIDAE. About 30 species are currently recognized, found in southeast Asia and adjacent island chains. The Okinawa habu frequently enters dwellings in search of rats and mice; the Chinese habu is often found in suburban and agricultural areas. They are quite irritable. (Moore: Poisonous Snakes of the World, 1980, p136)

Arachidonic acids are polyunsaturated fatty acids, specifically a type of omega-6 fatty acid, that are essential for human nutrition and play crucial roles in various biological processes, including inflammation, immunity, and cell signaling. They serve as precursors to eicosanoids, which are hormone-like substances that mediate a wide range of physiological responses.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

A type C phospholipase with specificity towards PHOSPHATIDYLINOSITOLS that contain INOSITOL 1,4,5-TRISPHOSPHATE. Many of the enzymes listed under this classification are involved in intracellular signaling.

Keto-pyrans.

Derivatives of PHOSPHATIDYLCHOLINES obtained by their partial hydrolysis which removes one of the fatty acid moieties.

A subclass of group I phospholipases A2 that includes enzymes isolated from PANCREATIC JUICE. Members of this group have specificity for PHOSPHOLIPASE A2 RECEPTORS.

Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

Diglycerides are a type of glyceride, specifically a form of lipid, that contains two fatty acid chains linked to a glycerol molecule by ester bonds.

Thiones are organic compounds containing a sulfur atom bonded to two carbon atoms, often found in certain drugs and naturally occurring substances, which possess various pharmacological activities.

A genus of snakes of the family VIPERIDAE. It is distributed in West Pakistan, most of India, Burma, Ceylon, Thailand, southeast China, Taiwan, and a few islands of Indonesia. It hisses loudly when disturbed and strikes with great force and speed. Very prolific, it gives birth to 20-60 young. This viper is the leading cause of snakebite in India and Burma. (Moore: Poisonous Snakes of the World, 1980, p127)

Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.

Derivatives of phosphatidic acid in which the hydrophobic regions are composed of two fatty acids and a polar alcohol is joined to the C-3 position of glycerol through a phosphodiester bond. They are named according to their polar head groups, such as phosphatidylcholine and phosphatidylethanolamine.

The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)

Isomeric forms and derivatives of butanol (C4H9OH).

Particles consisting of aggregates of molecules held loosely together by secondary bonds. The surface of micelles are usually comprised of amphiphatic compounds that are oriented in a way that minimizes the energy of interaction between the micelle and its environment. Liquids that contain large numbers of suspended micelles are referred to as EMULSIONS.

A phosphoinositide phospholipase C subtype that is primarily regulated by its association with HETEROTRIMERIC G-PROTEINS. It is structurally related to PHOSPHOLIPASE C DELTA with the addition of C-terminal extension of 400 residues.

Saturated indolizines that are fused six and five-membered rings with a nitrogen atom at the ring fusion. They are biosynthesized in PLANTS by cyclization of a LYSINE coupled to ACETYL COENZYME A. Many of them are naturally occurring ALKALOIDS.

Derivatives of PHOSPHATIDIC ACIDS that lack one of its fatty acyl chains due to its hydrolytic removal.

The most common etiologic agent of GAS GANGRENE. It is differentiable into several distinct types based on the distribution of twelve different toxins.

The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.

A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)

Cyclic hydrocarbons that contain multiple rings and share one or more atoms.

A class of compounds named after and generally derived from C20 fatty acids (EICOSANOIC ACIDS) that includes PROSTAGLANDINS; LEUKOTRIENES; THROMBOXANES, and HYDROXYEICOSATETRAENOIC ACIDS. They have hormone-like effects mediated by specialized receptors (RECEPTORS, EICOSANOID).

Compounds containing carbohydrate or glycosyl groups linked to phosphatidylinositols. They anchor GPI-LINKED PROTEINS or polysaccharides to cell membranes.

A four carbon linear hydrocarbon that has a hydroxy group at position 1.

Poisonous animal secretions forming fluid mixtures of many different enzymes, toxins, and other substances. These substances are produced in specialized glands and secreted through specialized delivery systems (nematocysts, spines, fangs, etc.) for disabling prey or predator.

A nitrogen-free class of lipids present in animal and particularly plant tissues and composed of one mole of glycerol and 1 or 2 moles of phosphatidic acid. Members of this group differ from one another in the nature of the fatty acids released on hydrolysis.

The use of fluorescence spectrometry to obtain quantitative results for the FLUORESCENT ANTIBODY TECHNIQUE. One advantage over the other methods (e.g., radioimmunoassay) is its extreme sensitivity, with a detection limit on the order of tenths of microgram/liter.

Antibiotic complex produced by Streptomyces fradiae. It is composed of neomycins A, B, and C. It acts by inhibiting translation during protein synthesis.

A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. EC 3.1.4.

Indolizines are organic compounds that consist of a condensed pyridine and pyrrole ring structure, which can be found in certain natural and synthetic substances, and have been studied for their potential biological activities.

Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).

A group of GLYCOLIPIDS in which the sugar group is GALACTOSE. They are distinguished from GLYCOSPHINGOLIPIDS in lacking nitrogen. They constitute the majority of MEMBRANE LIPIDS in PLANTS.

Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.

GLYCEROPHOSPHOLIPIDS in which one of the two acyl chains is attached to glycerol with an ether alkenyl linkage instead of an ester as with the other glycerophospholipids.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.

A basic constituent of lecithin that is found in many plants and animal organs. It is important as a precursor of acetylcholine, as a methyl donor in various metabolic processes, and in lipid metabolism.

Purifying or cleansing agents, usually salts of long-chain aliphatic bases or acids, that exert cleansing (oil-dissolving) and antimicrobial effects through a surface action that depends on possessing both hydrophilic and hydrophobic properties.

A chelating agent that sequesters a variety of polyvalent cations such as CALCIUM. It is used in pharmaceutical manufacturing and as a food additive.

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

Physiological processes in biosynthesis (anabolism) and degradation (catabolism) of LIPIDS.

Acetophenones are organic compounds that contain a ketone functional group (carbonyl, >C=O) attached to a phenyl ring, making them a subclass of aromatic ketones with the general formula C6H5COCH3.

Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.

The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.

A species of gram-positive, rod-shaped bacteria widely distributed in nature. It has been isolated from sewage, soil, silage, and from feces of healthy animals and man. Infection with this bacterium leads to encephalitis, meningitis, endocarditis, and abortion.

The destruction of ERYTHROCYTES by many different causal agents such as antibodies, bacteria, chemicals, temperature, and changes in tonicity.

Toxic substances from microorganisms, plants or animals that interfere with the functions of the nervous system. Most venoms contain neurotoxic substances. Myotoxins are included in this concept.

Two-ring crystalline hydrocarbons isolated from coal tar. They are used as intermediates in chemical synthesis, as insect repellents, fungicides, lubricants, preservatives, and, formerly, as topical antiseptics.

Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)

An ionophorous, polyether antibiotic from Streptomyces chartreusensis. It binds and transports CALCIUM and other divalent cations across membranes and uncouples oxidative phosphorylation while inhibiting ATPase of rat liver mitochondria. The substance is used mostly as a biochemical tool to study the role of divalent cations in various biological systems.

A lipoprotein-associated PHOSPHOLIPASE A2 which modulates the action of PLATELET ACTIVATING FACTOR by hydrolyzing the SN-2 ester bond to yield the biologically inactive lyso-platelet-activating factor. It has specificity for phospholipid substrates with short-chain residues at the SN-2 position, but inactive against long-chain phospholipids. Deficiency in this enzyme is associated with many diseases including ASTHMA, and HYPERCHOLESTEROLEMIA.

The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.

The degree of pathogenicity within a group or species of microorganisms or viruses as indicated by case fatality rates and/or the ability of the organism to invade the tissues of the host. The pathogenic capacity of an organism is determined by its VIRULENCE FACTORS.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

Chromatography on thin layers of adsorbents rather than in columns. The adsorbent can be alumina, silica gel, silicates, charcoals, or cellulose. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

Phosphoric acid esters of inositol. They include mono- and polyphosphoric acid esters, with the exception of inositol hexaphosphate which is PHYTIC ACID.

Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.

Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)

An enzyme that catalyzes the hydrolysis of sphingomyelin to ceramide (N-acylsphingosine) plus choline phosphate. A defect in this enzyme leads to NIEMANN-PICK DISEASE. EC 3.1.4.12.

A class of sphingolipids found largely in the brain and other nervous tissue. They contain phosphocholine or phosphoethanolamine as their polar head group so therefore are the only sphingolipids classified as PHOSPHOLIPIDS.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.

The sum of the weight of all the atoms in a molecule.

The principal cyclooxygenase metabolite of arachidonic acid. It is released upon activation of mast cells and is also synthesized by alveolar macrophages. Among its many biological actions, the most important are its bronchoconstrictor, platelet-activating-factor-inhibitory, and cytotoxic effects.

A kingdom of eukaryotic, heterotrophic organisms that live parasitically as saprobes, including MUSHROOMS; YEASTS; smuts, molds, etc. They reproduce either sexually or asexually, and have life cycles that range from simple to complex. Filamentous fungi, commonly known as molds, refer to those that grow as multicellular colonies.

Proteins prepared by recombinant DNA technology.

The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.

Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.

Nonionic surfactant mixtures varying in the number of repeating ethoxy (oxy-1,2-ethanediyl) groups. They are used as detergents, emulsifiers, wetting agents, defoaming agents, etc. Octoxynol-9, the compound with 9 repeating ethoxy groups, is a spermatocide.

Any compound containing one or more monosaccharide residues bound by a glycosidic linkage to a hydrophobic moiety such as an acylglycerol (see GLYCERIDES), a sphingoid, a ceramide (CERAMIDES) (N-acylsphingoid) or a prenyl phosphate. (From IUPAC's webpage)

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

Established cell cultures that have the potential to propagate indefinitely.

An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. It is produced by glands on the tongue and by the pancreas and initiates the digestion of dietary fats. (From Dorland, 27th ed) EC 3.1.1.3.

The addition of an organic acid radical into a molecule.

The most common and most biologically active of the mammalian prostaglandins. It exhibits most biological activities characteristic of prostaglandins and has been used extensively as an oxytocic agent. The compound also displays a protective effect on the intestinal mucosa.

Enzyme complexes that catalyze the formation of PROSTAGLANDINS from the appropriate unsaturated FATTY ACIDS, molecular OXYGEN, and a reduced acceptor.

Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a serine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and serine and 2 moles of fatty acids.

Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)

Induction of ectopic olfactory structures and bone morphogenetic protein inhibition by Rossy, a group XII secreted phospholipase A2. (1/94)

The secreted phospholipases A(2) (sPLA(2)s) comprise a family of small secreted proteins with the ability to catalyze the generation of bioactive lipids through glycophospholipid hydrolysis. Recently, a large number of receptor proteins and extracellular binding partners for the sPLA(2)s have been identified, suggesting that these secreted factors might exert a subset of their broad spectrum of biological activities independently of their enzymatic activity. Here, we describe an activity for the sPLA(2) group XII (sPLA(2)-gXII) gene during Xenopus laevis early development. In the ectoderm, sPLA(2)-gXII acts as a neural inducer by blocking bone morphogenetic protein (BMP) signaling. Gain of function in embryos leads to ectopic neurogenesis and to the specification of ectopic olfactory sensory structures, including olfactory bulb and sensory epithelia. This activity is conserved in the Drosophila melanogaster, Xenopus, and mammalian orthologs and appears to be independent of the lipid hydrolytic activity. Because of its effect on olfactory neurogenesis, we have renamed this gene Rossy, in homage to the Spanish actress Rossy de Palma. We present evidence that Rossy/sPLA(2)-gXII can inhibit the transcriptional activation of BMP direct-target gene reporters in Xenopus and mouse P19 embryonic carcinoma cells through the loss of DNA-binding activity of activated Smad1/4 complexes. Collectively, these data represent the first evidence for signaling cross talk between a secreted phospholipase A(2) and the BMP/transforming growth factor beta pathways and identify Rossy/sPLA(2)-gXII as the only factor thus far described which is sufficient to induce anterior sensory neural structures during vertebrate development. (+info)

Molecular basis of phospholipase A2 activity toward phospholipids with sn-1 substitutions. (2/94)

We studied secretory phospholipase A(2) type IIA (sPLA(2)) activity toward phospholipids that are derivatized in the sn-1 position of the glycerol backbone. We explored what type of side group (small versus bulky groups, hydrophobic versus polar groups) can be introduced at the sn-1 position of the glycerol backbone of glycerophospholipids and at the same time be hydrolyzed by sPLA(2). The biophysical characterization revealed that the modified phospholipids can form multilamellar vesicles, and several of the synthesized sn-1 functionalized phospholipids were hydrolyzed by sPLA(2). Molecular dynamics simulations provided detailed insight on an atomic level that can explain the observed sPLA(2) activity toward the different phospholipid analogs. The simulations revealed that, depending on the nature of the side chain located at the sn-1 position, the group may interfere with an incoming water molecule that acts as the nucleophile in the enzymatic reaction. The simulation results are in agreement with the experimentally observed sPLA(2) activity toward the different phospholipid analogs. (+info)

Secreted phospholipase A2 group X overexpression in asthma and bronchial hyperresponsiveness. (3/94)

RATIONALE: Secreted phospholipase A(2) enzymes (sPLA(2)s) play key regulatory roles in the biosynthesis of eicosanoids, such as the cysteinyl leukotrienes, but the role of these enzymes in the pathogenesis of asthma is not known. OBJECTIVES: To establish if sPLA(2)s are overexpressed in the airways of patients with asthma, and to determine if these enzymes may play a role in the generation of eicosanoids in exercise-induced bronchoconstriction. METHODS: Induced sputum samples were obtained from subjects with asthma with exercise-induced bronchoconstriction and nonasthmatic control subjects at baseline, and on a separate day 30 minutes after exercise challenge. The expression of the PLA(2)s in induced sputum cells and supernatant was determined by quantitative polymerase chain reaction, immunocytochemistry, and Western blot. MEASUREMENTS AND MAIN RESULTS: The sPLA(2)s expressed at the highest levels in airway cells of subjects with asthma were groups X and XIIA. Group X sPLA(2) (sPLA(2)-X) was differentially overexpressed in asthma and localized to airway epithelial cells and bronchial macrophages. The gene expression, immunostaining in airway epithelial cells and bronchial macrophages, and the level of the extracellular sPLA(2)-X protein in the airways increased in response to exercise challenge in the asthma group, whereas the levels were lower and unchanged after challenge in nonasthmatic control subjects. CONCLUSIONS: Increased expression of sPLA(2)-X may play a key role in the dysregulated eicosanoid synthesis in asthma. (+info)

Liquid-liquid immiscibility in model membranes activates secretory phospholipase A2. (4/94)

Secretory phospholipase A2 (sPLA2) hydrolyzes phosphatidylcholines (PC) within lipid bilayers to produce lyso-PC and a fatty acid, which can act as signaling molecule in biological membranes. The activity of sPLA2 depends on the membrane structure. Bilayer defects, curvature, and gel-fluid micro-heterogeneity are known to activate sPLA2. Here, we investigate if liquid-liquid immiscibility within model membranes is sufficient for sPLA2 activation. The onset of the hydrolytic activity of cobra-venom sPLA2 towards mixed monolayers of dimyristoyl-PC (DMPC)/cholesterol 2:1 (mol/mol) has been determined using infrared reflection-absorption spectroscopy (IRRAS) and polarization-modulated (PM-) IRRAS. The lag phase of sPLA2 activity increases exponentially with rising surface pressures starting at 12 mN/m. This indicates that enzyme activation is hampered at higher surface pressures. Below 12 mN/m, no lag phase is observed, and sPLA2 is efficiently activated. The surface pressure that is critical for sPLA2 activation correlates with the critical miscibility pressure according to the phase diagram of DMPC and cholesterol. Thus, coexisting, liquid-phase domains provide sufficient boundaries to activate sPLA2. Moreover, liquid-liquid immiscibility is an activating mechanism for sPLA2 that also applies to biological membranes under physiological conditions because the corresponding bilayer structure is associated with that of membrane rafts. (+info)

Jak2 dampens the induction by IL-1beta of prostaglandin endoperoxide H synthase 2 expression in human orbital fibroblasts: evidence for divergent influence on the prostaglandin E2 biosynthetic pathway. (5/94)

Prostaglandin endoperoxide H synthase 2 (PGHS-2) catalyzes the rate-limiting steps in the synthesis of PGE(2). It is substantially but transiently induced in human orbital fibroblasts treated with IL-1beta. In this study, we report that the induction of PGHS-2 by IL-1beta is dramatically enhanced and prolonged when Jak2 signaling is abrogated, either with the specific inhibitor AG490 or by transiently transfecting fibroblasts with a dominant negative mutant Jak2. Attenuating Jak2 increases PGHS-2 steady-state mRNA levels, a consequence of increased gene transcription and mRNA survival in IL-1beta-treated cultures. Surprisingly, interrupting Jak2 function also blocked the expected increase in PGE(2) synthesis usually provoked by IL-1beta. This resulted from the rapid loss of IL-1beta-dependent arachidonate release and by attenuation of group IIA secreted PLA(2) (sPLA(2)) gene induction. Supplying Jak2-compromised cultures with exogenous arachidonate failed to increase PGE(2) production in response to IL-1beta until cells were mechanically disrupted. However, transiently transfecting them with wild-type sPLA(2) fully restored prostanoid production to anticipated levels. sPLA(2) expression following transfection resulted in increased IL-1beta-dependent PGHS-2 and microsomal PGE(2) synthase levels. Thus, sPLA(2) plays important roles in PGE(2) synthesis in addition to its release of arachidonate. Our findings suggest that Jak2 ordinarily dampens and limits the duration of the PGHS-2 induction by IL-1beta. Moreover, it is required for IL-1beta-dependent signaling to sPLA(2), the expression and activity of which are necessary for up-regulating PGE(2) synthesis in orbital fibroblasts. (+info)

Honeybee venom secretory phospholipase A2 induces leukotriene production but not histamine release from human basophils. (6/94)

The role of basophils in an anaphylactic response is well recognized but is usually masked by mast cells, which contain similar mediators for the induction of generalized vasodilatation and laryngeal constriction. The rapid onset of systemic anaphylactic symptoms, particularly in insect stings and ingested food, suggest that basophils, a circulating pool of cells containing histamine and other potent mediators such as leukotrienes, may be more involved in systemic anaphylaxis than originally thought. We wished to examine if secretory phospholipase A2, a systemic allergen found in honey bee venom (HBV-sPLA2) may activate basophils directly leading to rapid systemic mediator release. Basophils were isolated from human blood and stimulated with increasing concentrations of HBV-sPLA2. We found that physiological concentrations of HBV-sPLA2 induce rapid leukotriene C4 production from purified human basophils within 5 min, while interleukin (IL)-4 expression and production was induced at later time-points. Histamine release was not induced, signifying that HBV-sPLA2 did not induce generalized degranulation. Surface expression of CD63, CD69 and CD11b were up-regulated following HBV-sPLA2 treatment. Stimulation of basophils with anti-immunoglobulin E (IgE) following treatment with HBV-sPLA2 did not induce more leukotriene release. To investigate the mechanism of leukotriene production, 9-12 octadecadiynioc acid, a cyclooxygenase-1 (COX-1) and 15-lipoxygenase inhibitor, was used and this abrogated leukotriene production. These results indicate that HBV-sPLA2 can directly activate human basophils in vitro to induce leukotriene production. (+info)

Antibacterial actions of secreted phospholipases A2. Review. (7/94)

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Effects of cholesterol on physical properties of human erythrocyte membranes: impact on susceptibility to hydrolysis by secretory phospholipase A2. (8/94)

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Phospholipases are a group of enzymes that catalyze the hydrolysis of phospholipids, which are major components of cell membranes. Phospholipases cleave specific ester bonds in phospholipids, releasing free fatty acids and other lipophilic molecules. Based on the site of action, phospholipases are classified into four types:

1. Phospholipase A1 (PLA1): This enzyme hydrolyzes the ester bond at the sn-1 position of a glycerophospholipid, releasing a free fatty acid and a lysophospholipid.
2. Phospholipase A2 (PLA2): PLA2 cleaves the ester bond at the sn-2 position of a glycerophospholipid, releasing a free fatty acid (often arachidonic acid) and a lysophospholipid. Arachidonic acid is a precursor for eicosanoids, which are signaling molecules involved in inflammation and other physiological processes.
3. Phospholipase C (PLC): PLC hydrolyzes the phosphodiester bond in the headgroup of a glycerophospholipid, releasing diacylglycerol (DAG) and a soluble head group, such as inositol trisphosphate (IP3). DAG acts as a secondary messenger in intracellular signaling pathways, while IP3 mediates the release of calcium ions from intracellular stores.
4. Phospholipase D (PLD): PLD cleaves the phosphoester bond between the headgroup and the glycerol moiety of a glycerophospholipid, releasing phosphatidic acid (PA) and a free head group. PA is an important signaling molecule involved in various cellular processes, including membrane trafficking, cytoskeletal reorganization, and cell survival.

Phospholipases have diverse roles in normal physiology and pathophysiological conditions, such as inflammation, immunity, and neurotransmission. Dysregulation of phospholipase activity can contribute to the development of various diseases, including cancer, cardiovascular disease, and neurological disorders.

Phospholipases A are a group of enzymes that hydrolyze phospholipids into fatty acids and lysophospholipids by cleaving the ester bond at the sn-1 or sn-2 position of the glycerol backbone. There are three main types of Phospholipases A:

* Phospholipase A1 (PLA1): This enzyme specifically hydrolyzes the ester bond at the sn-1 position, releasing a free fatty acid and a lysophospholipid.
* Phospholipase A2 (PLA2): This enzyme specifically hydrolyzes the ester bond at the sn-2 position, releasing a free fatty acid (often arachidonic acid, which is a precursor for eicosanoids) and a lysophospholipid.
* Phospholipase A/B (PLA/B): This enzyme has both PLA1 and PLA2 activity and can hydrolyze the ester bond at either the sn-1 or sn-2 position.

Phospholipases A play important roles in various biological processes, including cell signaling, membrane remodeling, and host defense. They are also involved in several diseases, such as atherosclerosis, neurodegenerative disorders, and cancer.

Phospholipase A2 (PLA2) is a type of enzyme that catalyzes the hydrolysis of the sn-2 ester bond in glycerophospholipids, releasing free fatty acids, such as arachidonic acid, and lysophospholipids. These products are important precursors for the biosynthesis of various signaling molecules, including eicosanoids, platelet-activating factor (PAF), and lipoxins, which play crucial roles in inflammation, immunity, and other cellular processes.

Phospholipases A2 are classified into several groups based on their structure, mechanism of action, and cellular localization. The secreted PLA2s (sPLA2s) are found in extracellular fluids and are characterized by a low molecular weight, while the calcium-dependent cytosolic PLA2s (cPLA2s) are larger proteins that reside within cells.

Abnormal regulation or activity of Phospholipase A2 has been implicated in various pathological conditions, such as inflammation, neurodegenerative diseases, and cancer. Therefore, understanding the biology and function of these enzymes is essential for developing novel therapeutic strategies to target these disorders.

Phospholipase A1 (PLA1) is an enzyme that catalyzes the hydrolysis of the ester bond at the sn-1 position of glycerophospholipids, resulting in the production of free fatty acids and lysophospholipids. This enzyme plays a crucial role in various biological processes, including cell signaling, membrane remodeling, and inflammation. PLA1 is widely distributed in nature and can be found in different organisms, such as bacteria, plants, and animals. In humans, PLA1 is involved in several physiological and pathological conditions, including lipid metabolism, atherosclerosis, neurodegenerative diseases, and cancer.

Group II Phospholipases A2 (PLA2) are a class of enzymes that hydrolyze the sn-2 ester bond of glycerophospholipids to release free fatty acids and lysophospholipids. They are classified as one of the several groups of PLA2 based on their structure, function, and calcium dependence.

Group II PLA2s are secreted enzymes that require millimolar concentrations of calcium ions for their activity. They consist of a single polypeptide chain with a molecular weight ranging from 14 to 18 kDa. These enzymes play important roles in various biological processes, including inflammation, host defense, and lipid metabolism. Dysregulation of Group II PLA2 activity has been implicated in several pathological conditions, such as atherosclerosis, arthritis, and neurodegenerative diseases.

Type C phospholipases, also known as group CIA phospholipases or patatin-like phospholipase domain containing proteins (PNPLAs), are a subclass of phospholipases that specifically hydrolyze the sn-2 ester bond of glycerophospholipids. They belong to the PNPLA family, which includes nine members (PNPLA1-9) with diverse functions in lipid metabolism and cell signaling.

Type C phospholipases contain a patatin domain, which is a conserved region of approximately 240 amino acids that exhibits lipase and acyltransferase activities. These enzymes are primarily involved in the regulation of triglyceride metabolism, membrane remodeling, and cell signaling pathways.

PNPLA1 (adiponutrin) is mainly expressed in the liver and adipose tissue, where it plays a role in lipid droplet homeostasis and triglyceride hydrolysis. PNPLA2 (ATGL or desnutrin) is a key regulator of triglyceride metabolism, responsible for the initial step of triacylglycerol hydrolysis in adipose tissue and other tissues.

PNPLA3 (calcium-independent phospholipase A2 epsilon or iPLA2ε) is involved in membrane remodeling, arachidonic acid release, and cell signaling pathways. Mutations in PNPLA3 have been associated with an increased risk of developing nonalcoholic fatty liver disease (NAFLD), alcoholic liver disease, and hepatic steatosis.

PNPLA4 (lipase maturation factor 1 or LMF1) is involved in the intracellular processing and trafficking of lipases, such as pancreatic lipase and hepatic lipase. PNPLA5 ( Mozart1 or GSPML) has been implicated in membrane trafficking and cell signaling pathways.

PNPLA6 (neuropathy target esterase or NTE) is primarily expressed in the brain, where it plays a role in maintaining neuronal integrity by regulating lipid metabolism. Mutations in PNPLA6 have been associated with neuropathy and cognitive impairment.

PNPLA7 (adiponutrin or ADPN) has been implicated in lipid droplet formation, triacylglycerol hydrolysis, and cell signaling pathways. Mutations in PNPLA7 have been associated with an increased risk of developing NAFLD and hepatic steatosis.

PNPLA8 (diglyceride lipase or DGLα) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA9 (calcium-independent phospholipase A2 gamma or iPLA2γ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA10 (calcium-independent phospholipase A2 delta or iPLA2δ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA11 (calcium-independent phospholipase A2 epsilon or iPLA2ε) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA12 (calcium-independent phospholipase A2 zeta or iPLA2ζ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA13 (calcium-independent phospholipase A2 eta or iPLA2η) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA14 (calcium-independent phospholipase A2 theta or iPLA2θ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA15 (calcium-independent phospholipase A2 iota or iPLA2ι) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA16 (calcium-independent phospholipase A2 kappa or iPLA2κ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA17 (calcium-independent phospholipase A2 lambda or iPLA2λ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA18 (calcium-independent phospholipase A2 mu or iPLA2μ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA19 (calcium-independent phospholipase A2 nu or iPLA2ν) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA20 (calcium-independent phospholipase A2 xi or iPLA2ξ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA21 (calcium-independent phospholipase A2 omicron or iPLA2ο) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA22 (calcium-independent phospholipase A2 pi or iPLA2π) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA23 (calcium-independent phospholipase A2 rho or iPLA2ρ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA24 (calcium-independent phospholipase A2 sigma or iPLA2σ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA25 (calcium-independent phospholipase A2 tau or iPLA2τ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA26 (calcium-independent phospholipase A2 upsilon or iPLA2υ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA27 (calcium-independent phospholipase A2 phi or iPLA2φ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA28 (calcium-independent phospholipase A2 chi or iPLA2χ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA29 (calcium-independent phospholipase A2 psi or iPLA2ψ) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA30 (calcium-independent phospholipase A2 omega or iPLA2ω) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA31 (calcium-independent phospholipase A2 pi or iPLA2π) has been implicated in membrane remodeling, arachidonic acid release, and cell signaling pathways.

PNPLA32 (calcium-independent phospholipase A2 rho or iPLA2ρ) is involved in the regulation of intracellular triacylglycerol metabolism, particularly in adipocytes and muscle cells. PNPLA33 (calcium-independent phospholipase A2 sigma or iPLA2σ) has been implicated in membrane remodeling, ar

Group X Phospholipases A2 (PLA2) are a group of enzymes that belong to the larger family of PLA2 enzymes, which are responsible for hydrolyzing the sn-2 ester bond of glycerophospholipids to release free fatty acids and lysophospholipids. Specifically, Group X PLA2 enzymes selectively hydrolyze arachidonic acid, a polyunsaturated fatty acid that is a precursor for eicosanoids, which are signaling molecules involved in inflammation and other physiological processes.

Group X PLA2 enzymes are secreted by various cells, including immune cells, and play important roles in host defense, inflammation, and lipid metabolism. Dysregulation of Group X PLA2 activity has been implicated in several diseases, such as atherosclerosis, arthritis, and neurodegenerative disorders. Therefore, understanding the function and regulation of these enzymes is crucial for developing new therapeutic strategies to treat these conditions.

Phospholipases A2, Secretory (sPLA2s) are a group of enzymes that hydrolyze the sn-2 ester bond of glycerophospholipids to release free fatty acids and lysophospholipids. They are called "secretory" because they are secreted by various cells, such as inflammatory cells, pancreatic acinar cells, and epididymal cells, into the extracellular space or biological fluids.

sPLA2s are small enzymes with a molecular weight of approximately 14-18 kDa and contain a highly conserved calcium-binding site that is essential for their catalytic activity. They play important roles in various physiological and pathophysiological processes, including inflammation, host defense, lipid metabolism, and cell signaling.

Inflammation is one of the main biological functions of sPLA2s. They are rapidly released from activated immune cells, such as macrophages and neutrophils, in response to various stimuli, including bacterial products, cytokines, and oxidative stress. Once secreted, sPLA2s can induce the production of pro-inflammatory mediators, such as eicosanoids and platelet-activating factor (PAF), which contribute to the amplification and perpetuation of the inflammatory response.

Dysregulation of sPLA2 activity has been implicated in various pathological conditions, including atherosclerosis, acute pancreatitis, sepsis, neurodegenerative diseases, and cancer. Therefore, sPLA2s are considered potential therapeutic targets for the treatment of these disorders.

Group I Phospholipases A2 (PLA2) are a group of enzymes that hydrolyze the sn-2 ester bond of glycerophospholipids to release free fatty acids and lysophospholipids. They are characterized by a low molecular weight, calcium-dependent enzymes, and a highly conserved catalytic site.

Group I PLA2s are further divided into subgroups based on their structure and function. The secreted PLA2s (sPLA2) are found in subgroup IB, which includes 10 human isoforms (sPLA2-IB to sPLA2-IN). These enzymes are produced by various cells, such as pancreas, macrophages and neutrophils, and are secreted into the extracellular space. They play a role in inflammation, host defense, and lipid metabolism.

The intracellular PLA2s (iPLA2) are found in subgroup IC, which includes 3 human isoforms (iPLA2-IC to iPLA2-IE). These enzymes are located in the cytosol and are involved in various cellular processes such as membrane remodeling, signal transduction, and apoptosis.

It's important to note that abnormal regulation of PLA2 activity has been implicated in several diseases, including atherosclerosis, arthritis, neurodegenerative disorders, and cancer.

Lysophospholipase is an enzyme that catalyzes the hydrolysis of a single fatty acid from lysophospholipids, producing a glycerophosphocholine and free fatty acid. This enzyme plays a role in the metabolism of lipids and membrane homeostasis. There are several types of lysophospholipases that differ based on their specificity for the head group of the lysophospholipid substrate, such as lysophosphatidylcholine-specific phospholipase or lysophospholipase 1 (LPLA1), and lysophosphatidic acid-specific phospholipase D or autotaxin (ATX).

Deficiency or mutations in lysophospholipases can lead to various diseases, such as LPI (lysophosphatidylinositol lipidosis) caused by a deficiency of the lysophospholipase superfamily member called Ptdlns-specific phospholipase C (PLC).

Note: This definition is for general information purposes only and may not include all the latest findings or medical terminologies. For accurate and comprehensive understanding, it's recommended to consult authoritative medical textbooks or resources.

Group V Phospholipases A2 (Group V PLA2s) are a subclass of the phospholipase A2 enzymes, which are a group of enzymes that hydrolyze the sn-2 ester bond of glycerophospholipids to release free fatty acids and lysophospholipids. Specifically, Group V PLA2s are calcium-dependent cytosolic enzymes that play a role in inflammation, immunity, and cell signaling processes.

Group V PLA2s consist of three isoforms (Group VA,VB,VC) which are expressed in various tissues including the brain, lungs, and reproductive organs. They have been implicated in several pathological conditions such as atherosclerosis, acute respiratory distress syndrome (ARDS), and cancer.

In addition to their enzymatic activity, Group V PLA2s also have non-enzymatic functions, including acting as chaperone proteins, regulating gene expression, and modulating the activity of other signaling molecules. Further research is needed to fully understand the complex roles and mechanisms of Group V PLA2s in health and disease.

Snake venoms are complex mixtures of bioactive compounds produced by specialized glands in snakes. They primarily consist of proteins and peptides, including enzymes, neurotoxins, hemotoxins, cytotoxins, and cardiotoxins. These toxins can cause a variety of pharmacological effects on the victim's body, such as disruption of the nervous system, blood coagulation, muscle function, and cell membrane integrity, ultimately leading to tissue damage and potentially death. The composition of snake venoms varies widely among different species, making each species' venom unique in its toxicity profile.

Phospholipase D is an enzyme that catalyzes the hydrolysis of phosphatidylcholine and other glycerophospholipids to produce phosphatidic acid and a corresponding alcohol. This reaction plays a crucial role in various cellular processes, including signal transduction, membrane trafficking, and lipid metabolism. There are several isoforms of Phospholipase D identified in different tissues and organisms, each with distinct regulatory mechanisms and functions. The enzyme's activity can be modulated by various factors such as calcium ions, protein kinases, and G proteins, making it a critical component in the regulation of cellular homeostasis.

Crotalid venoms are the toxic secretions produced by the members of the Crotalinae subfamily, also known as pit vipers. This group includes rattlesnakes, cottonmouths (or water moccasins), and copperheads, which are native to the Americas, as well as Old World vipers found in Asia and Europe, such as gaboon vipers and saw-scaled vipers.

Crotalid venoms are complex mixtures of various bioactive molecules, including enzymes, proteins, peptides, and other low molecular weight components. They typically contain a variety of pharmacologically active components, such as hemotoxic and neurotoxic agents, which can cause extensive local tissue damage, coagulopathy, cardiovascular dysfunction, and neuromuscular disorders in the victim.

The composition of crotalid venoms can vary significantly between different species and even among individual specimens within the same species. This variability is influenced by factors such as geographic location, age, sex, diet, and environmental conditions. As a result, the clinical manifestations of crotalid envenomation can be highly variable, ranging from mild local reactions to severe systemic effects that may require intensive medical treatment and supportive care.

Crotalid venoms have been the subject of extensive research in recent years due to their potential therapeutic applications. For example, certain components of crotalid venoms have shown promise as drugs for treating various medical conditions, such as cardiovascular diseases, pain, and inflammation. However, further studies are needed to fully understand the mechanisms of action of these venom components and to develop safe and effective therapies based on them.

Phospholipase A2 (PLA2) receptors are a group of proteins that are involved in the signaling pathways related to inflammation and immune response. PLA2 is an enzyme that cleaves phospholipids in cell membranes to produce arachidonic acid, which is a precursor for various eicosanoids, such as prostaglandins, leukotrienes, and thromboxanes, that play crucial roles in the inflammatory response.

There are two main types of PLA2 receptors: secreted PLA2 (sPLA2) receptors and intracellular PLA2 (iPLA2) receptors. The sPLA2 receptors are found on the cell surface and mediate the binding and internalization of sPLA2 enzymes, which are released from activated immune cells during inflammation. The iPLA2 receptors, on the other hand, are located inside the cell and regulate the intracellular levels of arachidonic acid and other lipid mediators.

Abnormal activation or regulation of PLA2 receptors has been implicated in various pathological conditions, including inflammatory diseases, neurodegenerative disorders, and cancer. Therefore, understanding the structure, function, and regulation of these receptors is important for developing new therapeutic strategies to target these diseases.

Group VI Phospholipases A2 (PLA2) are a subclass of the PLA2 family, which are enzymes that hydrolyze the sn-2 ester bond of glycerophospholipids to release free fatty acids and lysophospholipids. Specifically, Group VI PLA2s are calcium-dependent enzymes that have been identified in various tissues, including the brain and testis. They play important roles in several biological processes, such as cell signaling, inflammation, and lipid metabolism.

Group VI PLA2s are further divided into two subgroups: Group VI A and Group VI B. The Group VI A subgroup includes the iPLA2-VIA (also known as PLA2G6) enzyme, which has been implicated in several neurological disorders, such as neurodegenerative diseases and hereditary spastic paraplegia. On the other hand, the Group VI B subgroup includes the pancreatic-type PLA2 (also known as PLA2G1B) enzyme, which is primarily involved in digestion.

It's worth noting that while Group VI PLA2s have important physiological functions, they can also contribute to pathological conditions when their activity is dysregulated. For example, excessive activation of these enzymes has been linked to the development and progression of various inflammatory diseases, such as atherosclerosis, arthritis, and asthma.

Cobra venoms are a type of snake venom that is produced by cobras, which are members of the genus Naja in the family Elapidae. These venoms are complex mixtures of proteins and other molecules that have evolved to help the snake immobilize and digest its prey.

Cobra venoms typically contain a variety of toxic components, including neurotoxins, hemotoxins, and cytotoxins. Neurotoxins target the nervous system and can cause paralysis and respiratory failure. Hemotoxins damage blood vessels and tissues, leading to internal bleeding and organ damage. Cytotoxins destroy cells and can cause tissue necrosis.

The specific composition of cobra venoms can vary widely between different species of cobras, as well as between individual snakes of the same species. Some cobras have venoms that are primarily neurotoxic, while others have venoms that are more hemotoxic or cytotoxic. The potency and effects of cobra venoms can also be influenced by factors such as the age and size of the snake, as well as the temperature and pH of the environment.

Cobra bites can be extremely dangerous and even fatal to humans, depending on the species of cobra, the amount of venom injected, and the location of the bite. Immediate medical attention is required in the event of a cobra bite, including the administration of antivenom therapy to neutralize the effects of the venom.

Group IV Phospholipases A2 (PLA2) are a subclass of the PLA2 family, which are enzymes that hydrolyze the sn-2 acyl bond of glycerophospholipids to release free fatty acids and lysophospholipids. Specifically, Group IV PLA2s are calcium-dependent enzymes that are primarily located in the cytoplasm of cells and are involved in various cellular processes such as membrane remodeling, signal transduction, and inflammation.

Group IV PLA2s can be further divided into several subgroups, including Group IVA (also known as cPLA2s) and Group IVB (also known as iPLA2s). These enzymes have distinct structural features and play different roles in cellular physiology. For example, cPLA2s are involved in the production of eicosanoids, which are signaling molecules that mediate inflammation and other responses to injury or infection. On the other hand, iPLA2s are involved in maintaining membrane homeostasis and regulating cellular energy metabolism.

Abnormal regulation of Group IV PLA2 activity has been implicated in various pathological conditions, including cancer, neurodegenerative diseases, and cardiovascular disease. Therefore, understanding the function and regulation of these enzymes is an important area of research with potential therapeutic implications.

Viperidae is not a term that has a medical definition per se, but it is a term used in the field of biology and zoology. Viperidae is the family name for a group of venomous snakes commonly known as vipers. This family includes various types of pit vipers, adders, and rattlesnakes.

While Viperidae itself may not have direct medical relevance, understanding the biology and behavior of these creatures is important in the context of medical fields such as toxicology and emergency medicine. Knowledge about the venomous properties of viper snakes and their potential to cause harm to humans is crucial for appropriate treatment and management of snakebites.

"Bothrops" is a genus of venomous snakes commonly known as lancehead vipers, found primarily in Central and South America. The name "Bothrops" comes from the Greek words "bothros," meaning pit, and "ops," meaning face, referring to the deep pits on the sides of their heads that help them detect heat and locate prey. These snakes are known for their aggressive behavior and potent venom, which can cause severe pain, swelling, tissue damage, and potentially life-threatening systemic effects if left untreated.

The genus "Bothrops" includes over 30 species of pit vipers, many of which are considered medically important due to their ability to inflict serious envenomations in humans. Some notable examples include Bothrops asper (the terciopelo or fer-de-lance), Bothrops atrox (the common lancehead), and Bothrops jararaca (the jararaca).

If you encounter a snake of this genus, it is essential to seek medical attention immediately if bitten, as the venom can cause significant harm if not treated promptly.

I'm sorry for any confusion, but the term "Reptilian Proteins" does not have a specific or established medical or scientific meaning. The term "reptilian" generally refers to characteristics of reptiles, and proteins are complex molecules that perform various functions within all living organisms, including reptiles. However, there isn't a recognized category or classification called "Reptilian Proteins" in the field of medicine or biology. If you have any questions about specific reptile-related proteins or reptile physiology, I would be happy to try and help with those!

Phospholipids are a major class of lipids that consist of a hydrophilic (water-attracting) head and two hydrophobic (water-repelling) tails. The head is composed of a phosphate group, which is often bound to an organic molecule such as choline, ethanolamine, serine or inositol. The tails are made up of two fatty acid chains.

Phospholipids are a key component of cell membranes and play a crucial role in maintaining the structural integrity and function of the cell. They form a lipid bilayer, with the hydrophilic heads facing outwards and the hydrophobic tails facing inwards, creating a barrier that separates the interior of the cell from the outside environment.

Phospholipids are also involved in various cellular processes such as signal transduction, intracellular trafficking, and protein function regulation. Additionally, they serve as emulsifiers in the digestive system, helping to break down fats in the diet.

"Viper venoms" refer to the toxic secretions produced by members of the Viperidae family of snakes, which include pit vipers (such as rattlesnakes, copperheads, and cottonmouths) and true vipers (like adders, vipers, and gaboon vipers). These venoms are complex mixtures of proteins, enzymes, and other bioactive molecules that can cause a wide range of symptoms in prey or predators, including local tissue damage, pain, swelling, bleeding, and potentially life-threatening systemic effects such as coagulopathy, cardiovascular shock, and respiratory failure.

The composition of viper venoms varies widely between different species and even among individuals within the same species. However, many viper venoms contain a variety of enzymes (such as phospholipases A2, metalloproteinases, and serine proteases) that can cause tissue damage and disrupt vital physiological processes in the victim. Additionally, some viper venoms contain neurotoxins that can affect the nervous system and cause paralysis or other neurological symptoms.

Understanding the composition and mechanisms of action of viper venoms is important for developing effective treatments for venomous snakebites, as well as for gaining insights into the evolution and ecology of these fascinating and diverse creatures.

Crotoxin is a type of protein toxin found in the venom of the South American rattlesnake, Crotalus durissus terrificus. It is a heterodimeric presynaptic neurotoxin composed of two subunits, an acidic subunit (CA) and a basic subunit (CB), which work together to inhibit the release of neurotransmitters from nerve endings. Crotoxin has been extensively studied for its potential therapeutic applications in various medical conditions, including inflammation, pain, and cancer. However, it is also highly toxic and can cause serious harm if ingested or introduced into the body through a snake bite.

Group III Phospholipases A2 (PLA2) are a subclass of the PLA2 family, which are enzymes that hydrolyze the sn-2 ester bond of glycerophospholipids to release free fatty acids and lysophospholipids. Specifically, Group III PLA2s are secreted enzymes that require calcium ions for their activity and are further divided into subgroups based on their structure and function. They play important roles in various biological processes, including inflammation, host defense, and lipid metabolism.

Group III PLA2s have been implicated in several pathological conditions, such as atherosclerosis, arthritis, and neurodegenerative diseases. Therefore, they are considered potential therapeutic targets for these disorders. However, further research is needed to fully understand their functions and regulatory mechanisms.

Elapid venoms are the toxic secretions produced by elapid snakes, a family of venomous snakes that includes cobras, mambas, kraits, and coral snakes. These venoms are primarily composed of neurotoxins, which can cause paralysis and respiratory failure in prey or predators.

Elapid venoms work by targeting the nervous system, disrupting communication between the brain and muscles. This results in muscle weakness, paralysis, and eventually respiratory failure if left untreated. Some elapid venoms also contain hemotoxins, which can cause tissue damage, bleeding, and other systemic effects.

The severity of envenomation by an elapid snake depends on several factors, including the species of snake, the amount of venom injected, the location of the bite, and the size and health of the victim. Prompt medical treatment is essential in cases of elapid envenomation, as the effects of the venom can progress rapidly and lead to serious complications or death if left untreated.

Phosphatidylcholines (PtdCho) are a type of phospholipids that are essential components of cell membranes in living organisms. They are composed of a hydrophilic head group, which contains a choline moiety, and two hydrophobic fatty acid chains. Phosphatidylcholines are crucial for maintaining the structural integrity and function of cell membranes, and they also serve as important precursors for the synthesis of signaling molecules such as acetylcholine. They can be found in various tissues and biological fluids, including blood, and are abundant in foods such as soybeans, eggs, and meat. Phosphatidylcholines have been studied for their potential health benefits, including their role in maintaining healthy lipid metabolism and reducing the risk of cardiovascular disease.

Elapidae is a family of venomous snakes, also known as elapids. This family includes many well-known species such as cobras, mambas, death adders, and sea snakes. Elapids are characterized by their fixed fangs, which are located at the front of the upper jaw and deliver venom through a hollow canal. The venom of these snakes is typically neurotoxic, causing paralysis and respiratory failure in prey or attackers.

Elapids are found throughout the world, with the greatest diversity occurring in tropical regions. They vary widely in size, from small species like the death adders that measure only a few inches long, to large species like the king cobra, which can reach lengths of up to 18 feet (5.5 meters).

Elapids are generally shy and avoid confrontations with humans whenever possible. However, they will defend themselves aggressively if threatened or cornered. Bites from elapid snakes can be medically significant and may require antivenom treatment.

Arachidonic acid is a type of polyunsaturated fatty acid that is found naturally in the body and in certain foods. It is an essential fatty acid, meaning that it cannot be produced by the human body and must be obtained through the diet. Arachidonic acid is a key component of cell membranes and plays a role in various physiological processes, including inflammation and blood clotting.

In the body, arachidonic acid is released from cell membranes in response to various stimuli, such as injury or infection. Once released, it can be converted into a variety of bioactive compounds, including prostaglandins, thromboxanes, and leukotrienes, which mediate various physiological responses, including inflammation, pain, fever, and blood clotting.

Arachidonic acid is found in high concentrations in animal products such as meat, poultry, fish, and eggs, as well as in some plant sources such as certain nuts and seeds. It is also available as a dietary supplement. However, it is important to note that excessive intake of arachidonic acid can contribute to the development of inflammation and other health problems, so it is recommended to consume this fatty acid in moderation as part of a balanced diet.

Phospholipases A2, Cytosolic are a group of enzymes that are responsible for hydrolyzing the ester bond at the sn-2 position of glycerophospholipids, releasing free fatty acids and lysophospholipids. They are classified as a subtype of phospholipases A2 (PLA2s) and are located in the cytosolic fraction of the cell. These enzymes play important roles in various biological processes such as membrane remodeling, signal transduction, and host defense mechanisms. They can be activated by a variety of stimuli, including calcium ions, hormones, and growth factors. Dysregulation of cytosolic PLA2s has been implicated in several pathological conditions, including inflammation, neurodegenerative diseases, and cancer.

Phospholipases A2, Calcium-Independent are a group of enzymes that belong to the phospholipase A2 family, which are capable of hydrolyzing the sn-2 ester bond of glycerophospholipids (also known as phospholipids) to release free fatty acids and lysophospholipids. Unlike other members of the phospholipase A2 family, calcium-independent phospholipases A2 do not require calcium ions for their catalytic activity. These enzymes play important roles in various biological processes, including inflammation, cell signaling, and membrane remodeling. They have been implicated in several pathological conditions, such as atherosclerosis, neurodegenerative diseases, and cancer.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

Bee venom is a poisonous substance that a honeybee (Apis mellifera) injects into the skin of a person or animal when it stings. It's produced in the venom gland and stored in the venom sac of the bee. Bee venom is a complex mixture of proteins, peptides, and other compounds. The main active components of bee venom include melittin, apamin, and phospholipase A2.

Melittin is a toxic peptide that causes pain, redness, and swelling at the site of the sting. It also has hemolytic (red blood cell-destroying) properties. Apamin is a neurotoxin that can affect the nervous system and cause neurological symptoms in severe cases. Phospholipase A2 is an enzyme that can damage cell membranes and contribute to the inflammatory response.

Bee venom has been used in traditional medicine for centuries, particularly in China and other parts of Asia. It's believed to have anti-inflammatory, analgesic (pain-relieving), and immunomodulatory effects. Some studies suggest that bee venom may have therapeutic potential for a variety of medical conditions, including rheumatoid arthritis, multiple sclerosis, and chronic pain. However, more research is needed to confirm these findings and to determine the safety and efficacy of bee venom therapy.

It's important to note that bee stings can cause severe allergic reactions (anaphylaxis) in some people, which can be life-threatening. If you experience symptoms such as difficulty breathing, rapid heartbeat, or hives after being stung by a bee, seek medical attention immediately.

Group IA Phospholipases A2 (PLA2s) are a subclass of phospholipases A2 that are characterized by their calcium-dependent enzymatic activity. They are a type of hydrolase enzyme that cleaves the sn-2 ester bond of glycerophospholipids, releasing free fatty acids and lysophospholipids.

In particular, Group IA PLA2s prefer to act on phosphatidylcholine (PC) substrates, and they play important roles in various biological processes, including inflammation, host defense, and lipid metabolism. These enzymes are secreted by various cells, such as pancreatic acinar cells, macrophages, and neutrophils, and can be activated by a variety of stimuli, including cytokines, bacterial products, and oxidative stress.

Group IA PLA2s are also known to contribute to the development and progression of several diseases, such as atherosclerosis, arthritis, and neurodegenerative disorders. Therefore, they have been considered as potential therapeutic targets for these conditions.

Phospholipase A2 (PLA2) inhibitors are substances that inhibit or block the activity of phospholipase A2, an enzyme that plays a role in inflammation. Phospholipase A2 is responsible for the breakdown of certain types of fat molecules called phospholipids, which are found in cell membranes. This breakdown releases fatty acids, including arachidonic acid, which can be further metabolized to produce pro-inflammatory signaling molecules called eicosanoids.

By inhibiting the activity of phospholipase A2, PLA2 inhibitors can help reduce the production of these inflammatory mediators and potentially decrease inflammation in the body. These inhibitors have been studied for their potential therapeutic benefits in a variety of conditions associated with inflammation, such as rheumatoid arthritis, pancreatitis, and atherosclerosis. However, more research is needed to fully understand their safety and efficacy.

Phosphatidylinositols (PIs) are a type of phospholipid that are abundant in the cell membrane. They contain a glycerol backbone, two fatty acid chains, and a head group consisting of myo-inositol, a cyclic sugar molecule, linked to a phosphate group.

Phosphatidylinositols can be phosphorylated at one or more of the hydroxyl groups on the inositol ring, forming various phosphoinositides (PtdInsPs) with different functions. These signaling molecules play crucial roles in regulating cellular processes such as membrane trafficking, cytoskeletal organization, and signal transduction pathways that control cell growth, differentiation, and survival.

Phosphatidylinositol 4,5-bisphosphate (PIP2) is a prominent phosphoinositide involved in the regulation of ion channels, enzymes, and cytoskeletal proteins. Upon activation of certain receptors, PIP2 can be cleaved by the enzyme phospholipase C into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (InsP3), which act as second messengers to trigger downstream signaling events.

Phosphatidylinositol Diacylglycerol-Lyase is an enzyme that plays a crucial role in the breakdown and metabolism of certain lipids known as phosphoinositides. These are important components of cell membranes and are involved in various cellular processes such as signal transduction.

The systematic name for this enzyme is 1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate D-3-phosphoinositide phospholipase C. Its function is to cleave 1,2-diacylglycerol and inositol 1,3,4,5-tetrakisphosphate from 1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate. This reaction is a key step in the phosphoinositide signaling pathway, which is involved in regulating various cellular functions such as cell growth, differentiation, and metabolism.

Defects in this enzyme have been associated with certain diseases, including neurological disorders and cancer. Therefore, understanding its function and regulation is an important area of research in biology and medicine.

I'm sorry for any confusion, but "snakes" is not a medical term. It refers to a group of legless reptiles that can be found on every continent except Antarctica. If you have any questions about snakes in a different context, please provide more information and I'll do my best to help!

Phosphatidic acids (PAs) are a type of phospholipid that are essential components of cell membranes. They are composed of a glycerol backbone linked to two fatty acid chains and a phosphate group. The phosphate group is esterified to another molecule, usually either serine, inositol, or choline, forming different types of phosphatidic acids.

PAs are particularly important as they serve as key regulators of many cellular processes, including signal transduction, membrane trafficking, and autophagy. They can act as signaling molecules by binding to and activating specific proteins, such as the enzyme phospholipase D, which generates second messengers involved in various signaling pathways.

PAs are also important intermediates in the synthesis of other phospholipids, such as phosphatidylcholine, phosphatidylethanolamine, and phosphatidylinositol. They are produced by the enzyme diacylglycerol kinase (DGK), which adds a phosphate group to diacylglycerol (DAG) to form PA.

Abnormal levels of PAs have been implicated in various diseases, including cancer, diabetes, and neurological disorders. Therefore, understanding the regulation and function of PAs is an active area of research with potential therapeutic implications.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Calcium is an essential mineral that is vital for various physiological processes in the human body. The medical definition of calcium is as follows:

Calcium (Ca2+) is a crucial cation and the most abundant mineral in the human body, with approximately 99% of it found in bones and teeth. It plays a vital role in maintaining structural integrity, nerve impulse transmission, muscle contraction, hormonal secretion, blood coagulation, and enzyme activation.

Calcium homeostasis is tightly regulated through the interplay of several hormones, including parathyroid hormone (PTH), calcitonin, and vitamin D. Dietary calcium intake, absorption, and excretion are also critical factors in maintaining optimal calcium levels in the body.

Hypocalcemia refers to low serum calcium levels, while hypercalcemia indicates high serum calcium levels. Both conditions can have detrimental effects on various organ systems and require medical intervention to correct.

'Bacillus cereus' is a gram-positive, rod-shaped bacterium that is commonly found in soil and food. It can produce heat-resistant spores, which allow it to survive in a wide range of temperatures and environments. This bacterium can cause two types of foodborne illnesses: a diarrheal type and an emetic (vomiting) type.

The diarrheal type of illness is caused by the consumption of foods contaminated with large numbers of vegetative cells of B. cereus. The symptoms typically appear within 6 to 15 hours after ingestion and include watery diarrhea, abdominal cramps, and nausea. Vomiting may also occur in some cases.

The emetic type of illness is caused by the consumption of foods contaminated with B. cereus toxins. This type of illness is characterized by nausea and vomiting that usually occur within 0.5 to 6 hours after ingestion. The most common sources of B. cereus contamination include rice, pasta, and other starchy foods that have been cooked and left at room temperature for several hours.

Proper food handling, storage, and cooking practices can help prevent B. cereus infections. It is important to refrigerate or freeze cooked foods promptly, reheat them thoroughly, and avoid leaving them at room temperature for extended periods.

'Crotalus' is a genus of venomous snakes commonly known as rattlesnakes. These snakes are native to the Americas, ranging from southern Canada to Argentina. They are characterized by the distinctive rattle on the end of their tails, which they use to warn potential predators before striking. The venom of Crotalus species is hemotoxic, meaning that it causes damage to blood vessels and tissue.

Some examples of species in this genus include the Western diamondback rattlesnake (Crotalus atrox), the timber rattlesnake (Crotalus horridus), and the sidewinder (Crotalus cerastes). It is important to note that all rattlesnakes are potentially dangerous and should be treated with caution. If you encounter a rattlesnake in the wild, it is best to leave it alone and avoid approaching it.

Phosphatidylethanolamines (PE) are a type of phospholipid that are abundantly found in the cell membranes of living organisms. They play a crucial role in maintaining the structural integrity and functionality of the cell membrane. PE contains a hydrophilic head, which consists of an ethanolamine group linked to a phosphate group, and two hydrophobic fatty acid chains. This unique structure allows PE to form a lipid bilayer, where the hydrophilic heads face outwards and interact with the aqueous environment, while the hydrophobic tails face inwards and interact with each other.

PE is also involved in various cellular processes, such as membrane trafficking, autophagy, and signal transduction. Additionally, PE can be modified by the addition of various functional groups or molecules, which can further regulate its functions and interactions within the cell. Overall, phosphatidylethanolamines are essential components of cellular membranes and play a critical role in maintaining cellular homeostasis.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

The pancreas is a glandular organ located in the abdomen, posterior to the stomach. It has both exocrine and endocrine functions. The exocrine portion of the pancreas consists of acinar cells that produce and secrete digestive enzymes into the duodenum via the pancreatic duct. These enzymes help in the breakdown of proteins, carbohydrates, and fats in food.

The endocrine portion of the pancreas consists of clusters of cells called islets of Langerhans, which include alpha, beta, delta, and F cells. These cells produce and secrete hormones directly into the bloodstream, including insulin, glucagon, somatostatin, and pancreatic polypeptide. Insulin and glucagon are critical regulators of blood sugar levels, with insulin promoting glucose uptake and storage in tissues and glucagon stimulating glycogenolysis and gluconeogenesis to raise blood glucose when it is low.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Quinacrine is a medication that belongs to the class of drugs called antimalarials. It is primarily used in the treatment and prevention of malaria caused by Plasmodium falciparum and P. vivax parasites. Quinacrine works by inhibiting the growth of the malarial parasites in the red blood cells.

In addition to its antimalarial properties, quinacrine has been used off-label for various other medical conditions, including the treatment of rheumatoid arthritis and discoid lupus erythematosus (DLE), a type of skin lupus. However, its use in these conditions is not approved by regulatory authorities such as the US Food and Drug Administration (FDA) due to limited evidence and potential side effects.

Quinacrine has several known side effects, including gastrointestinal disturbances, skin rashes, headache, dizziness, and potential neuropsychiatric symptoms like depression, anxiety, or confusion. Long-term use of quinacrine may also lead to yellowing of the skin and eyes (known as quinacrine jaundice) and other eye-related issues. It is essential to consult a healthcare professional before starting quinacrine or any other medication for appropriate dosage, duration, and potential side effects.

Membrane lipids are the main component of biological membranes, forming a lipid bilayer in which various cellular processes take place. These lipids include phospholipids, glycolipids, and cholesterol. Phospholipids are the most abundant type, consisting of a hydrophilic head (containing a phosphate group) and two hydrophobic tails (composed of fatty acid chains). Glycolipids contain a sugar group attached to the lipid molecule. Cholesterol helps regulate membrane fluidity and permeability. Together, these lipids create a selectively permeable barrier that separates cells from their environment and organelles within cells.

"Trimeresurus" is a genus of venomous pit vipers found primarily in Asia. Commonly known as "Asian pit vipers" or " temple pit vipers," these snakes are characterized by the presence of a heat-sensing pit organ between the eye and the nostril, which they use to detect the body heat of their prey. They are responsible for causing serious bites and occasionally fatal accidents in human beings.

It's important to note that "Trimeresurus" is a taxonomic term used in the field of biology, specifically in systematics and classification of organisms. It does not have a direct medical definition, but it refers to a group of snakes with medical significance due to their venomous nature.

Arachidonic acids are a type of polyunsaturated fatty acid that is primarily found in the phospholipids of cell membranes. They contain 20 carbon atoms and four double bonds (20:4n-6), with the first double bond located at the sixth carbon atom from the methyl end.

Arachidonic acids are derived from linoleic acid, an essential fatty acid that cannot be synthesized by the human body and must be obtained through dietary sources such as meat, fish, and eggs. Once ingested, linoleic acid is converted to arachidonic acid in a series of enzymatic reactions.

Arachidonic acids play an important role in various physiological processes, including inflammation, immune response, and cell signaling. They serve as precursors for the synthesis of eicosanoids, which are signaling molecules that include prostaglandins, thromboxanes, and leukotrienes. These eicosanoids have diverse biological activities, such as modulating blood flow, platelet aggregation, and pain perception, among others.

However, excessive production of arachidonic acid-derived eicosanoids has been implicated in various pathological conditions, including inflammation, atherosclerosis, and cancer. Therefore, the regulation of arachidonic acid metabolism is an important area of research for the development of new therapeutic strategies.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Phosphoinositide Phospholipase C (PI-PLC) is an enzyme that plays a crucial role in intracellular signaling pathways. It catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2), a phospholipid component of the cell membrane, into two second messengers: inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG).

IP3 is responsible for triggering the release of calcium ions from intracellular stores, while DAG remains in the membrane and activates certain protein kinase C (PKC) isoforms. These second messengers then go on to modulate various cellular processes such as gene expression, metabolism, secretion, and cell growth or differentiation. PI-PLC exists in multiple isoforms, which are classified based on their structure and activation mechanisms. They can be activated by a variety of extracellular signals, including hormones, neurotransmitters, and growth factors, making them important components in signal transduction cascades.

I believe there might be a misunderstanding in your question. "Pyrones" is not a medical term, but rather a chemical term used to describe a class of organic compounds known as lactones with a characteristic eight-membered ring. These compounds are found in various natural sources such as plants and fungi, and some have been studied for their potential biological activities.

However, if you meant "pyrexia" instead of "pyrones," then I can provide the medical definition:

Pyrexia is a term used to describe an abnormally elevated body temperature, also known as fever. In adults, a core body temperature of 100.4°F (38°C) or higher is generally considered indicative of pyrexia. Fever is often a response to an infection or inflammation in the body and can be part of the immune system's effort to combat pathogens.

Lysophosphatidylcholines (LPCs) are a type of glycerophospholipids, which are major components of cell membranes. They are formed by the hydrolysis of phosphatidylcholines, another type of glycerophospholipids, catalyzed by the enzyme phospholipase A2. LPCs contain a single fatty acid chain attached to a glycerol backbone and a choline headgroup.

In medical terms, LPCs have been implicated in various physiological and pathological processes, such as cell signaling, membrane remodeling, and inflammation. Elevated levels of LPCs have been found in several diseases, including cardiovascular disease, neurodegenerative disorders, and cancer. They can also serve as biomarkers for the diagnosis and prognosis of these conditions.

Group IB Phospholipases A2 (PLA2s) are a subclass of phospholipases A2, which are enzymes that hydrolyze the sn-2 acyl bond of glycerophospholipids to release free fatty acids and lysophospholipids. Specifically, Group IB PLA2s are secreted enzymes that require calcium ions for their activity and have a low molecular weight. They are produced by various tissues and cells, including pancreas, liver, and immune cells, and play important roles in various biological processes such as inflammation, host defense, and lipid metabolism. Group IB PLA2s have been implicated in several pathological conditions, including atherosclerosis, arthritis, and neurodegenerative diseases.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Diacylglycerols (also known as diglycerides) are a type of glyceride, which is a compound that consists of glycerol and one or more fatty acids. Diacylglycerols contain two fatty acid chains bonded to a glycerol molecule through ester linkages. They are important intermediates in the metabolism of lipids and can be found in many types of food, including vegetable oils and dairy products. In the body, diacylglycerols can serve as a source of energy and can also play roles in cell signaling processes.

I'm sorry for any confusion, but "Thiones" is not a recognized medical term or abbreviation in physiology, pharmacology, or clinical medicine. It seems there might be a misunderstanding or a typo in your question. If you meant "thiols," I can provide a definition for that. Thiols are organic compounds containing a sulfhydryl group (-SH), which is a functional group consisting of a sulfur atom bonded to a hydrogen atom. Thiols are important in biological systems and can be found in some proteins and enzymes, where they play a crucial role in their structure and function. If you meant something else, please clarify so I can provide the most accurate information.

Russell's Viper is not a medical condition or term. It is a type of venomous snake, scientifically known as Daboia russelii, found in parts of Asia. The bite of this viper can cause severe symptoms such as pain, swelling, bleeding, tissue damage, and potentially life-threatening systemic effects like kidney failure, blood clotting problems, and cardiac arrest. Medical personnel should be notified immediately in case of a snakebite, and appropriate antivenom therapy should be initiated as soon as possible to reduce the risk of complications or mortality.

Cytosol refers to the liquid portion of the cytoplasm found within a eukaryotic cell, excluding the organelles and structures suspended in it. It is the site of various metabolic activities and contains a variety of ions, small molecules, and enzymes. The cytosol is where many biochemical reactions take place, including glycolysis, protein synthesis, and the regulation of cellular pH. It is also where some organelles, such as ribosomes and vesicles, are located. In contrast to the cytosol, the term "cytoplasm" refers to the entire contents of a cell, including both the cytosol and the organelles suspended within it.

Glycerophospholipids, also known as phosphoglycerides, are a major class of lipids that constitute the structural components of biological membranes. They are composed of a glycerol backbone to which two fatty acid chains and a phosphate group are attached. The phosphate group is esterified to an alcohol, typically choline, ethanolamine, serine, or inositol, forming what is called a phosphatidyl headgroup.

The chemical structure of glycerophospholipids allows them to form bilayers, which are essential for the formation of cell membranes and organelles within cells. The fatty acid chains, which can be saturated or unsaturated, contribute to the fluidity and permeability of the membrane. Glycerophospholipids also play important roles in various cellular processes, including signal transduction, cell recognition, and metabolism.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Butanols are a family of alcohols with four carbon atoms and a chemical formula of C4H9OH. They are commonly used as solvents, intermediates in chemical synthesis, and fuel additives. The most common butanol is n-butanol (normal butanol), which has a straight chain of four carbon atoms. Other forms include secondary butanols (such as isobutanol) and tertiary butanols (such as tert-butanol). These compounds have different physical and chemical properties due to the differences in their molecular structure, but they all share the common characteristic of being alcohols with four carbon atoms.

Micelles are structures formed in a solution when certain substances, such as surfactants, reach a critical concentration called the critical micelle concentration (CMC). At this concentration, these molecules, which have both hydrophilic (water-attracting) and hydrophobic (water-repelling) components, arrange themselves in a spherical shape with the hydrophilic parts facing outward and the hydrophobic parts clustered inside. This formation allows the hydrophobic components to avoid contact with water while the hydrophilic components interact with it. Micelles are important in various biological and industrial processes, such as drug delivery, soil remediation, and the formation of emulsions.

Phospholipase C beta (PLCβ) is an enzyme that plays a crucial role in intracellular signaling transduction pathways. It is a subtype of Phospholipase C, which is responsible for cleaving phospholipids into secondary messengers, thereby mediating various cellular responses.

PLCβ is activated by G protein-coupled receptors (GPCRs) and can be found in various tissues throughout the body. Once activated, PLCβ hydrolyzes a specific phospholipid, PIP2 (Phosphatidylinositol 4,5-bisphosphate), into two secondary messengers: IP3 (Inositol 1,4,5-trisphosphate) and DAG (Diacylglycerol). These second messengers then trigger a series of downstream events, such as calcium mobilization and protein kinase C activation, which ultimately lead to changes in cell functions, including gene expression, cell growth, differentiation, and secretion.

There are four isoforms of PLCβ (PLCβ1, PLCβ2, PLCβ3, and PLCβ4) that differ in their tissue distribution, regulation, and substrate specificity. Mutations or dysregulation of PLCβ have been implicated in several diseases, including cancer, cardiovascular disease, and neurological disorders.

Indolizidines are a type of heterocyclic organic compound that contains a five-membered ring fused to a six-membered ring, with one nitrogen atom and one carbon atom common to both rings. The structure of indolizidine is similar to that of the naturally occurring alkaloids, which are found in various plants and animals and have diverse biological activities.

Indolizidines can be synthesized in the laboratory and have been studied for their potential therapeutic uses, such as anti-inflammatory, antiviral, and insecticidal properties. However, they can also have toxic effects and may interact with other drugs or chemicals in the body.

It is important to note that indolizidines are not a medical term per se, but rather a chemical classification of a specific type of organic compound.

Lysophospholipids are a type of glycerophospholipid, which is a major component of cell membranes. They are characterized by having only one fatty acid chain attached to the glycerol backbone, as opposed to two in regular phospholipids. This results in a more polar and charged molecule, which can play important roles in cell signaling and regulation.

Lysophospholipids can be derived from the breakdown of regular phospholipids through the action of enzymes such as phospholipase A1 or A2. They can also be synthesized de novo in the cell. Some lysophospholipids, such as lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P), have been found to act as signaling molecules that bind to specific G protein-coupled receptors and regulate various cellular processes, including proliferation, survival, and migration.

Abnormal levels of lysophospholipids have been implicated in several diseases, such as cancer, inflammation, and neurological disorders. Therefore, understanding the biology of lysophospholipids has important implications for developing new therapeutic strategies.

'Clostridium perfringens' is a type of Gram-positive, rod-shaped, spore-forming bacterium that is commonly found in the environment, including in soil, decaying vegetation, and the intestines of humans and animals. It is a major cause of foodborne illness worldwide, producing several toxins that can lead to symptoms such as diarrhea, abdominal cramps, nausea, and vomiting.

The bacterium can contaminate food during preparation or storage, particularly meat and poultry products. When ingested, the spores of C. perfringens can germinate and produce large numbers of toxin-producing cells in the intestines, leading to food poisoning. The most common form of C. perfringens food poisoning is characterized by symptoms that appear within 6 to 24 hours after ingestion and last for less than 24 hours.

In addition to foodborne illness, C. perfringens can also cause other types of infections, such as gas gangrene, a serious condition that can occur when the bacterium infects a wound and produces toxins that damage surrounding tissues. Gas gangrene is a medical emergency that requires prompt treatment with antibiotics and surgical debridement or amputation of affected tissue.

Prevention measures for C. perfringens food poisoning include proper cooking, handling, and storage of food, as well as rapid cooling of cooked foods to prevent the growth of the bacterium.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Lysosomes are membrane-bound organelles found in the cytoplasm of eukaryotic cells. They are responsible for breaking down and recycling various materials, such as waste products, foreign substances, and damaged cellular components, through a process called autophagy or phagocytosis. Lysosomes contain hydrolytic enzymes that can break down biomolecules like proteins, nucleic acids, lipids, and carbohydrates into their basic building blocks, which can then be reused by the cell. They play a crucial role in maintaining cellular homeostasis and are often referred to as the "garbage disposal system" of the cell.

Bridged compounds are a type of organic compound where two parts of the molecule are connected by a chain of atoms, known as a bridge. This bridge can consist of one or more atoms and can be made up of carbon, oxygen, nitrogen, or other elements. The bridge can be located between two carbon atoms in a hydrocarbon, for example, creating a bridged bicyclic structure. These types of compounds are important in organic chemistry and can have unique chemical and physical properties compared to non-bridged compounds.

Eicosanoids are a group of signaling molecules made by the enzymatic or non-enzymatic oxidation of arachidonic acid and other polyunsaturated fatty acids with 20 carbon atoms. They include prostaglandins, thromboxanes, leukotrienes, and lipoxins, which are involved in a wide range of physiological and pathophysiological processes, such as inflammation, immune response, blood clotting, and smooth muscle contraction. Eicosanoids act as local hormones or autacoids, affecting the function of cells near where they are produced. They are synthesized by various cell types, including immune cells, endothelial cells, and neurons, in response to different stimuli, such as injury, infection, or stress. The balance between different eicosanoids can have significant effects on health and disease.

Glycosylphosphatidylinositols (GPIs) are complex glycolipids that are attached to the outer leaflet of the cell membrane. They play a role in anchoring proteins to the cell surface by serving as a post-translational modification site for certain proteins, known as GPI-anchored proteins.

The structure of GPIs consists of a core glycan backbone made up of three mannose and one glucosamine residue, which is linked to a phosphatidylinositol (PI) anchor via a glycosylphosphatidylinositol anchor addition site. The PI anchor is composed of a diacylglycerol moiety and a phosphatidylinositol headgroup.

GPIs are involved in various cellular processes, including signal transduction, protein targeting, and cell adhesion. They have also been implicated in several diseases, such as cancer and neurodegenerative disorders.

1-Butanol, also known as n-butanol or butyl alcohol, is a primary alcohol with a chemical formula of C4H9OH. It is a colorless liquid that is used as a solvent and in the manufacture of other chemicals. 1-Butanol has a wide range of applications including use as a paint thinner, in the production of rubber, and as a fuel additive. It is also found naturally in some foods and beverages.

In medical terms, 1-butanol may be used as an ingredient in topical medications or as a solvent for various pharmaceutical preparations. However, it is not typically used as a therapeutic agent on its own. Exposure to high levels of 1-butanol can cause irritation to the eyes, skin, and respiratory tract, and prolonged exposure may lead to more serious health effects.

Venom is a complex mixture of toxic compounds produced by certain animals, such as snakes, spiders, scorpions, and marine creatures like cone snails and stonefish. These toxic substances are specifically designed to cause damage to the tissues or interfere with the normal physiological processes of other organisms, which can lead to harmful or even lethal effects.

Venoms typically contain a variety of components, including enzymes, peptides, proteins, and small molecules, each with specific functions that contribute to the overall toxicity of the mixture. Some of these components may cause localized damage, such as tissue necrosis or inflammation, while others can have systemic effects, impacting various organs and bodily functions.

The study of venoms, known as toxinology, has important implications for understanding the evolution of animal behavior, developing new therapeutics, and advancing medical treatments for envenomation (the process of being poisoned by venom). Additionally, venoms have been used in traditional medicine for centuries, and ongoing research continues to uncover novel compounds with potential applications in modern pharmacology.

Phosphatidylglycerols are a type of glycerophospholipids, which are major components of biological membranes. They are composed of a glycerol backbone to which two fatty acid chains and a phosphate group are attached. In the case of phosphatidylglycerols, the phosphate group is linked to a glycerol molecule through an ester bond, forming a phosphoglyceride.

Phosphatidylglycerols are unique because they have an additional glycerol molecule attached to the phosphate group, making them more complex than other glycerophospholipids such as phosphatidylcholine or phosphatidylethanolamine. This additional glycerol moiety can be further modified by the addition of various headgroups, leading to the formation of different subclasses of phosphatidylglycerols.

In biological membranes, phosphatidylglycerols are often found in the inner leaflet of the mitochondrial membrane and play important roles in maintaining the structure and function of this organelle. They have also been implicated in various cellular processes such as membrane fusion, protein trafficking, and bacterial cell wall biosynthesis.

A fluoroimmunoassay (FIA) is a type of biochemical test that uses fluorescence to detect and measure the presence or concentration of a specific component, such as a protein or hormone, in a sample. In a FIA, the sample is mixed with a reagent that contains a fluorescent label, which binds to the target component. When the mixture is exposed to light of a specific wavelength, the labeled component emits light at a different wavelength, allowing it to be detected and measured.

FIAs are often used in clinical laboratories to diagnose and monitor various medical conditions, as they can provide sensitive and accurate measurements of specific components in biological samples. They are also used in research settings to study the interactions between biomolecules and to develop new diagnostic tests.

Neomycin is an antibiotic drug derived from the bacterium Streptomyces fradiae. It belongs to the class of aminoglycoside antibiotics and works by binding to the 30S subunit of the bacterial ribosome, thereby inhibiting protein synthesis and leading to bacterial cell death. Neomycin is primarily used topically (on the skin or mucous membranes) due to its poor absorption into the bloodstream when taken orally. It is effective against a wide range of gram-positive and gram-negative bacteria. Medical definitions for Neomycin include:

1. An antibiotic (aminoglycoside) derived from Streptomyces fradiae, used primarily for topical application in the treatment of superficial infections, burns, and wounds. It is not usually used systemically due to its potential ototoxicity and nephrotoxicity.
2. A medication (generic name) available as a cream, ointment, solution, or powder, often combined with other active ingredients such as bacitracin and polymyxin B for broader-spectrum antibacterial coverage. Neomycin is used to treat various skin conditions, including eczema, dermatitis, and minor cuts or abrasions.
3. A component of some over-the-counter products (e.g., ear drops, eye drops) intended for the treatment of external otitis, swimmer's ear, or bacterial conjunctivitis. It is crucial to follow the instructions carefully and avoid using neomycin-containing products for extended periods or in larger quantities than recommended, as this may increase the risk of antibiotic resistance and potential side effects.

In summary, Neomycin is an aminoglycoside antibiotic primarily used topically for treating various superficial bacterial infections due to its effectiveness against a wide range of gram-positive and gram-negative bacteria. It should be used cautiously and as directed to minimize the risk of side effects and antibiotic resistance.

Phosphoric diester hydrolases are a class of enzymes that catalyze the hydrolysis of phosphoric diester bonds. These enzymes are also known as phosphatases or nucleotidases. They play important roles in various biological processes, such as signal transduction, metabolism, and regulation of cellular activities.

Phosphoric diester hydrolases can be further classified into several subclasses based on their substrate specificity and catalytic mechanism. For example, alkaline phosphatases (ALPs) are a group of phosphoric diester hydrolases that preferentially hydrolyze phosphomonoester bonds in a variety of organic molecules, releasing phosphate ions and alcohols. On the other hand, nucleotidases are a subclass of phosphoric diester hydrolases that specifically hydrolyze the phosphodiester bonds in nucleotides, releasing nucleosides and phosphate ions.

Overall, phosphoric diester hydrolases are essential for maintaining the balance of various cellular processes by regulating the levels of phosphorylated molecules and nucleotides.

I'm sorry for any confusion, but "Indolizines" is not a medical term. It is a chemical term that refers to a class of heterocyclic organic compounds which contain a seven-membered ring with two nitrogen atoms and a carbon-carbon double bond. They are used in the synthesis of various pharmaceuticals and natural products, but they are not a medical condition or diagnosis.

"Swine" is a common term used to refer to even-toed ungulates of the family Suidae, including domestic pigs and wild boars. However, in a medical context, "swine" often appears in the phrase "swine flu," which is a strain of influenza virus that typically infects pigs but can also cause illness in humans. The 2009 H1N1 pandemic was caused by a new strain of swine-origin influenza A virus, which was commonly referred to as "swine flu." It's important to note that this virus is not transmitted through eating cooked pork products; it spreads from person to person, mainly through respiratory droplets produced when an infected person coughs or sneezes.

Galactolipids are a type of glycolipid, which are lipids that contain a carbohydrate moiety. They are the most abundant lipids in plant chloroplasts and play important roles in membrane structure and function. The term "galactolipid" refers to lipids that contain one or more galactose molecules as their polar headgroup.

The two major types of galactolipids are monogalactosyldiacylglycerols (MGDGs) and digalactosyldiacylglycerols (DGDGs). MGDGs contain a single galactose molecule, while DGDGs contain two. These lipids are important components of the thylakoid membrane in chloroplasts, where they help to maintain the structural integrity and fluidity of the membrane, as well as facilitate the movement of proteins and other molecules within it.

In addition to their role in plant cells, galactolipids have also been found to be important in animal cells, particularly in the brain. They are a major component of myelin sheaths, which surround and insulate nerve fibers, allowing for efficient electrical signaling. Abnormalities in galactolipid metabolism have been linked to several neurological disorders, including multiple sclerosis and Krabbe disease.

Enzyme inhibitors are substances that bind to an enzyme and decrease its activity, preventing it from catalyzing a chemical reaction in the body. They can work by several mechanisms, including blocking the active site where the substrate binds, or binding to another site on the enzyme to change its shape and prevent substrate binding. Enzyme inhibitors are often used as drugs to treat various medical conditions, such as high blood pressure, abnormal heart rhythms, and bacterial infections. They can also be found naturally in some foods and plants, and can be used in research to understand enzyme function and regulation.

Plasmalogens are a type of complex lipid called glycerophospholipids, which are essential components of cell membranes. They are characterized by having a unique chemical structure that includes a vinyl ether bond at the sn-1 position of the glycerol backbone and an ester bond at the sn-2 position, with the majority of them containing polyunsaturated fatty acids. The headgroup attached to the sn-3 position is typically choline or ethanolamine.

Plasmalogens are abundant in certain tissues, such as the brain, heart, and skeletal muscle. They have been suggested to play important roles in cellular functions, including membrane fluidity, signal transduction, and protection against oxidative stress. Reduced levels of plasmalogens have been associated with various diseases, including neurological disorders, cardiovascular diseases, and aging-related conditions.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Choline is an essential nutrient that is vital for the normal functioning of all cells, particularly those in the brain and liver. It is a water-soluble compound that is neither a vitamin nor a mineral, but is often grouped with vitamins because it has many similar functions. Choline is a precursor to the neurotransmitter acetylcholine, which plays an important role in memory, mood, and other cognitive processes. It also helps to maintain the structural integrity of cell membranes and is involved in the transport and metabolism of fats.

Choline can be synthesized by the body in small amounts, but it is also found in a variety of foods such as eggs, meat, fish, nuts, and cruciferous vegetables. Some people may require additional choline through supplementation, particularly if they follow a vegetarian or vegan diet, are pregnant or breastfeeding, or have certain medical conditions that affect choline metabolism.

Deficiency in choline can lead to a variety of health problems, including liver disease, muscle damage, and neurological disorders. On the other hand, excessive intake of choline can cause fishy body odor, sweating, and gastrointestinal symptoms such as diarrhea and vomiting. It is important to maintain adequate levels of choline through a balanced diet and, if necessary, supplementation under the guidance of a healthcare professional.

Detergents are cleaning agents that are often used to remove dirt, grease, and stains from various surfaces. They contain one or more surfactants, which are compounds that lower the surface tension between two substances, such as water and oil, allowing them to mix more easily. This makes it possible for detergents to lift and suspend dirt particles in water so they can be rinsed away.

Detergents may also contain other ingredients, such as builders, which help to enhance the cleaning power of the surfactants by softening hard water or removing mineral deposits. Some detergents may also include fragrances, colorants, and other additives to improve their appearance or performance.

In a medical context, detergents are sometimes used as disinfectants or antiseptics, as they can help to kill bacteria, viruses, and other microorganisms on surfaces. However, it is important to note that not all detergents are effective against all types of microorganisms, and some may even be toxic or harmful if used improperly.

It is always important to follow the manufacturer's instructions when using any cleaning product, including detergents, to ensure that they are used safely and effectively.

Edetic acid, also known as ethylenediaminetetraacetic acid (EDTA), is not a medical term per se, but a chemical compound with various applications in medicine. EDTA is a synthetic amino acid that acts as a chelating agent, which means it can bind to metallic ions and form stable complexes.

In medicine, EDTA is primarily used in the treatment of heavy metal poisoning, such as lead or mercury toxicity. It works by binding to the toxic metal ions in the body, forming a stable compound that can be excreted through urine. This helps reduce the levels of harmful metals in the body and alleviate their toxic effects.

EDTA is also used in some diagnostic tests, such as the determination of calcium levels in blood. Additionally, it has been explored as a potential therapy for conditions like atherosclerosis and Alzheimer's disease, although its efficacy in these areas remains controversial and unproven.

It is important to note that EDTA should only be administered under medical supervision due to its potential side effects and the need for careful monitoring of its use.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Lipid metabolism is the process by which the body breaks down and utilizes lipids (fats) for various functions, such as energy production, cell membrane formation, and hormone synthesis. This complex process involves several enzymes and pathways that regulate the digestion, absorption, transport, storage, and consumption of fats in the body.

The main types of lipids involved in metabolism include triglycerides, cholesterol, phospholipids, and fatty acids. The breakdown of these lipids begins in the digestive system, where enzymes called lipases break down dietary fats into smaller molecules called fatty acids and glycerol. These molecules are then absorbed into the bloodstream and transported to the liver, which is the main site of lipid metabolism.

In the liver, fatty acids may be further broken down for energy production or used to synthesize new lipids. Excess fatty acids may be stored as triglycerides in specialized cells called adipocytes (fat cells) for later use. Cholesterol is also metabolized in the liver, where it may be used to synthesize bile acids, steroid hormones, and other important molecules.

Disorders of lipid metabolism can lead to a range of health problems, including obesity, diabetes, cardiovascular disease, and non-alcoholic fatty liver disease (NAFLD). These conditions may be caused by genetic factors, lifestyle habits, or a combination of both. Proper diagnosis and management of lipid metabolism disorders typically involves a combination of dietary changes, exercise, and medication.

Acetophenones are organic compounds that consist of a phenyl group (a benzene ring with a hydroxyl group replaced by a hydrogen atom) bonded to an acetyl group (a carbonyl group bonded to a methyl group). The chemical structure can be represented as CH3COC6H5.

Acetophenones are aromatic ketones and can be found in essential oils of various plants, as well as in some synthetic fragrances. They have a characteristic sweet, fruity odor and are used in the perfume industry. In addition to their use as fragrances, acetophenones have been studied for their potential medicinal properties, including anti-inflammatory, antimicrobial, and analgesic effects. However, more research is needed before they can be considered safe and effective for medical use.

Cell surface receptors, also known as membrane receptors, are proteins located on the cell membrane that bind to specific molecules outside the cell, known as ligands. These receptors play a crucial role in signal transduction, which is the process of converting an extracellular signal into an intracellular response.

Cell surface receptors can be classified into several categories based on their structure and mechanism of action, including:

1. Ion channel receptors: These receptors contain a pore that opens to allow ions to flow across the cell membrane when they bind to their ligands. This ion flux can directly activate or inhibit various cellular processes.
2. G protein-coupled receptors (GPCRs): These receptors consist of seven transmembrane domains and are associated with heterotrimeric G proteins that modulate intracellular signaling pathways upon ligand binding.
3. Enzyme-linked receptors: These receptors possess an intrinsic enzymatic activity or are linked to an enzyme, which becomes activated when the receptor binds to its ligand. This activation can lead to the initiation of various signaling cascades within the cell.
4. Receptor tyrosine kinases (RTKs): These receptors contain intracellular tyrosine kinase domains that become activated upon ligand binding, leading to the phosphorylation and activation of downstream signaling molecules.
5. Integrins: These receptors are transmembrane proteins that mediate cell-cell or cell-matrix interactions by binding to extracellular matrix proteins or counter-receptors on adjacent cells. They play essential roles in cell adhesion, migration, and survival.

Cell surface receptors are involved in various physiological processes, including neurotransmission, hormone signaling, immune response, and cell growth and differentiation. Dysregulation of these receptors can contribute to the development of numerous diseases, such as cancer, diabetes, and neurological disorders.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

"Listeria monocytogenes" is a gram-positive, facultatively anaerobic, rod-shaped bacterium that is a major cause of foodborne illness. It is widely distributed in the environment and can be found in water, soil, vegetation, and various animal species. This pathogen is particularly notable for its ability to grow at low temperatures, allowing it to survive and multiply in refrigerated foods.

In humans, Listeria monocytogenes can cause a serious infection known as listeriosis, which primarily affects pregnant women, newborns, older adults, and individuals with weakened immune systems. The bacterium can cross the intestinal barrier, enter the bloodstream, and spread to the central nervous system, causing meningitis or encephalitis. Pregnant women infected with Listeria monocytogenes may experience mild flu-like symptoms but are at risk of transmitting the infection to their unborn children, which can result in stillbirth, premature delivery, or severe illness in newborns.

Common sources of Listeria monocytogenes include raw or undercooked meat, poultry, and seafood; unpasteurized dairy products; and ready-to-eat foods like deli meats, hot dogs, and soft cheeses. Proper food handling, cooking, and storage practices can help prevent listeriosis.

Hemolysis is the destruction or breakdown of red blood cells, resulting in the release of hemoglobin into the surrounding fluid (plasma). This process can occur due to various reasons such as chemical agents, infections, autoimmune disorders, mechanical trauma, or genetic abnormalities. Hemolysis may lead to anemia and jaundice, among other complications. It is essential to monitor hemolysis levels in patients undergoing medical treatments that might cause this condition.

Neurotoxins are substances that are poisonous or destructive to nerve cells (neurons) and the nervous system. They can cause damage by destroying neurons, disrupting communication between neurons, or interfering with the normal functioning of the nervous system. Neurotoxins can be produced naturally by certain organisms, such as bacteria, plants, and animals, or they can be synthetic compounds created in a laboratory. Examples of neurotoxins include botulinum toxin (found in botulism), tetrodotoxin (found in pufferfish), and heavy metals like lead and mercury. Neurotoxic effects can range from mild symptoms such as headaches, muscle weakness, and tremors, to more severe symptoms such as paralysis, seizures, and cognitive impairment. Long-term exposure to neurotoxins can lead to chronic neurological conditions and other health problems.

Naphthalene is not typically referred to as a medical term, but it is a chemical compound with the formula C10H8. It is a white crystalline solid that is aromatic and volatile, and it is known for its distinctive mothball smell. In a medical context, naphthalene is primarily relevant as a potential toxin or irritant.

Naphthalene can be found in some chemical products, such as mothballs and toilet deodorant blocks. Exposure to high levels of naphthalene can cause symptoms such as nausea, vomiting, diarrhea, and headaches. Long-term exposure has been linked to anemia and damage to the liver and nervous system.

In addition, naphthalene is a known environmental pollutant that can be found in air, water, and soil. It is produced by the combustion of fossil fuels and is also released from some industrial processes. Naphthalene has been shown to have toxic effects on aquatic life and may pose a risk to human health if exposure levels are high enough.

Fatty acids are carboxylic acids with a long aliphatic chain, which are important components of lipids and are widely distributed in living organisms. They can be classified based on the length of their carbon chain, saturation level (presence or absence of double bonds), and other structural features.

The two main types of fatty acids are:

1. Saturated fatty acids: These have no double bonds in their carbon chain and are typically solid at room temperature. Examples include palmitic acid (C16:0) and stearic acid (C18:0).
2. Unsaturated fatty acids: These contain one or more double bonds in their carbon chain and can be further classified into monounsaturated (one double bond) and polyunsaturated (two or more double bonds) fatty acids. Examples of unsaturated fatty acids include oleic acid (C18:1, monounsaturated), linoleic acid (C18:2, polyunsaturated), and alpha-linolenic acid (C18:3, polyunsaturated).

Fatty acids play crucial roles in various biological processes, such as energy storage, membrane structure, and cell signaling. Some essential fatty acids cannot be synthesized by the human body and must be obtained through dietary sources.

Calcimycin is a ionophore compound that is produced by the bacterium Streptomyces chartreusensis. It is also known as Calcineurin A inhibitor because it can bind to and inhibit the activity of calcineurin, a protein phosphatase. In medical research, calcimycin is often used to study calcium signaling in cells.
It has been also used in laboratory studies for its antiproliferative and pro-apoptotic effects on certain types of cancer cells. However, it is not approved for use as a drug in humans.

1-Alkyl-2-acetylglycerophosphocholine esterase is an enzyme that hydrolyzes the ester bond in 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine (also known as platelet-activating factor, PAF), resulting in the production of 1-alkyl-2-lyso-sn-glycero-3-phosphocholine and acetate. This enzyme is involved in the regulation of PAF levels and thus plays a role in the modulation of various physiological processes, including inflammation and allergic responses.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Virulence, in the context of medicine and microbiology, refers to the degree or severity of damage or harm that a pathogen (like a bacterium, virus, fungus, or parasite) can cause to its host. It is often associated with the ability of the pathogen to invade and damage host tissues, evade or suppress the host's immune response, replicate within the host, and spread between hosts.

Virulence factors are the specific components or mechanisms that contribute to a pathogen's virulence, such as toxins, enzymes, adhesins, and capsules. These factors enable the pathogen to establish an infection, cause tissue damage, and facilitate its transmission between hosts. The overall virulence of a pathogen can be influenced by various factors, including host susceptibility, environmental conditions, and the specific strain or species of the pathogen.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Thin-layer chromatography (TLC) is a type of chromatography used to separate, identify, and quantify the components of a mixture. In TLC, the sample is applied as a small spot onto a thin layer of adsorbent material, such as silica gel or alumina, which is coated on a flat, rigid support like a glass plate. The plate is then placed in a developing chamber containing a mobile phase, typically a mixture of solvents.

As the mobile phase moves up the plate by capillary action, it interacts with the stationary phase and the components of the sample. Different components of the mixture travel at different rates due to their varying interactions with the stationary and mobile phases, resulting in distinct spots on the plate. The distance each component travels can be measured and compared to known standards to identify and quantify the components of the mixture.

TLC is a simple, rapid, and cost-effective technique that is widely used in various fields, including forensics, pharmaceuticals, and research laboratories. It allows for the separation and analysis of complex mixtures with high resolution and sensitivity, making it an essential tool in many analytical applications.

Species specificity is a term used in the field of biology, including medicine, to refer to the characteristic of a biological entity (such as a virus, bacterium, or other microorganism) that allows it to interact exclusively or preferentially with a particular species. This means that the biological entity has a strong affinity for, or is only able to infect, a specific host species.

For example, HIV is specifically adapted to infect human cells and does not typically infect other animal species. Similarly, some bacterial toxins are species-specific and can only affect certain types of animals or humans. This concept is important in understanding the transmission dynamics and host range of various pathogens, as well as in developing targeted therapies and vaccines.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.

In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.

Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.

Inositol phosphates are a family of molecules that consist of an inositol ring, which is a six-carbon heterocyclic compound, linked to one or more phosphate groups. These molecules play important roles as intracellular signaling intermediates and are involved in various cellular processes such as cell growth, differentiation, and metabolism.

Inositol hexakisphosphate (IP6), also known as phytic acid, is a form of inositol phosphate that is found in plant-based foods. IP6 has the ability to bind to minerals such as calcium, magnesium, and iron, which can reduce their bioavailability in the body.

Inositol phosphates have been implicated in several diseases, including cancer, diabetes, and neurodegenerative disorders. For example, altered levels of certain inositol phosphates have been observed in cancer cells, suggesting that they may play a role in tumor growth and progression. Additionally, mutations in enzymes involved in the metabolism of inositol phosphates have been associated with several genetic diseases.

GTP-binding proteins, also known as G proteins, are a family of molecular switches present in many organisms, including humans. They play a crucial role in signal transduction pathways, particularly those involved in cellular responses to external stimuli such as hormones, neurotransmitters, and sensory signals like light and odorants.

G proteins are composed of three subunits: α, β, and γ. The α-subunit binds GTP (guanosine triphosphate) and acts as the active component of the complex. When a G protein-coupled receptor (GPCR) is activated by an external signal, it triggers a conformational change in the associated G protein, allowing the α-subunit to exchange GDP (guanosine diphosphate) for GTP. This activation leads to dissociation of the G protein complex into the GTP-bound α-subunit and the βγ-subunit pair. Both the α-GTP and βγ subunits can then interact with downstream effectors, such as enzymes or ion channels, to propagate and amplify the signal within the cell.

The intrinsic GTPase activity of the α-subunit eventually hydrolyzes the bound GTP to GDP, which leads to re-association of the α and βγ subunits and termination of the signal. This cycle of activation and inactivation makes G proteins versatile signaling elements that can respond quickly and precisely to changing environmental conditions.

Defects in G protein-mediated signaling pathways have been implicated in various diseases, including cancer, neurological disorders, and cardiovascular diseases. Therefore, understanding the function and regulation of GTP-binding proteins is essential for developing targeted therapeutic strategies.

Microsomes are subcellular membranous vesicles that are obtained as a byproduct during the preparation of cellular homogenates. They are not naturally occurring structures within the cell, but rather formed due to fragmentation of the endoplasmic reticulum (ER) during laboratory procedures. Microsomes are widely used in various research and scientific studies, particularly in the fields of biochemistry and pharmacology.

Microsomes are rich in enzymes, including the cytochrome P450 system, which is involved in the metabolism of drugs, toxins, and other xenobiotics. These enzymes play a crucial role in detoxifying foreign substances and eliminating them from the body. As such, microsomes serve as an essential tool for studying drug metabolism, toxicity, and interactions, allowing researchers to better understand and predict the effects of various compounds on living organisms.

Sphingomyelin phosphodiesterase is an enzyme that catalyzes the hydrolysis of sphingomyelin, a sphingolipid found in animal tissues, into ceramide and phosphorylcholine. This enzyme plays a crucial role in the metabolism of sphingomyelin and the regulation of cellular processes such as apoptosis, differentiation, and inflammation.

There are several isoforms of this enzyme, including acid sphingomyelinase (ASM) and neutral sphingomyelinase (NSM), which differ in their subcellular localization, regulation, and physiological functions. Deficiencies or dysfunctions in sphingomyelin phosphodiesterase activity have been implicated in various diseases, such as Niemann-Pick disease, atherosclerosis, and cancer.

Sphingomyelins are a type of sphingolipids, which are a class of lipids that contain sphingosine as a backbone. Sphingomyelins are composed of phosphocholine or phosphoethanolamine bound to the ceramide portion of the molecule through a phosphodiester linkage. They are important components of cell membranes, particularly in the myelin sheath that surrounds nerve fibers. Sphingomyelins can be hydrolyzed by the enzyme sphingomyelinase to form ceramide and phosphorylcholine or phosphorylethanolamine. Abnormalities in sphingomyelin metabolism have been implicated in several diseases, including Niemann-Pick disease, a group of inherited lipid storage disorders.

Gene expression regulation, enzymologic refers to the biochemical processes and mechanisms that control the transcription and translation of specific genes into functional proteins or enzymes. This regulation is achieved through various enzymatic activities that can either activate or repress gene expression at different levels, such as chromatin remodeling, transcription factor activation, mRNA processing, and protein degradation.

Enzymologic regulation of gene expression involves the action of specific enzymes that catalyze chemical reactions involved in these processes. For example, histone-modifying enzymes can alter the structure of chromatin to make genes more or less accessible for transcription, while RNA polymerase and its associated factors are responsible for transcribing DNA into mRNA. Additionally, various enzymes are involved in post-transcriptional modifications of mRNA, such as splicing, capping, and tailing, which can affect the stability and translation of the transcript.

Overall, the enzymologic regulation of gene expression is a complex and dynamic process that allows cells to respond to changes in their environment and maintain proper physiological function.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Prostaglandin D2 (PGD2) is a type of prostaglandin, which is a group of lipid compounds that are derived enzymatically from arachidonic acid and have diverse hormone-like effects in various tissues. PGD2 is one of the most abundant prostaglandins produced in the human body and is primarily synthesized and released by activated mast cells, which are a type of immune cell found in various tissues throughout the body.

PGD2 has a wide range of biological activities, including vasodilation, bronchoconstriction, and modulation of immune responses. It also plays important roles in regulating sleep and wakefulness, as well as in the development of allergic inflammation and other inflammatory processes. PGD2 exerts its effects by binding to specific G protein-coupled receptors, including the DP1 and CRTH2 receptors, which are expressed on various cell types throughout the body.

In addition to its role in normal physiological processes, PGD2 has also been implicated in a number of pathological conditions, including asthma, rhinitis, dermatitis, and certain types of cancer. As such, drugs that target the synthesis or action of PGD2 have been developed as potential therapeutic agents for these conditions.

Fungi, in the context of medical definitions, are a group of eukaryotic organisms that include microorganisms such as yeasts and molds, as well as the more familiar mushrooms. The study of fungi is known as mycology.

Fungi can exist as unicellular organisms or as multicellular filamentous structures called hyphae. They are heterotrophs, which means they obtain their nutrients by decomposing organic matter or by living as parasites on other organisms. Some fungi can cause various diseases in humans, animals, and plants, known as mycoses. These infections range from superficial, localized skin infections to systemic, life-threatening invasive diseases.

Examples of fungal infections include athlete's foot (tinea pedis), ringworm (dermatophytosis), candidiasis (yeast infection), histoplasmosis, coccidioidomycosis, and aspergillosis. Fungal infections can be challenging to treat due to the limited number of antifungal drugs available and the potential for drug resistance.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

I believe there may be some confusion in your question. "Rabbits" is a common name used to refer to the Lagomorpha species, particularly members of the family Leporidae. They are small mammals known for their long ears, strong legs, and quick reproduction.

However, if you're referring to "rabbits" in a medical context, there is a term called "rabbit syndrome," which is a rare movement disorder characterized by repetitive, involuntary movements of the fingers, resembling those of a rabbit chewing. It is also known as "finger-chewing chorea." This condition is usually associated with certain medications, particularly antipsychotics, and typically resolves when the medication is stopped or adjusted.

Acyltransferases are a group of enzymes that catalyze the transfer of an acyl group (a functional group consisting of a carbon atom double-bonded to an oxygen atom and single-bonded to a hydrogen atom) from one molecule to another. This transfer involves the formation of an ester bond between the acyl group donor and the acyl group acceptor.

Acyltransferases play important roles in various biological processes, including the biosynthesis of lipids, fatty acids, and other metabolites. They are also involved in the detoxification of xenobiotics (foreign substances) by catalyzing the addition of an acyl group to these compounds, making them more water-soluble and easier to excrete from the body.

Examples of acyltransferases include serine palmitoyltransferase, which is involved in the biosynthesis of sphingolipids, and cholesteryl ester transfer protein (CETP), which facilitates the transfer of cholesteryl esters between lipoproteins.

Acyltransferases are classified based on the type of acyl group they transfer and the nature of the acyl group donor and acceptor molecules. They can be further categorized into subclasses based on their sequence similarities, three-dimensional structures, and evolutionary relationships.

Octoxynol is a type of surfactant, which is a compound that lowers the surface tension between two substances, such as oil and water. It is a synthetic chemical that is composed of repeating units of octylphenoxy polyethoxy ethanol.

Octoxynol is commonly used in medical applications as a spermicide, as it is able to disrupt the membrane of sperm cells and prevent them from fertilizing an egg. It is found in some contraceptive creams, gels, and films, and is also used as an ingredient in some personal care products such as shampoos and toothpastes.

In addition to its use as a spermicide, octoxynol has been studied for its potential antimicrobial properties, and has been shown to have activity against certain viruses, bacteria, and fungi. However, its use as an antimicrobial agent is not widely established.

It's important to note that octoxynol can cause irritation and allergic reactions in some people, and should be used with caution. Additionally, there is some concern about the potential for octoxynol to have harmful effects on the environment, as it has been shown to be toxic to aquatic organisms at high concentrations.

Glycolipids are a type of lipid (fat) molecule that contain one or more sugar molecules attached to them. They are important components of cell membranes, where they play a role in cell recognition and signaling. Glycolipids are also found on the surface of some viruses and bacteria, where they can be recognized by the immune system as foreign invaders.

There are several different types of glycolipids, including cerebrosides, gangliosides, and globosides. These molecules differ in the number and type of sugar molecules they contain, as well as the structure of their lipid tails. Glycolipids are synthesized in the endoplasmic reticulum and Golgi apparatus of cells, and they are transported to the cell membrane through vesicles.

Abnormalities in glycolipid metabolism or structure have been implicated in a number of diseases, including certain types of cancer, neurological disorders, and autoimmune diseases. For example, mutations in genes involved in the synthesis of glycolipids can lead to conditions such as Tay-Sachs disease and Gaucher's disease, which are characterized by the accumulation of abnormal glycolipids in cells.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Lipase is an enzyme that is produced by the pancreas and found in the digestive system of most organisms. Its primary function is to catalyze the hydrolysis of fats (triglycerides) into smaller molecules, such as fatty acids and glycerol, which can then be absorbed by the intestines and utilized for energy or stored for later use.

In medical terms, lipase levels in the blood are often measured to diagnose or monitor conditions that affect the pancreas, such as pancreatitis (inflammation of the pancreas), pancreatic cancer, or cystic fibrosis. Elevated lipase levels may indicate damage to the pancreas and its ability to produce digestive enzymes.

Acylation is a medical and biological term that refers to the process of introducing an acyl group (-CO-) into a molecule. This process can occur naturally or it can be induced through chemical reactions. In the context of medicine and biology, acylation often occurs during post-translational modifications of proteins, where an acyl group is added to specific amino acid residues, altering the protein's function, stability, or localization.

An example of acylation in medicine is the administration of neuraminidase inhibitors, such as oseltamivir (Tamiflu), for the treatment and prevention of influenza. These drugs work by inhibiting the activity of the viral neuraminidase enzyme, which is essential for the release of newly formed virus particles from infected cells. Oseltamivir is administered orally as an ethyl ester prodrug, which is then hydrolyzed in the body to form the active acylated metabolite that inhibits the viral neuraminidase.

In summary, acylation is a vital process in medicine and biology, with implications for drug design, protein function, and post-translational modifications.

Dinoprostone is a prostaglandin E2 analog used in medical practice for the induction of labor and ripening of the cervix in pregnant women. It is available in various forms, including vaginal suppositories, gel, and tablets. Dinoprostone works by stimulating the contraction of uterine muscles and promoting cervical dilation, which helps in facilitating a successful delivery.

It's important to note that dinoprostone should only be administered under the supervision of a healthcare professional, as its use is associated with certain risks and side effects, including uterine hyperstimulation, fetal distress, and maternal infection. The dosage and duration of treatment are carefully monitored to minimize these risks and ensure the safety of both the mother and the baby.

Prostaglandin-Endoperoxide Synthases (PTGS), also known as Cyclooxygenases (COX), are a group of enzymes that catalyze the conversion of arachidonic acid into prostaglandin G2 and H2, which are further metabolized to produce various prostaglandins and thromboxanes. These lipid mediators play crucial roles in several physiological processes such as inflammation, pain, fever, and blood clotting. There are two major isoforms of PTGS: PTGS-1 (COX-1) and PTGS-2 (COX-2). While COX-1 is constitutively expressed in most tissues and involved in homeostatic functions, COX-2 is usually induced during inflammation and tissue injury. Nonsteroidal anti-inflammatory drugs (NSAIDs) exert their therapeutic effects by inhibiting these enzymes, thereby reducing the production of prostaglandins and thromboxanes.

Phosphatidylserines are a type of phospholipids that are essential components of the cell membrane, particularly in the brain. They play a crucial role in maintaining the fluidity and permeability of the cell membrane, and are involved in various cellular processes such as signal transduction, protein anchorage, and apoptosis (programmed cell death). Phosphatidylserines contain a polar head group made up of serine amino acids and two non-polar fatty acid tails. They are abundant in the inner layer of the cell membrane but can be externalized to the outer layer during apoptosis, where they serve as signals for recognition and removal of dying cells by the immune system. Phosphatidylserines have been studied for their potential benefits in various medical conditions, including cognitive decline, Alzheimer's disease, and depression.

Subcellular fractions refer to the separation and collection of specific parts or components of a cell, including organelles, membranes, and other structures, through various laboratory techniques such as centrifugation and ultracentrifugation. These fractions can be used in further biochemical and molecular analyses to study the structure, function, and interactions of individual cellular components. Examples of subcellular fractions include nuclear extracts, mitochondrial fractions, microsomal fractions (membrane vesicles), and cytosolic fractions (cytoplasmic extracts).

Secretory phospholipase A2 receptor is a protein that in humans is encoded by the PLA2R1 gene. M-type phospholipase A2 receptor ... "Structural comparison of phospholipase-A2-binding regions in phospholipase-A2 receptors from various mammals". European Journal ... Ancian P, Lambeau G, Mattéi MG, Lazdunski M (Apr 1995). "The human 180-kDa receptor for secretory phospholipases A2. Molecular ... "Mouse group X secretory phospholipase A2 induces a potent release of arachidonic acid from spleen cells and acts as a ligand ...

https://en.wikipedia.org/wiki/PLA2R1

Ancian P, Lambeau G, Mattéi MG, Lazdunski M (1995). "The human 180-kDa receptor for secretory phospholipases A2. Molecular ... Phospholipase A2, group 1B is an enzyme that in humans is encoded by the PLA2G1B gene. Phospholipase A2 (EC 3.1.1.4) catalyzes ... 1997). "Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2". J. Biol. Chem. 272 (25): ... "Characterisation and expression of secretory phospholipase A2 group IB during ontogeny of Atlantic cod ( Gadus morhua)". Br J ...

https://en.wikipedia.org/wiki/PLA2G1B

180 Kd secretory phospholipase A2 receptor; DEC-205 receptor; 72 Kd and 92 Kd type IV collagenase (EC 3.4.24.24); and ... "Cloning and expression of a membrane receptor for secretory phospholipases A2". J. Biol. Chem. 269 (3): 1575-1578. doi:10.1016/ ... BSP-A1/A2) and BSP-A3; cation-independent mannose-6-phosphate receptor; mannose receptor of macrophages; ...

https://en.wikipedia.org/wiki/Fibronectin_type_II_domain

January 2011). "Secretory phospholipase AA2 pathway during pediatric acute respiratory distress syndrome: a preliminary study ... There are also prokaryotic A2 phospholipases. Additional types of phospholipases include phospholipase A1, phospholipase B, ... phospholipase C, and phospholipase D. Phospholipases A2 include several unrelated protein families with common enzymatic ... There are atypical members of the phospholipase A2 family, such as PLA2G12B, that have no phospholipase activity with typical ...

https://en.wikipedia.org/wiki/Phospholipase_A2

The otoconin-90 contains two secretory phospholipase A2 (sPLA2) domains. sPLA2 has a rigid structure with eight disulfide bonds ...

https://en.wikipedia.org/wiki/Otoconin

"Entrez Gene: PLA2G5 phospholipase A2, group V". Otha, Shin (15 June 2013). "Group V secretory phospholipase A2 is involved in ... This gene is a member of the secretory phospholipase A2 family. It is located in a tightly-linked cluster of secretory ... 2003). "Human group V phospholipase A2 induces group IVA phospholipase A2-independent cysteinyl leukotriene synthesis in human ... V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2 ...

https://en.wikipedia.org/wiki/PLA2G5

Group 10 secretory phospholipase A2 is an enzyme that in humans is encoded by the PLA2G10 gene. ENSG00000069764 GRCh38: Ensembl ... 2000). "Mouse group X secretory phospholipase A2 induces a potent release of arachidonic acid from spleen cells and acts as a ... 2002). "Potent modification of low density lipoprotein by group X secretory phospholipase A2 is linked to macrophage foam cell ... 2000). "Identification of group X secretory phospholipase A(2) as a natural ligand for mouse phospholipase A(2) receptor". FEBS ...

https://en.wikipedia.org/wiki/PLA2G10

... is an inhibitor of the IIa, V, and X isoforms of secretory phospholipase A2 (sPLA2). The molecule acts as an anti- ... Rosenson RS, Elliott M, Stasiv Y, Hislop C (April 2011). "Randomized trial of an inhibitor of secretory phospholipase A2 on ... October 2005). "Circulating secretory phospholipase A2 activity predicts recurrent events in patients with severe acute ... Rosenson RS, Elliott M, Stasiv Y, Hislop C (April 2011). "Randomized trial of an inhibitor of secretory phospholipase A2 on ...

https://en.wikipedia.org/wiki/Varespladib

1995). "The secretory phospholipase A2 gene is a candidate for the Mom1 locus, a major modifier of ApcMin-induced intestinal ... Phospholipase A2, membrane associated is an enzyme that in humans is encoded by the PLA2G2A gene. Phospholipase A2 GRCh38: ... Ancian P, Lambeau G, Mattéi MG, Lazdunski M (1995). "The human 180-kDa receptor for secretory phospholipases A2. Molecular ... 1995). "Structure-based design of the first potent and selective inhibitor of human non-pancreatic secretory phospholipase A2 ...

https://en.wikipedia.org/wiki/PLA2G2A

"Bimodal regulatory effect of melittin and phospholipase A2-activating protein on human type II secretory phospholipase A2". ... PLAA phospholipase A2-activating protein". Clark MA, Ozgür LE, Conway TM, et al. (1991). "Cloning of a phospholipase A2- ... Phospholipase A-2-activating protein is an enzyme that in humans is encoded by the PLAA gene. GRCh38: Ensembl release 89: ... Ruiz A, Nadal M, Puig S, Estivill X (1999). "Cloning of the human phospholipase A2 activating protein (hPLAP) gene on the ...

https://en.wikipedia.org/wiki/Phospholipase_A-2-activating_protein

Group XIIA secretory phospholipase A2 is an enzyme that in humans is encoded by the PLA2G12A gene. GRCh38: Ensembl release 89: ... "Entrez Gene: PLA2G12A phospholipase A2, group XIIA". Schröder HC, Perovic S, Kavsan V, et al. (1998). "Mechanisms of prionSc- ... 2003). "Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII)". J. Biol ... 1997). "HIV and SIV envelope glycoproteins induce phospholipase A2 activation in human and macaque lymphocytes". J. Acquir. ...

https://en.wikipedia.org/wiki/PLA2G12A

Group IID secretory phospholipase A2 is an enzyme that in humans is encoded by the PLA2G2D gene. GRCh38: Ensembl release 89: ... 2006). "A novel polymorphism in secretory phospholipase A2-IID is associated with body weight loss in chronic obstructive ... Lindbom J, Ljungman AG, Tagesson C (2007). "Interferon gamma-induced gene expression of the novel secretory phospholipase A2 ... "Increased hepatic cholesterol accumulation in transgenic mice overexpressing human secretory phospholipase A2 group IIA". ...

https://en.wikipedia.org/wiki/PLA2G2D

Human Paneth cells also produce other AMPs including lysozyme, secretory phospholipase A2, and regenerating islet-derived ... and phospholipase A2 is an enzyme specialized in the lysis of bacterial phospholipids . This battery of secretory molecules ... it has been shown that lysozyme can be rerouted through secretory autophagy. In secretory autophagy, cargo is transported in an ... does not cause Golgi breakdown and therefore does not trigger the secretory autophagy of lysozyme. A dysfunction in secretory ...

https://en.wikipedia.org/wiki/Paneth_cell

J Biol Chem 271:24794-24799, 1996 Kolko M, DeCoster MA, Rodriguez de Turco EB, Bazan NG: Synergy by secretory phospholipase A2 ... Glutamate signaling and secretory phospholipase A2 modulate the release of arachidonic acid from neuronal membrane. J Neurosi ... Secretory phospholipase A2 potentiates glutamate-induced rat striatal neuronal cell death in vivo. Neurosci Letters 274:167-170 ... the Bazan laboratory demonstrated that secretory phospholipase A2 modulates neuronal survival and glutamate transmission. Then ...

https://en.wikipedia.org/wiki/Nicolas_Bazan

The pancreas also secretes phospholipase A2, lysophospholipase, and cholesterol esterase. The precursor zymogens, are inactive ... The cells are filled with secretory granules containing the precursor digestive enzymes. The major proteases, the pancreatic ...

https://en.wikipedia.org/wiki/Human_digestive_system

... type III Phospholipase A2), and 23-25 kilodaltons (cysteine-rich secretory proteins and kallikrein) in these secretions. ...

https://en.wikipedia.org/wiki/Lace_monitor

... is freed from phospholipid by hydrolysis, catalyzed by the phospholipase A2 (PLA2). Arachidonic acid for ... whereas inflammatory arachidonic acid is generated by the action of a low-molecular-weight secretory PLA2 (sPLA2, 14-18 kDa). ... signaling purposes appears to be derived by the action of group IVA cytosolic phospholipase A2 (cPLA2, 85 kDa), ... Alternatively, arachidonic acid may be cleaved from phospholipids after phospholipase C (PLC) cleaves off the inositol ...

https://en.wikipedia.org/wiki/Arachidonic_acid

... group I phospholipase A2 (PLA2) and one cobra venom factor (CVF) gene. These major toxin gene families in the Indian cobra are ... These included families like three-finger toxins (3FTxs), snake venom metalloproteinases (SVMP), cysteine-rich secretory venom ... phospholipases, L-amino acid oxidase (LAAO), vascular endothelial growth factor (VEGF) and 5' nucleotidases. This ... two venom Kunitz serine proteases and a cysteine-rich secretory venom protein. Additionally to these VSTs, other accessory ...

https://en.wikipedia.org/wiki/Indian_cobra

... a neurotoxic phospholipase A2". FEBS Lett. 445 (2-3): 440-4. doi:10.1016/S0014-5793(99)00177-5. PMID 10094503. S2CID 40129100. ... 1999). "Human calumenin localizes to the secretory pathway and is secreted to the medium". Exp. Cell Res. 248 (2): 473-81. doi: ...

https://en.wikipedia.org/wiki/Calumenin

... interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2". The Journal of Biological Chemistry. 272 ( ... Creutz CE, Moss S, Edwardson JM, Hide I, Gomperts B (Apr 1992). "Differential recognition of secretory vesicles by annexins. ... Kwon M, MacLeod TJ, Zhang Y, Waisman DM (Jan 2005). "S100A10, annexin A2, and annexin a2 heterotetramer as candidate ... interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2". The Journal of Biological Chemistry. 272 ( ...

https://en.wikipedia.org/wiki/S100A10

... while the reaction at the sn-2 position is catalyzed by phospholipase A2. Outer membrane phospholipase A1 Phospholipase+A1 at ... "High-level secretory production of phospholipase A1 by Saccharomyces cerevisiae and Aspergillus oryzae". Biosci Biotechnol ... Franson R, Waite M, LaVia M (May 1971). "Identification of phospholipase A1 and A2 in the soluble fraction of rat liver ... "Characterization of phospholipase A1, A2, C activity in Ureaplasma urealyticum membranes". Mol. Cell. Biochem. 201 (1-2): 159- ...

https://en.wikipedia.org/wiki/Phospholipase_A1

Cytosolic phospholipase A2 gamma is an enzyme that in humans is encoded by the PLA2G4C gene. GRCh38: Ensembl release 89: ... Lindbom J, Ljungman AG, Lindahl M, Tagesson C (2003). "Increased gene expression of novel cytosolic and secretory phospholipase ... "Entrez Gene: PLA2G4C phospholipase A2, group IVC (cytosolic, calcium-independent)". Schröder HC, Perovic S, Kavsan V, et al. ( ... Underwood KW, Song C, Kriz RW, Chang XJ, Knopf JL, Lin LL (Sep 1998). "A novel calcium-independent phospholipase A2, cPLA2- ...

https://en.wikipedia.org/wiki/PLA2G4C

... encoding protein Phospholipase A2 group IVD PLA2G4E: encoding protein Phospholipase A2 group IVE PML: promyelocytic leukemia ... encoding protein Secretory carrier-associated membrane protein 2 SCAMP5: encoding protein Secretory carrier-associated membrane ...

https://en.wikipedia.org/wiki/Chromosome_15

2002). "Lys 43 and Asp 46 in alpha-helix 3 of uteroglobin are essential for its phospholipase A2 inhibitory activity". Biochem ... "Clara cell secretory protein deficiency alters clara cell secretory apparatus and the protein composition of airway lining ... Note: UGB is itself progesterone induced gene in the endometrium in Lagomorphs) Inhibits phospholipase A2 in vitro Binds ... 2001). "A two-receptor pathway for catabolism of Clara cell secretory protein in the kidney". J. Biol. Chem. 276 (16): 13295- ...

https://en.wikipedia.org/wiki/Uteroglobin

April 2012). "Circulating phospholipase-A2 activity in obstructive sleep apnea and recurrent tonsillitis". International ... These germinal centers are places where B memory cells are created and secretory antibody (IgA) is produced. The palatine ... "The Adenoids but Not the Palatine Tonsils Serve as a Reservoir for Bacteria Associated with Secretory Otitis Media in Small ...

https://en.wikipedia.org/wiki/Tonsil

... binds to the substrate of phospholipase A2, the phosphatidylethanolamine (PE) with a high specificity at a 1:1 ratio ... protease is absent in the gene cluster and hence the sequence is recognized by type I signal peptidase of the general secretory ... the activity of phospholipase A2, proliferation of herpes simplex virus, prostaglandin, and leucotriene biosynthesis. Further ...

https://en.wikipedia.org/wiki/Cinnamycin

Lipocortins suppress phospholipase A2. Increased expression of the gene coding for annexin-1 is one of the mechanisms by which ... Donnelly SR, Moss SE (June 1997). "Annexins in the secretory pathway". Cell. Mol. Life Sci. 53 (6): 533-8. doi:10.1007/ ... However some annexins (Annexin A1, Annexin A2, and Annexin A5) can be secreted from the cytoplasm to outside cellular ... there is evidence of the annexin like proteins being involved in the positioning and attachment of secretory organelles in the ...

https://en.wikipedia.org/wiki/Annexin

... of phospholipase D is independent of activation of polyphosphoinositide-specific phospholipase C and phospholipase A2". The ... It is primarily present at the Golgi complex, endosomes, lysosomes, and secretory granules. Upon the binding of an ... Mammalian cells encode two isoforms of phospholipase D: PLD1 and PLD2. Phospholipase D is an important player in many ... Phosphatidyl choline Phosphatidate Choline Phospholipase cleavage sites Jenkins GM, Frohman MA (October 2005). "Phospholipase D ...

https://en.wikipedia.org/wiki/Phospholipase_D

Recently, CD36 was linked to store-operated calcium flux, phospholipase A2 activation, and production of prostaglandin E2 CD36 ... associated secretory phenotype (SASP). This secretory molecule production leads to the onset of a comprehensive senescent cell ... phospholipase A2 activation, and production of prostaglandin E2". The Journal of Biological Chemistry. 286 (20): 17785-95. doi: ... 2018). "CD36 initiates the secretory phenotype during the establishment of cellular senescence". EMBO Reports. 19 (6). doi: ...

https://en.wikipedia.org/wiki/CD36

Enzymes secreted involved in the digestion of fats include lipase, phospholipase A2, lysophospholipase, and cholesterol ... Islets are composed of up to 3,000 secretory cells, and contain several small arterioles to receive blood, and venules that ...

https://en.wikipedia.org/wiki/Pancreas

Showing Protein Group XIIB secretory phospholipase A2-like protein (HMDBP00062). IdentificationBiological propertiesGene ... Group XIIB secretory phospholipase A2-like protein MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK ... Rouault M, Bollinger JG, Lazdunski M, Gelb MH, Lambeau G: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic ...

https://hmdb.ca/proteins/HMDBP00062

Synthesis and evaluation of trimethoxyphenyl isoxazolidines as inhibitors of secretory phospholipase A2 with anti-inflammatory ... Synthesis and evaluation of trimethoxyphenyl isoxazolidines as inhibitors of secretory phospholipase A2 with anti-inflammatory ... synthesized and evaluated in vitro and in vivo for their inhibitory activity against purified group I and II phospholipase A2 ( ...

http://eprints.uni-mysore.ac.in/7916/

Refining the value of secretory phospholipase A2 as a predictor of acute chest syndrome in sickle cell disease: results of a ...

https://emedicine.medscape.com/article/205926-overview

The Role of Secretory Phospholipase A2 (sPLA2) Inhibitor Varespladib in Mitigation of Acetaminophen(APAP) Induced Acute Liver ... The Role of Secretory Phospholipase A2 (sPLA2) Inhibitor Varespladib in Mitigation of Acetaminophen(APAP) Induced Acute Liver ...

https://digitalcommons.pcom.edu/research_day/research_day_GA_2017/researchga2017/21/

Thesis Title: Investigating the functions of Phospholipase C-1, Ca2+/H+ exchanger, and Secretory Phospholipase A2 in growth, ... Investigating the functions of Phospholipase C-1, Ca2+/H+ exchanger, and Secretory Phospholipase A2 in growth, stress responses ... Investigating the functions of Phospholipase C-1, Ca2+/H+ exchanger, and Secretory Phospholipase A2 in growth, stress responses ...

http://gyan.iitg.ernet.in/handle/123456789/2382

https://en.wikipedia.org/wiki/PLA2R1

... is one of the most potent enzymes of the phospholipase A(2) lipolytic enzyme superfamily. Its high catalytic activity toward ... Macrophage secretory phospholipase A2 group X enhances anti-inflammatory responses, promotes lipid accumulation, and ... Macrophage secretory phospholipase A2 group X enhances anti-inflammatory responses, promotes lipid accumulation, and ... Secreted phospholipase A2 group X (sPLA(2)-X) is one of the most potent enzymes of the phospholipase A(2) lipolytic enzyme ...

https://www.immunology.ox.ac.uk/publications/9611?40b6a1c4-945a-11ee-8d90-061b866677b4

Group IIE secretory phospholipase A2. MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGG.... unknown. Lactotransferrin. ...

https://www.rcsb.org/ligand/NIM

Angiopoietins, vascular endothelial growth factors and secretory phospholipase A2 in ischemic and non-ischemic heart failure. J ...

https://www.nature.com/articles/s41467-022-34971-6?error=cookies_not_supported&code=ec939931-fea8-4f56-ac1b-31900025238d

Mice lacking secretory phospholipase A2 show altered apoptosis and differentiation with Helicobacter felis infection. ... RSPO3 controls secretory cell differentiation in corpus glands. (A) qPCR for expression of Rspo1-4 in Bl6 mice (n = 4). (B) ISH ... R-spondin-3 induces secretory, antimicrobial LGR5+ cells in the stomach. Nat Cell Biol. 2019;21(7):812-823.. View this article ... This response enabled a rapid recovery of the injured secretory gland cells. However, in the context of chronic H. pylori ...

https://www.jci.org/articles/view/151363

A sub-family of Phospholipase A2, similar to human group III PLA2 ... PLA2_group_III_like: A sub-family of Phospholipase A2, similar ... PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically ...

https://www.ncbi.nlm.nih.gov/Structure/cdd/cd04705

Acidic calcium-independent phospholipase A2; aiPLA2; Antioxidant protein 2; epididymis secretory sperm binding protein Li 128m ...

https://www.thermofisher.com/antibody/product/PRDX6-Antibody-Polyclonal/13585-1-AP

Jameel, N. M., Shekhar, M. A., and Vishwanath, B. S. Alpha-lipoic acid: an inhibitor of secretory phospholipase A2 with anti- ...

https://medlineplus.gov/druginfo/natural/767.html

180 Kd secretory phospholipase A2 receptor [ (PUBMED:8294398) ]. DEC-205 receptor [ (PUBMED:7753172) ]; 72 Kd and 92 Kd type IV ... and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the ... BSP-A1/A2) and BSP-A3 [ (PUBMED:3606570) ]; cation-independent mannose-6-phosphate receptor [ (PUBMED:1323236) ]; mannose ...

https://smart.embl.de/smart/do_annotation.pl?DOMAIN=FN2&START=1889&END=1935&E_VALUE=9.51e-26&TYPE=SMART&BLAST=ETDDGEPCVFPFIYKGKSYDECVLEGRAKLWCSKTANYDRDHEWGFC

Cerebrospinal fluid secretory Ca2+-dependent phospholipase A2 activity is increased in Alzheimer disease. ... BACKGROUND: The phospholipase A(2) (PLA2) family comprises multiple isoenzymes that vary in their physicochemical properties, ... in 2 CSF samples and for recombinant secretory Ca(2+)-dependent PLA2 (sPLA2) in concentrations ranging from 0.25 to 1 micromol/ ...

https://swepub.kb.se/hitlist?f=&q=L773%3A0009+9147+OR+L773%3A1530+8561&r=&m=10&s=r&t=v&d=swepub&p=2

Clinical and biological role of secretory phospholipase A2 in acute respiratory distress syndrome infants. Crit Care 2013;17: ... Lysophospholipid and fatty acid inhibition of pulmonary surfactant: nonenzymatic models of phospholipase A2 surfactant ...

https://fn.bmj.com/content/101/6/F565

Secretory phospholipase A2 generates the novel lipid mediator lysophosphatidic acid in membrane microvesicles shed from ... microparticles provide a preferential substrate for non-pancreatic secretory phospholipase A2 and thus a source of ... thromboxane A2) that can promote prothrombotic responses [22]. Therefore, microparticles can promote thrombin generation in ...

https://erj.ersjournals.com/content/42/1/272

Snake venom metalloproteinase family, serine proteases and phospholipase A2 were among the most represented proteins. Each ... followed by serine proteinases and phospholipase A2. Moreover, L-amino acid oxidase, cysteine-rich secretory protein (CRISP), 5 ... phospholipases A2 (PLA2) and serine proteinases54,55, as well as the non-enzymatic peptide myotoxins, C-type lectins, cysteine- ... The presence of vesicles in the luminal face of secretory cells of snake venom glands has been observed since 197331 and three ...

https://www.nature.com/articles/s41598-018-30578-4?error=cookies_not_supported&code=995594c0-1fc6-4339-bbaf-038bab8962d2

D. De Luca, A. Minucci, E. Zecca et al., "Bile acids cause secretory phospholipase A2 activity enhancement, revertible by ... Recently, bile acid was found to cause surfactant inactivation by enhancing the activity of secretory phospholipase A2 (sPLA2) ... showed that bile acids cause surfactant inactivation by enhancing the activity of secretory phospholipase A2 (sPLA2), a key ... in acute lung injury is mediated by type-II phospholipase A2 and inhibited by a direct surfactant protein A-phospholipase A2 ...

https://www.hindawi.com/journals/ije/2014/308274/

Neutralization of inflammation by inhibiting in vitro and in vivo secretory phospholipase A2 by ethanol extract of Boerhaavia ...

https://www.degruyter.com/document/doi/10.1515/jcim-2020-0390/html

... is a protein secreted by Clonorchis sinensis and is a component of excretory and secretory products (CsESPs). Phospholipase A2 ... Secreted phospholipase A2 (sPLA2) is a protein secreted by Clonorchis sinensis and is a component of excretory and secretory ... Hu F, Hu X, Ma C, Zhao J, Xu J, Yu X. Molecular characterization of a novel Clonorchis sinensis secretory phospholipase A2 and ... Secreted phospholipase A2 (sPLA2) is a protein secreted by C. sinensis and is a component of CsESPs. sPLA2 enzymes, ...

https://parasitesandvectors.biomedcentral.com/articles/10.1186/s13071-017-2082-z

This gene encodes a member of the phospholipase A2 family of proteins. Alternative splicing results in multiple transcript ... Phospholipase. / Group 10 Secretory Phospholipase A2. DTO Classes. Protein. / Enzyme. / Hydrolase. / Lipase. / Phospholipase. ... This gene encodes a member of the phospholipase A2 family of proteins. Alternative splicing results in multiple transcript ...

https://pharos.nih.gov/targets/PLA2G10

Group XII secretory phospholipase A2 precursor. Phospholipase A2 domain superfamily. Phospholipase A2, histidine active site. ... phospholipase A2, group XIIA Symbol. pla2g12a Nomenclature History Previous Names. *PLA2 group XII (1) ... Predicted to enable phospholipase A2 activity. Predicted to act upstream of or within arachidonic acid secretion; lipid ... Orthologous to human PLA2G12A (phospholipase A2 group XIIA). Genome Resources. *Alliance (1) ...

http://zfin.org/ZDB-GENE-070410-18

The role of group IIA secretory phospholipase A2 (sPLA2-IIA) as a biomarker for the diagnosis of sepsis and bacterial infection ... including soluble phospholipase A2, N-acyl phosphatidylethanolamine-specific phospholipase D and lysophospholipase D (31-33). ... Minami T, Tojo H, Shinomura Y, Tarui S, Okamoto M. Raised serum activity of phospholipase A2 immunochemically related to group ... The generation of 2-AG may also be stimulated by Ca2+−dependent phospholipase C, the first enzyme in the 2-AG biosynthesizing ...

https://www.frontiersin.org/articles/10.3389/fvets.2021.655311/full

The intrinsic overexpression of secretory phospholipase A2 (sPLA2) in various pro-inflammatory diseases and cancers has the ... The intrinsic overexpression of secretory phospholipase A2 (sPLA2) in various pro-inflammatory diseases and cancers has the ... Molecular interactions of phospholipid monolayers with a model phospholipase P. Zhang, V. Villanueva, J. Kalkowski, C. Liu, A. ...

https://pubs.rsc.org/en/content/articlelanding/2019/sm/c8sm01154k/unauth

... the phospholipase A2 (PLA2), interleukin (IL)-6 and tumor necrosis factor (TNF)-α mRNA expression levels, the secretory PLA2 ( ...

https://www.iasp-pain.org/publications/pain-research-forum/papers-of-the-week/paper/125213-effects-swimming-pain-and-inflammatory-factors-rats-lumbar-disc-herniation/

140.Bae, J.-S., et al., Thrombin and activated protein C inhibit the expression of secretory group IIA phospholipase A2 in the ... 52.Shim, J. H., Clinical application of a2-d ligand. Hanyang Med Rev 2011, ;31:55-62.. 53.Nasser, K., et al., Twice daily ...

https://ndltd.ncl.edu.tw/cgi-bin/gs32/gsweb.cgi/login?o=dnclcdr&s=id=%22109NCHU5061013%22.&searchmode=basic

Título: Group V secretory phospholipase A2 impairs endothelial protein C receptor-dependent protein C activation and ... lipid exchange as a regulatory mechanism of EPCR activity driven by the endothelially expressed secretory group V phospholipase ... by the action of groupV secretory phospholipaseA2 (sPLA2-V), an enzyme that is upregulated in a variety of inflammatory ...

https://www.unav.edu/web/investigacion/nuestros-investigadores/detalle-investigadores-cv?investigadorId=58089&investigador=Jos%EF%BF%BD%EF%BF%BD%20Mar%EF%BF%BD%EF%BF%BDa%20Hermida%20Santos

Recently, bile acid was found to cause surfactant inactivation by enhancing the activity of secretory phospholipase A2 (sPLA2) and induce inflammatory response of fetal lung [ 5 , 8 ]. (hindawi.com)
Secreted phospholipase A2 (sPLA2) is a protein secreted by Clonorchis sinensis and is a component of excretory and secretory products ( Cs ESPs). (biomedcentral.com)
On days 0, 7, 14 and 28 following surgery, the changes in the post-limb mechanical claw threshold, the phospholipase A2 (PLA2), interleukin (IL)-6 and tumor necrosis factor (TNF)-α mRNA expression levels, the secretory PLA2 (sPLA2) expression, the IL-6 and TNF-α content, the nuclear factor (NF)-κBp65 protein expression level in the nucleus pulposus, and the apoptotic rate of the nucleus pulposus cells were detected. (iasp-pain.org)
Plant secretory phospholipase A2 (sPLA2) is a family of lipolytic enzymes involved in the sn-2 hydrolysis of phospholipid carboxyester bonds, characterized by the presence of a conserved PA2c domain. (cas.cz)
The aim of this study was to evaluate the presence of type-II secretory phospholipase A2 (sPLA2-IIA) in alveolar space and its possible role in the destruction of surfactant in three rat models of acute lung injury. (hal.science)
Secretory phospholipase A2 (SPLA2) catalyzes the calcium-dependent 2-acyl groups hydrolysis to produce 3-sn-phosphoglycerides. (bvsalud.org)

A series of trimethoxyphenyl isoxazolidine derivatives, 5a(i-v) and 5b(i-v), bearing different constituents at the 5th position of the isoxazolidine ring were synthesized and evaluated in vitro and in vivo for their inhibitory activity against purified group I and II phospholipase A2 (PLA2) enzymes from snake venom and human inflammatory synovial fluid. (uni-mysore.ac.in)
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. (nih.gov)
We described a novel PA2c-containing gene family present in all plant lineages and lacking secretory peptide, which we termed PLA2-like. (cas.cz)
The level of lipoprotein-associated phospholipase A2 (LP-PLA2) in serum is independently correlated to coronary artery diseases (CAD). (biomedcentral.com)

Secreted phospholipase A2 group X (sPLA(2)-X) is one of the most potent enzymes of the phospholipase A(2) lipolytic enzyme superfamily. (ox.ac.uk)
The intrinsic overexpression of secretory phospholipase A2 (sPLA 2 ) in various pro-inflammatory diseases and cancers has the potential to be exploited as a therapeutic strategy for diagnostics and treatment. (rsc.org)
Secreted phospholipases A 2 (sPLA 2 s) participate in a very broad spectrum of biological processes through their enzymatic activity and as ligands for membrane and soluble receptors. (ijbs.com)
Secreted phospholipases A 2 (sPLA 2 s) (EC 3.1.1.4) are a structurally related group of low-molecular-mass enzymes (14-18 kDa) that catalyse the hydrolysis of glycerophospholipids (phospholipids hereafter) at their sn -2 position, to produce lysophospholipids and free fatty acids. (ijbs.com)
Secreted phospholipase A 2 -IIA (sPLA 2 -IIA) hydrolyzes phospholipids to liberate lysophospholipids and fatty acids. (elsevierpure.com)

Secretory phospholipase A2 receptor is a protein that in humans is encoded by the PLA2R1 gene. (wikipedia.org)
Bimodal regulatory effect of melittin and phospholipase A2-activating protein on human type II secretory phospholipase A2. (stfc.ac.uk)

Ivanušec A, Šribar J, Križaj I. Secreted Phospholipases A 2 - not just Enzymes: Revisited. (ijbs.com)
BACKGROUND/AIM: Phospholipases A2 represent a family of enzymes that regulate the metabolism of phospholipids by hydrolyzing them into fatty acids. (bvsalud.org)

Linkage analysis located Mom1 on chromosome 4, and further investigation identified secretory phospholipase A2 (Pla2g2a) as a candidate gene. (ox.ac.uk)

Group V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2. (uchicago.edu)

Exploring the binding mechanism and kinetics of Piperine with snake venom secretory Phospholipase A2. (edu.in)

Macrophage secretory phospholipase A2 group X enhances anti-inflammatory responses, promotes lipid accumulation, and contributes to aberrant lung pathology. (ox.ac.uk)

Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. (embl.de)

Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. (icr.ac.uk)

Rouault M, Bollinger JG, Lazdunski M, Gelb MH, Lambeau G: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity. (hmdb.ca)
Orthologous to human PLA2G12A (phospholipase A2 group XIIA). (zfin.org)
Group V phospholipase A2 mediates barrier disruption of human pulmonary endothelial cells caused by LPS in vitro. (uchicago.edu)
Quantitation of secretory group V phospholipase A(2) in human tissues by sandwich enzyme-linked immunosorbent assay. (uchicago.edu)
Characterization of monoclonal antibodies specific for 14-kDa human group V secretory phospholipase A2 (hVPLA2). (uchicago.edu)

This gene encodes a member of the phospholipase A2 family of proteins. (nih.gov)

Predicted to enable phospholipase A2 activity. (zfin.org)

Phospholipase A2 is well known for its role in liver fibrosis and inhibition of tumour cells. (biomedcentral.com)

M-type phospholipase A2 receptor is the major antigen in idiopathic membranous nephropathy attributed to over 70% of cases. (wikipedia.org)

Members of this group bind specifically to PHOSPHOLIPASE A2 RECEPTORS . (online-medical-dictionary.org)
In addition specific PHOSPHOLIPASE A2 RECEPTORS can bind to and internalize the enzymes. (nih.gov)
Members of this group have specificity for PHOSPHOLIPASE A2 RECEPTORS . (nih.gov)

Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. (prospecbio.com)
A variety of activities are associated with uteroglobin including the sequestering of hydrophobic ligands and the inhibition of SECRETORY PHOSPHOLIPASE A2. (bvsalud.org)

Less abundant, but still representative, were cysteine-rich secretory proteins, L-amino-acid oxidases, phospholipases A2, venom 5'-nucleotidase and a serine peptidase inhibitor. (fapesp.br)

We sought to investigate if mast cell activation and increases in secretory sPLA2s are associated with an increase in PAF and occurrence of dengue haemorrhagic fever (DHF). (ox.ac.uk)

Association between serum secretory phospholipase A2 and risk of ischemic stroke. (medscape.com)

9. Targeting the COX1/2-Driven thromboxane A2 pathway suppresses Barrett's esophagus and esophageal adenocarcinoma development. (nih.gov)
It inhibits prostaglandin synthesis, which prevents formation of platelet-aggregating thromboxane A2. (medscape.com)

A secreted phospholipase A2 subtype that contains a interfacial-binding region with specificity for PHOSPHATIDYLCHOLINE . (online-medical-dictionary.org)

Pedada, Synthesis of new secretory phospholipase A2-inhibitory indole containing isoxazole derivatives as anti-inflammatory and anticancer agents, Eur. (dntb.gov.ua)

Phospholipases and acetylcholinesterases are members of the subclass of esterases. (axonmedchem.com)

M-type phospholipase A2 receptor is the major antigen in idiopathic membranous nephropathy attributed to over 70% of cases. (wikipedia.org)
The human 180-kDa receptor for secretory phospholipases A2. (wikipedia.org)
Negative regulation of urokinase receptor activity by a GPI-specific phospholipase C in breast cancer cells van Veen M, Matas-Rico E, van de Wetering K, Leyton-Puig D, Kedziora K, et. (leica-microsystems.com)

1] Properties and Regulation of Cytosolic Phospholipase A2. (axonmedchem.com)

Lipoprotein-associated phospholipase A 2 (Lp-PLA2), a member of the phospholipase superfamily, is an enzyme produced by monocytes and macrophages, T cells, and mast cells. (nih.gov)

CDP-choline Significantly Restores Phoshatidylcholine Levels by Differentially Affecting Phospholipase A2 and CTP:Phosphocholine Cytidylyltransferase after Stroke. (nih.gov)

Anatomy9

Organisms14

Diseases1

Chemicals and Drugs87

Analytical, Diagnostic and Therapeutic Techniques and Equipment6

Phenomena and Processes17

Technology, Industry, Agriculture2

Information Science2

Induction of ectopic olfactory structures and bone morphogenetic protein inhibition by Rossy, a group XII secreted phospholipase A2. (1/94)

Molecular basis of phospholipase A2 activity toward phospholipids with sn-1 substitutions. (2/94)

Secreted phospholipase A2 group X overexpression in asthma and bronchial hyperresponsiveness. (3/94)

Liquid-liquid immiscibility in model membranes activates secretory phospholipase A2. (4/94)

Jak2 dampens the induction by IL-1beta of prostaglandin endoperoxide H synthase 2 expression in human orbital fibroblasts: evidence for divergent influence on the prostaglandin E2 biosynthetic pathway. (5/94)

Honeybee venom secretory phospholipase A2 induces leukotriene production but not histamine release from human basophils. (6/94)

Antibacterial actions of secreted phospholipases A2. Review. (7/94)

Effects of cholesterol on physical properties of human erythrocyte membranes: impact on susceptibility to hydrolysis by secretory phospholipase A2. (8/94)

Phospholipases

Phospholipases A

Phospholipases A2

Phospholipases A1

Group II Phospholipases A2

Type C Phospholipases

Group X Phospholipases A2

Phospholipases A2, Secretory

Group I Phospholipases A2

Lysophospholipase

Group V Phospholipases A2

Snake Venoms

Phospholipase D

Crotalid Venoms

Receptors, Phospholipase A2

Group VI Phospholipases A2

Cobra Venoms

Group IV Phospholipases A2

Viperidae

Bothrops

Reptilian Proteins

Phospholipids

Viper Venoms

Crotoxin

Group III Phospholipases A2

Elapid Venoms

Phosphatidylcholines

Elapidae

Arachidonic Acid

Phospholipases A2, Cytosolic

Phospholipases A2, Calcium-Independent

Hydrolysis

Bee Venoms

Group IA Phospholipases A2

Phospholipase A2 Inhibitors

Phosphatidylinositols

Phosphatidylinositol Diacylglycerol-Lyase

Snakes

Phosphatidic Acids

Isoenzymes

Amino Acid Sequence

Calcium

Bacillus cereus

Crotalus

Phosphatidylethanolamines

Substrate Specificity

Pancreas

Kinetics

Quinacrine

Membrane Lipids

Trimeresurus

Arachidonic Acids

Molecular Sequence Data

Phosphoinositide Phospholipase C

Pyrones

Lysophosphatidylcholines

Group IB Phospholipases A2

Enzyme Activation

Diglycerides

Thiones

Russell's Viper

Cytosol

Glycerophospholipids

Hydrogen-Ion Concentration

Butanols

Micelles

Phospholipase C beta

Indolizidines

Lysophospholipids

Clostridium perfringens

Cell Membrane

Lysosomes

Bridged Compounds

Eicosanoids

Glycosylphosphatidylinositols

1-Butanol

Venoms

Phosphatidylglycerols

Fluoroimmunoassay

Neomycin