An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
Tartrates are salts or esters of tartaric acid, primarily used in pharmaceutical industry as buffering agents, and in medical laboratories for the precipitation of proteins.
An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.
A phosphoprotein phosphatase subtype that is comprised of a catalytic subunit and two different regulatory subunits. At least two genes encode isoforms of the protein phosphatase catalytic subunit, while several isoforms of regulatory subunits exist due to the presence of multiple genes and the alternative splicing of their mRNAs. Protein phosphatase 2 acts on a broad variety of cellular proteins and may play a role as a regulator of intracellular signaling processes.
A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions.
A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.
An enzyme that catalyzes the conversion of D-glucose 6-phosphate and water to D-glucose and orthophosphate. EC 3.1.3.9.
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)
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
A phosphomonoesterase involved in the synthesis of triacylglycerols. It catalyzes the hydrolysis of phosphatidates with the formation of diacylglycerols and orthophosphate. EC 3.1.3.4.
Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods.
A gland in males that surrounds the neck of the URINARY BLADDER and the URETHRA. It secretes a substance that liquefies coagulated semen. It is situated in the pelvic cavity behind the lower part of the PUBIC SYMPHYSIS, above the deep layer of the triangular ligament, and rests upon the RECTUM.
A large multinuclear cell associated with the BONE RESORPTION. An odontoclast, also called cementoclast, is cytomorphologically the same as an osteoclast and is involved in CEMENTUM resorption.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
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 sub-class of protein tyrosine phosphatases that contain an additional phosphatase activity which cleaves phosphate ester bonds on SERINE or THREONINE residues that are located on the same protein.
A subtype of non-receptor protein tyrosine phosphatases that contain two SRC HOMOLOGY DOMAINS. Mutations in the gene for protein tyrosine phosphatase, non-receptor type 11 are associated with NOONAN SYNDROME.
A subclass of dual specificity phosphatases that play a role in the progression of the CELL CYCLE. They dephosphorylate and activate CYCLIN-DEPENDENT KINASES.
A subtype of non-receptor protein tyrosine phosphatases that includes two distinctive targeting motifs; an N-terminal motif specific for the INSULIN RECEPTOR, and a C-terminal motif specific for the SH3 domain containing proteins. This subtype includes a hydrophobic domain which localizes it to the ENDOPLASMIC RETICULUM.
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.
Inorganic salts of phosphoric acid.
A Src-homology domain-containing protein tyrosine phosphatase found in the CYTOSOL of hematopoietic cells. It plays a role in signal transduction by dephosphorylating signaling proteins that are activated or inactivated by PROTEIN-TYROSINE KINASES.
A specific inhibitor of phosphoserine/threonine protein phosphatase 1 and 2a. It is also a potent tumor promoter. (Thromb Res 1992;67(4):345-54 & Cancer Res 1993;53(2):239-41)
A phosphoprotein phosphatase that is specific for MYOSIN LIGHT CHAINS. It is composed of three subunits, which include a catalytic subunit, a myosin binding subunit, and a third subunit of unknown function.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The rate dynamics in chemical or physical systems.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.
A subcategory of protein tyrosine phosphatases that occur in the CYTOPLASM. Many of the proteins in this category play a role in intracellular signal transduction.
An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. EC 3.1.3.17.
Bone loss due to osteoclastic activity.
Glucuronidase is an enzyme (specifically, a glycosidase) that catalyzes the hydrolysis of glucuronic acid from various substrates, playing crucial roles in metabolic processes like detoxification and biotransformation within organisms.
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)
A subclass of receptor-like protein tryosine phosphatases that contain multiple extracellular immunoglobulin G-like domains and fibronectin type III-like domains. An additional memprin-A5-mu domain is found on some members of this subclass.
Compounds of the general formula R-O-R arranged in a ring or crown formation.
A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for P38 MITOGEN-ACTIVATED PROTEIN KINASES and JNK MITOGEN-ACTIVATED PROTEIN KINASES.
A transmembrane protein belonging to the tumor necrosis factor superfamily that specifically binds RECEPTOR ACTIVATOR OF NUCLEAR FACTOR-KAPPA B and OSTEOPROTEGERIN. It plays an important role in regulating OSTEOCLAST differentiation and activation.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
An enzyme that catalyzes the hydrolysis of nitrophenyl phosphates to nitrophenols. At acid pH it is probably ACID PHOSPHATASE (EC 3.1.3.2); at alkaline pH it is probably ALKALINE PHOSPHATASE (EC 3.1.3.1). EC 3.1.3.41.
Used as a pH indicator and as a reagent for blood after decolorizing the alkaline solution by boiling with zinc dust.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Nitrophenols are organic compounds characterized by the presence of a nitro group (-NO2) attached to a phenol molecule, known for their potential use in chemical and pharmaceutical industries, but also recognized as environmental pollutants due to their toxicity and potential carcinogenicity.
A specialized CONNECTIVE TISSUE that is the main constituent of the SKELETON. The principle cellular component of bone is comprised of OSTEOBLASTS; OSTEOCYTES; and OSTEOCLASTS, while FIBRILLAR COLLAGENS and hydroxyapatite crystals form the BONE MATRIX.
Esterases are hydrolase enzymes that catalyze the hydrolysis of ester bonds, converting esters into alcohols and acids, playing crucial roles in various biological processes including metabolism and detoxification.
Oxyvanadium ions in various states of oxidation. They act primarily as ion transport inhibitors due to their inhibition of Na(+)-, K(+)-, and Ca(+)-ATPase transport systems. They also have insulin-like action, positive inotropic action on cardiac ventricular muscle, and other metabolic effects.
Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.
Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.
A subclass of receptor-like protein tryosine phosphatases that contain a single cytosolic protein tyrosine phosphate domain and multiple extracellular fibronectin III-like domains.
The interference in synthesis of an enzyme due to the elevated level of an effector substance, usually a metabolite, whose presence would cause depression of the gene responsible for enzyme synthesis.
The sum of the weight of all the atoms in a molecule.
Organic compounds that contain phosphorus as an integral part of the molecule. Included under this heading is broad array of synthetic compounds that are used as PESTICIDES and DRUGS.
The thick, yellowish-white, viscid fluid secretion of male reproductive organs discharged upon ejaculation. In addition to reproductive organ secretions, it contains SPERMATOZOA and their nutrient plasma.
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.
Enzymes that catalyze the hydrolysis of a phenol sulfate to yield a phenol and sulfate. Arylsulfatase A, B, and C have been separated. A deficiency of arylsulfatases is one of the causes of metachromatic leukodystrophy (LEUKODYSTROPHY, METACHROMATIC). EC 3.1.6.1.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
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.
A subclass of receptor-like protein tryosine phosphatases that contain short highly glycosylated extracellular domains and two active cytosolic protein tyrosine phosphatase domains.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A subcategory of phosphohydrolases that are specific for MITOGEN-ACTIVATED PROTEIN KINASES. They play a role in the inactivation of the MAP KINASE SIGNALING SYSTEM.
Established cell cultures that have the potential to propagate indefinitely.
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.
A class of enzymes that catalyze the conversion of a nucleotide and water to a nucleoside and orthophosphate. EC 3.1.3.-.
Carbon-containing phosphoric acid derivatives. Included under this heading are compounds that have CARBON atoms bound to one or more OXYGEN atoms of the P(=O)(O)3 structure. Note that several specific classes of endogenous phosphorus-containing compounds such as NUCLEOTIDES; PHOSPHOLIPIDS; and PHOSPHOPROTEINS are listed elsewhere.
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.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
An enzyme that hydrolyzes thiamine pyrophosphate to thiamine monophosphate plus inorganic phosphate. EC 3.6.1.-.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
An organization of cells into an organ-like structure. Organoids can be generated in culture. They are also found in certain neoplasms.
A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for EXTRACELLULAR SIGNAL-REGULATED MAP KINASES and is primarily localized to the CYTOSOL.
A subtype of non-receptor protein tyrosine phosphatase that is closely-related to PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1. Alternative splicing of the mRNA for this phosphatase results in the production at two gene products, one of which includes a C-terminal nuclear localization domain that may be involved in the transport of the protein to the CELL NUCLEUS. Although initially referred to as T-cell protein tyrosine phosphatase the expression of this subtype occurs widely.
Five-membered heterocyclic ring structures containing an oxygen in the 1-position and a nitrogen in the 3-position, in distinction from ISOXAZOLES where they are at the 1,2 positions.
Tumors or cancer of the PROSTATE.
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)
A subcategory of protein tyrosine phosphatases that contain SH2 type SRC HOMOLOGY DOMAINS. Many of the proteins in this class are recruited to specific cellular targets such as a cell surface receptor complexes via their SH2 domain.
A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.
A CALCIUM and CALMODULIN-dependent serine/threonine protein phosphatase that is composed of the calcineurin A catalytic subunit and the calcineurin B regulatory subunit. Calcineurin has been shown to dephosphorylate a number of phosphoproteins including HISTONES; MYOSIN LIGHT CHAIN; and the regulatory subunits of CAMP-DEPENDENT PROTEIN KINASES. It is involved in the regulation of signal transduction and is the target of an important class of immunophilin-immunosuppressive drug complexes.
An enzyme that catalyzes the conversion of myo-inositol hexakisphosphate and water to 1L-myo-inositol 1,2,3,4,5-pentakisphosphate and orthophosphate. EC 3.1.3.26.
The relatively long-lived phagocytic cell of mammalian tissues that are derived from blood MONOCYTES. Main types are PERITONEAL MACROPHAGES; ALVEOLAR MACROPHAGES; HISTIOCYTES; KUPFFER CELLS of the liver; and OSTEOCLASTS. They may further differentiate within chronic inflammatory lesions to EPITHELIOID CELLS or may fuse to form FOREIGN BODY GIANT CELLS or LANGHANS GIANT CELLS. (from The Dictionary of Cell Biology, Lackie and Dow, 3rd ed.)
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.
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)
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria whose organisms occur in the lower part of the intestine of warm-blooded animals. The species are either nonpathogenic or opportunistic pathogens.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.
Analyses for a specific enzyme activity, or of the level of a specific enzyme that is used to assess health and disease risk, for early detection of disease or disease prediction, diagnosis, and change in disease status.
Proteins prepared by recombinant DNA technology.
A lipid phosphatase that acts on phosphatidylinositol-3,4,5-trisphosphate to regulate various SIGNAL TRANSDUCTION PATHWAYS. It modulates CELL GROWTH PROCESSES; CELL MIGRATION; and APOPTOSIS. Mutations in PTEN are associated with COWDEN DISEASE and PROTEUS SYNDROME as well as NEOPLASTIC CELL TRANSFORMATION.
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.
Elements of limited time intervals, contributing to particular results or situations.
An enzyme that catalyzes the conversion of phosphorylated, inactive glycogen synthase D to active dephosphoglycogen synthase I. EC 3.1.3.42.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A tumor necrosis factor receptor family member that is specific for RANK LIGAND and plays a role in bone homeostasis by regulating osteoclastogenesis. It is also expressed on DENDRITIC CELLS where it plays a role in regulating dendritic cell survival. Signaling by the activated receptor occurs through its association with TNF RECEPTOR-ASSOCIATED FACTORS.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Cyclic heptapeptides found in MICROCYSTIS and other CYANOBACTERIA. Hepatotoxic and carcinogenic effects have been noted. They are sometimes called cyanotoxins, which should not be confused with chemicals containing a cyano group (CN) which are toxic.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
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.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
A subclass of receptor-like protein tryosine phosphatases that contain an extracellular fibronectin III-like domain along with a carbonic anhydrase-like domain.
Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.
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.
Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.
Vitamin K-dependent calcium-binding protein synthesized by OSTEOBLASTS and found primarily in BONES. Serum osteocalcin measurements provide a noninvasive specific marker of bone metabolism. The protein contains three residues of the amino acid gamma-carboxyglutamic acid (Gla), which, in the presence of CALCIUM, promotes binding to HYDROXYAPATITE and subsequent accumulation in BONE MATRIX.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
(Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
A toxic compound, isolated from the Spanish fly or blistering beetle (Lytta (Cantharis) vesicatoria) and other insects. It is a potent and specific inhibitor of protein phosphatases 1 (PP1) and 2A (PP2A). This compound can produce severe skin inflammation, and is extremely toxic if ingested orally.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Condensed areas of cellular material that may be bounded by a membrane.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of a N-terminal catalytic domain and a large C-terminal domain that is enriched in PROLINE, GLUTAMIC ACID, SERINE, and THREONINE residues (PEST sequences). The phosphatase subtype is ubiquitously expressed and implicated in the regulation of a variety of biological processes such as CELL MOVEMENT; CYTOKINESIS; focal adhesion disassembly; and LYMPHOCYTE ACTIVATION.
A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for EXTRACELLULAR SIGNAL-REGULATED MAP KINASES.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Peroxidases are enzymes that catalyze the reduction of hydrogen peroxide to water, while oxidizing various organic and inorganic compounds, playing crucial roles in diverse biological processes including stress response, immune defense, and biosynthetic reactions.
Bone-forming cells which secrete an EXTRACELLULAR MATRIX. HYDROXYAPATITE crystals are then deposited into the matrix to form bone.
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 subcategory of protein tyrosine phosphatases that are bound to the cell membrane. They contain cytoplasmic tyrosine phosphatase domains and extracellular protein domains that may play a role in cell-cell interactions by interacting with EXTRACELLULAR MATRIX components. They are considered receptor-like proteins in that they appear to lack specific ligands.
A non-metal element that has the atomic symbol P, atomic number 15, and atomic weight 31. It is an essential element that takes part in a broad variety of biochemical reactions.
A species of MORGANELLA formerly classified as a Proteus species. It is found in the feces of humans, dogs, other mammals, and reptiles. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
A family of 3,3-bis(p-hydroxyphenyl)phthalides. They are used as CATHARTICS, indicators, and COLORING AGENTS.
An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis.
The study of the structure, behavior, growth, reproduction, and pathology of cells; and the function and chemistry of cellular components.
A secreted member of the TNF receptor superfamily that negatively regulates osteoclastogenesis. It is a soluble decoy receptor of RANK LIGAND that inhibits both CELL DIFFERENTIATION and function of OSTEOCLASTS by inhibiting the interaction between RANK LIGAND and RECEPTOR ACTIVATOR OF NUCLEAR FACTOR-KAPPA B.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
A neoplastic disease of the lymphoreticular cells which is considered to be a rare type of chronic leukemia; it is characterized by an insidious onset, splenomegaly, anemia, granulocytopenia, thrombocytopenia, little or no lymphadenopathy, and the presence of "hairy" or "flagellated" cells in the blood and bone marrow.

Enzymes and reproduction in natural populations of Drosophila euronotus. (1/2302)

Populations of Drosophila euronotus, one from southern Louisiana )3 samples), and one from Missouri (2 samples), were classified for allele frequencies at alkaline phosphatase (APH) and acid phosphatase (ACPH) loci. The two populations differed consistently in allele frequencies at both loci. The APH locus is on the inversion-free X chromosome; the chromosomal locus of the autosomal ACPH is unknown, and could involve inversion polymorphism. Wild females from Missouri and Louisiana populations heterozygous at the APH locus carried more sperm at capture than did the corresponding homozygotes. This heterotic association was significant for the combined samples, and whether it was the result of heterosis at the enzyme locus studied, or due to geographically widespread close linkage with other heterotic loci, it should help to maintain heterozygosity at the APH locus. In a Louisiana collection which included large numbers of sperm-free females, simultaneous homozygosity at both enzyme loci was significantly associated with lack of sperm. It is suggested that the latter association is the result of young heterozygous females achieving sexual maturity earlier than do the double homozygotes. The average effective sperm load for 225 wild females was only 29.4, suggesting the necessity for frequent repeat-mating in nature to maintain female fertility. A comparison of the sex-linked APH genotypes of wild females with those of their daughters indicated that among 295 wild-inseminated females from five populations, 35% had mated more than once, and of this 35%, six females had mated at least three times. Because of ascertainment difficulties, it is clear that the true frequency of multiple-mating in nature must have been much higher than the observed 35%. Laboratory studies indicate that multiple-mating in this species does not involve sperm displacement, possibly due to the small number of sperms transmitted per mating, and the fact that the sperm receptacles are only partially filled by a given mating.  (+info)

Endometrial lysosomal enzyme activity in normal cycling endometrium. (2/2302)

The objective of this study was to evaluate the possible role of four lysosomal enzymes in endometrial function and remodelling during the normal menstrual cycle by fluorimetric measurement (acid phosphatase, N-acetyl-beta-D-glucosaminidase, alpha-L-fucosidase and alpha-D-mannosidase). A prospective study was conducted of 45 endometrial biopsies obtained from women with normal menstrual cycles. Activity of all four enzymes was identified in human endometrium. Activity of acid phosphatase and N-acetyl-beta-D-glucosaminidase was relatively high, whilst that of alpha-L-fucosidase and alpha-D-mannosidase was low. There was no significant change in the activity of any of the four enzymes from the proliferative to the secretory phase of the cycle. This study suggests that the activity of these enzymes remains constant throughout a major portion of the normal cycle.  (+info)

Strong induction of members of the chitinase family of proteins in atherosclerosis: chitotriosidase and human cartilage gp-39 expressed in lesion macrophages. (3/2302)

Atherosclerosis is initiated by the infiltration of monocytes into the subendothelial space of the vessel wall and subsequent lipid accumulation of the activated macrophages. The molecular mechanisms involved in the anomalous behavior of macrophages in atherogenesis have only partially been disclosed. Chitotriosidase and human cartilage gp-39 (HC gp-39) are members of the chitinase family of proteins and are expressed in lipid-laden macrophages accumulated in various organs during Gaucher disease. In addition, as shown in this study, chitotriosidase and HC gp-39 can be induced with distinct kinetics in cultured macrophages. We investigated the expression of these chitinase-like genes in the human atherosclerotic vessel wall by in situ hybridizations on atherosclerotic specimens derived from femoral artery (4 specimens), aorta (4 specimens), iliac artery (3 specimens), carotid artery (4 specimens), and coronary artery (1 specimen), as well as 5 specimens derived from apparently normal vascular tissue. We show for the first time that chitotriosidase and HC gp-39 expression was strongly upregulated in distinct subsets of macrophages in the atherosclerotic plaque. The expression patterns of chitotriosidase and HC gp-39 were compared and shown to be different from the patterns observed for the extracellular matrix protein osteopontin and the macrophage marker tartrate-resistant acid phosphatase. Our data emphasize the remarkable phenotypic variation among macrophages present in the atherosclerotic lesion. Furthermore, chitotriosidase enzyme activity was shown to be elevated up to 55-fold in extracts of atherosclerotic tissue. Although a function for chitotriosidase and HC gp-39 has not been identified, we hypothesize a role in cell migration and tissue remodeling during atherogenesis.  (+info)

An activation-specific role for transcription factor TFIIB in vivo. (4/2302)

A yeast mutant was isolated encoding a single amino acid substitution [serine-53 --> proline (S53P)] in transcription factor TFIIB that impairs activation of the PHO5 gene in response to phosphate starvation. This effect is activation-specific because S53P did not affect the uninduced level of PHO5 expression, yet is not specific to PHO5 because Adr1-mediated activation of the ADH2 gene also was impaired by S53P. Pho4, the principal activator of PHO5, directly interacted with TFIIB in vitro, and this interaction was impaired by the S53P replacement. Furthermore, Pho4 induced a conformational change in TFIIB, detected by enhanced sensitivity to V8 protease. The S53P replacement also impaired activation of a lexA(op)-lacZ reporter by a LexA fusion protein to the activation domain of Adr1, thereby indicating that the transcriptional effect on ADH2 expression is specific to the activation function of Adr1. These results define an activation-specific role for TFIIB in vivo and suggest that certain activators induce a conformational change in TFIIB as part of their mechanism of transcriptional stimulation.  (+info)

A study of the genetical structure of the Cuban population: red cell and serum biochemical markers. (5/2302)

Gene frequencies of several red cell and serum gentic markers were determined in the three main racial groups--whites, mulattoes and Negroes--of the Cuban population. The results were used to estimate the relative contribution of Caucasian and Negro genes to the genetic makeup of these three groups and to calculate the frequencies of these genes in the general Cuban population.  (+info)

An in vitro system recapitulates chromatin remodeling at the PHO5 promoter. (6/2302)

The Saccharomyces cerevisiae gene PHO5 is an excellent system with which to study regulated changes in chromatin structure. The PHO5 promoter is packaged into four positioned nucleosomes under repressing conditions; upon induction, the structure of these nucleosomes is altered such that the promoter DNA becomes accessible to nucleases. We report here the development and characterization of an in vitro system in which partially purified PHO5 minichromosomes undergo promoter chromatin remodeling. Several hallmarks of the PHO5 chromatin transition in vivo were reproduced in this system. Chromatin remodeling of PHO5 minichromosomes required the transcription factors Pho4 and Pho2, was localized to the promoter region of PHO5, and was independent of the chromatin-remodeling complex Swi-Snf. In vitro chromatin remodeling also required the addition of fractionated nuclear extract and hydrolyzable ATP. This in vitro system should serve as a useful tool for identifying the components required for this reaction and for elucidating the mechanism by which the PHO5 promoter chromatin structure is changed.  (+info)

Laser induced phagocytosis in the pigment epithelium of the Hunter dystrophic rat. (7/2302)

The retinae of 14-day-old Hunter dystrophic rats have been subjected to low-energy irradiation by a pulsed ruby laser. Fifteen days after exposure, pigment epithelial cells had proliferated and repopulated the irradiated areas. In all such areas the subretinal photoreceptor debris had been reduced or lost.  (+info)

The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas) metal content and spectroscopic characterization. (8/2302)

Purple acid phosphatase from sweet potatoes Ipomoea batatas (spPAP) has been purified to homogeneity and characterized using spectroscopic investigations. Matrix-assisted laser desorption/ionization mass spectrometry analysis revealed a molecular mass of approximately 112 kDa. The metal content was determined by X-ray fluorescence using synchrotron radiation. In contrast to previous studies it is shown that spPAP contains a Fe(III)-Zn(II) center in the active site as previously determined for the purple acid phosphatase from red kidney bean (kbPAP). Moreover, an alignment of the amino acid sequences suggests that the residues involved in metal-binding are identical in both plant PAPs. Tyrosine functions as one of the ligands for the chromophoric Fe(III). Low temperature EPR spectra of spPAP show a signal near g = 4.3, characteristic for high-spin Fe(III) in a rhombic environment. The Tyr-Fe(III) charge transfer transition and the EPR signal are both very sensitive to changes in pH. The pH dependency strongly suggests the presence of an ionizable group with a pKa of 4.7, arising from an aquo ligand coordinated to Fe(III). EPR and UV/visible studies of spPAP in the presence of the inhibitors phosphate or arsenate suggest that both anions bind to Fe(III) in the binuclear center replacing the coordinated water or hydroxide ligand necessary for hydrolysis. The conserved histidine residues of spPAP corresponding to His202 and His296 in kbPAP probably interact in catalysis.  (+info)

Acid phosphatase is a type of enzyme that is found in various tissues and organs throughout the body, including the prostate gland, red blood cells, bone, liver, spleen, and kidneys. This enzyme plays a role in several biological processes, such as bone metabolism and the breakdown of molecules like nucleotides and proteins.

Acid phosphatase is classified based on its optimum pH level for activity. Acid phosphatases have an optimal activity at acidic pH levels (below 7.0), while alkaline phosphatases have an optimal activity at basic or alkaline pH levels (above 7.0).

In clinical settings, measuring the level of acid phosphatase in the blood can be useful as a tumor marker for prostate cancer. Elevated acid phosphatase levels may indicate the presence of metastatic prostate cancer or disease progression. However, it is important to note that acid phosphatase is not specific to prostate cancer and can also be elevated in other conditions, such as bone diseases, liver disorders, and some benign conditions. Therefore, acid phosphatase should be interpreted in conjunction with other diagnostic tests and clinical findings for a more accurate diagnosis.

Phosphoprotein phosphatases (PPPs) are a family of enzymes that play a crucial role in the regulation of various cellular processes by removing phosphate groups from serine, threonine, and tyrosine residues on proteins. Phosphorylation is a post-translational modification that regulates protein function, localization, and stability, and dephosphorylation by PPPs is essential for maintaining the balance of this regulation.

The PPP family includes several subfamilies, such as PP1, PP2A, PP2B (also known as calcineurin), PP4, PP5, and PP6. Each subfamily has distinct substrate specificities and regulatory mechanisms. For example, PP1 and PP2A are involved in the regulation of metabolism, signal transduction, and cell cycle progression, while PP2B is involved in immune response and calcium signaling.

Dysregulation of PPPs has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. Therefore, understanding the function and regulation of PPPs is important for developing therapeutic strategies to target these diseases.

Tartrates are salts or esters of tartaric acid, a naturally occurring organic acid found in many fruits, particularly grapes. In a medical context, potassium bitartrate (also known as cream of tartar) is sometimes used as a mild laxative or to treat acidosis by helping to restore the body's normal pH balance. Additionally, sodium tartrate has been historically used as an antidote for lead poisoning. However, these uses are not common in modern medicine.

Protein Tyrosine Phosphatases (PTPs) are a group of enzymes that play a crucial role in the regulation of various cellular processes, including cell growth, differentiation, and signal transduction. PTPs function by removing phosphate groups from tyrosine residues on proteins, thereby counteracting the effects of tyrosine kinases, which add phosphate groups to tyrosine residues to activate proteins.

PTPs are classified into several subfamilies based on their structure and function, including classical PTPs, dual-specificity PTPs (DSPs), and low molecular weight PTPs (LMW-PTPs). Each subfamily has distinct substrate specificities and regulatory mechanisms.

Classical PTPs are further divided into receptor-like PTPs (RPTPs) and non-receptor PTPs (NRPTPs). RPTPs contain a transmembrane domain and extracellular regions that mediate cell-cell interactions, while NRPTPs are soluble enzymes located in the cytoplasm.

DSPs can dephosphorylate both tyrosine and serine/threonine residues on proteins and play a critical role in regulating various signaling pathways, including the mitogen-activated protein kinase (MAPK) pathway.

LMW-PTPs are a group of small molecular weight PTPs that localize to different cellular compartments, such as the endoplasmic reticulum and mitochondria, and regulate various cellular processes, including protein folding and apoptosis.

Overall, PTPs play a critical role in maintaining the balance of phosphorylation and dephosphorylation events in cells, and dysregulation of PTP activity has been implicated in various diseases, including cancer, diabetes, and neurological disorders.

Protein Phosphatase 2 (PP2A) is a type of serine/threonine protein phosphatase that plays a crucial role in the regulation of various cellular processes, including signal transduction, cell cycle progression, and metabolism. PP2A is a heterotrimeric enzyme composed of a catalytic subunit (C), a regulatory subunit A (A), and a variable regulatory subunit B (B). The different combinations of the B subunits confer specificity to PP2A, allowing it to regulate a diverse array of cellular targets.

PP2A is responsible for dephosphorylating many proteins that have been previously phosphorylated by protein kinases. This function is essential for maintaining the balance of phosphorylation and dephosphorylation in cells, which is necessary for proper protein function and cell signaling. Dysregulation of PP2A has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular disease.

Protein Phosphatase 1 (PP1) is a type of serine/threonine protein phosphatase that plays a crucial role in the regulation of various cellular processes, including metabolism, signal transduction, and cell cycle progression. PP1 functions by removing phosphate groups from specific serine and threonine residues on target proteins, thereby reversing the effects of protein kinases and controlling protein activity, localization, and stability.

PP1 is a highly conserved enzyme found in eukaryotic cells and is composed of a catalytic subunit associated with one or more regulatory subunits that determine its substrate specificity, subcellular localization, and regulation. The human genome encodes several isoforms of the PP1 catalytic subunit, including PP1α, PP1β/δ, and PP1γ, which share a high degree of sequence similarity and functional redundancy.

PP1 has been implicated in various physiological processes, such as muscle contraction, glycogen metabolism, DNA replication, transcription, and RNA processing. Dysregulation of PP1 activity has been associated with several pathological conditions, including neurodegenerative diseases, cancer, and diabetes. Therefore, understanding the molecular mechanisms that regulate PP1 function is essential for developing novel therapeutic strategies to treat these disorders.

Phosphoric monoester hydrolases are a class of enzymes that catalyze the hydrolysis of phosphoric monoesters into alcohol and phosphate. This class of enzymes includes several specific enzymes, such as phosphatases and nucleotidases, which play important roles in various biological processes, including metabolism, signal transduction, and regulation of cellular processes.

Phosphoric monoester hydrolases are classified under the EC number 3.1.3 by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB). The enzymes in this class share a common mechanism of action, which involves the nucleophilic attack on the phosphorus atom of the substrate by a serine or cysteine residue in the active site of the enzyme. This results in the formation of a covalent intermediate, which is then hydrolyzed to release the products.

Phosphoric monoester hydrolases are important therapeutic targets for the development of drugs that can modulate their activity. For example, inhibitors of phosphoric monoester hydrolases have been developed as potential treatments for various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

Glucose-6-phosphatase is an enzyme that plays a crucial role in the regulation of glucose metabolism. It is primarily located in the endoplasmic reticulum of cells in liver, kidney, and intestinal mucosa. The main function of this enzyme is to remove the phosphate group from glucose-6-phosphate (G6P), converting it into free glucose, which can then be released into the bloodstream and used as a source of energy by cells throughout the body.

The reaction catalyzed by glucose-6-phosphatase is as follows:

Glucose-6-phosphate + H2O → Glucose + Pi (inorganic phosphate)

This enzyme is essential for maintaining normal blood glucose levels, particularly during periods of fasting or starvation. In these situations, the body needs to break down stored glycogen in the liver and convert it into glucose to supply energy to the brain and other vital organs. Glucose-6-phosphatase is a key enzyme in this process, allowing for the release of free glucose into the bloodstream.

Deficiencies or mutations in the gene encoding glucose-6-phosphatase can lead to several metabolic disorders, such as glycogen storage disease type I (von Gierke's disease) and other related conditions. These disorders are characterized by an accumulation of glycogen and/or fat in various organs, leading to impaired glucose metabolism, growth retardation, and increased risk of infection and liver dysfunction.

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.

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.

Phosphatidate phosphatase is an enzyme that plays a crucial role in the metabolism of lipids, particularly in the synthesis of glycerophospholipids, which are key components of cell membranes.

The term "phosphatidate" refers to a type of lipid molecule known as a diacylglycerol phosphate. This molecule contains two fatty acid chains attached to a glycerol backbone, with a phosphate group also attached to the glycerol.

Phosphatidate phosphatase functions to remove the phosphate group from phosphatidate, converting it into diacylglycerol (DAG). This reaction is an important step in the biosynthesis of glycerophospholipids, as DAG can be further metabolized to produce various types of these lipids, including phosphatidylcholine, phosphatidylethanolamine, and phosphatidylinositol.

There are two main types of phosphatidate phosphatase enzymes: type 1 and type 2. Type 1 phosphatidate phosphatase is primarily located in the cytosol and is involved in the synthesis of triacylglycerols, which are stored as energy reserves in cells. Type 2 phosphatidate phosphatase, on the other hand, is found on the endoplasmic reticulum membrane and plays a key role in the biosynthesis of glycerophospholipids.

Deficiencies or mutations in phosphatidate phosphatase enzymes can lead to various metabolic disorders, including some forms of lipodystrophy, which are characterized by abnormalities in fat metabolism and distribution.

Histochemistry is the branch of pathology that deals with the microscopic localization of cellular or tissue components using specific chemical reactions. It involves the application of chemical techniques to identify and locate specific biomolecules within tissues, cells, and subcellular structures. This is achieved through the use of various staining methods that react with specific antigens or enzymes in the sample, allowing for their visualization under a microscope. Histochemistry is widely used in diagnostic pathology to identify different types of tissues, cells, and structures, as well as in research to study cellular and molecular processes in health and disease.

The prostate is a small gland that is part of the male reproductive system. Its main function is to produce a fluid that, together with sperm cells from the testicles and fluids from other glands, makes up semen. This fluid nourishes and protects the sperm, helping it to survive and facilitating its movement.

The prostate is located below the bladder and in front of the rectum. It surrounds part of the urethra, the tube that carries urine and semen out of the body. This means that prostate problems can affect urination and sexual function. The prostate gland is about the size of a walnut in adult men.

Prostate health is an important aspect of male health, particularly as men age. Common prostate issues include benign prostatic hyperplasia (BPH), which is an enlarged prostate not caused by cancer, and prostate cancer, which is one of the most common types of cancer in men. Regular check-ups with a healthcare provider can help to detect any potential problems early and improve outcomes.

Osteoclasts are large, multinucleated cells that are primarily responsible for bone resorption, a process in which they break down and dissolve the mineralized matrix of bones. They are derived from monocyte-macrophage precursor cells of hematopoietic origin and play a crucial role in maintaining bone homeostasis by balancing bone formation and bone resorption.

Osteoclasts adhere to the bone surface and create an isolated microenvironment, called the "resorption lacuna," between their cell membrane and the bone surface. Here, they release hydrogen ions into the lacuna through a process called proton pumping, which lowers the pH and dissolves the mineral component of the bone matrix. Additionally, osteoclasts secrete proteolytic enzymes, such as cathepsin K, that degrade the organic components, like collagen, in the bone matrix.

An imbalance in osteoclast activity can lead to various bone diseases, including osteoporosis and Paget's disease, where excessive bone resorption results in weakened and fragile bones.

Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.

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.

Dual-specificity phosphatases (DUSPs) are a group of enzymes that regulate various cellular processes by removing phosphate groups from specific proteins. They are called "dual-specificity" because they can remove phosphates from both tyrosine and serine/threonine residues on their target proteins, whereas most other protein phosphatases can only remove phosphates from one or the other.

DUSPs play important roles in regulating signal transduction pathways that are involved in various cellular functions such as proliferation, differentiation, survival, and apoptosis. They act as negative regulators of these pathways by dephosphorylating and inactivating key signaling molecules, including mitogen-activated protein kinases (MAPKs) and extracellular signal-regulated kinases (ERKs).

There are several subfamilies of DUSPs, each with distinct substrate specificities and cellular localizations. Some DUSPs are primarily cytoplasmic, while others are nuclear or associated with the plasma membrane. Dysregulation of DUSP activity has been implicated in various diseases, including cancer, diabetes, and neurodegenerative disorders. Therefore, understanding the function and regulation of DUSPs is important for developing new therapeutic strategies for these diseases.

Protein Tyrosine Phosphatase, Non-Receptor Type 11 (PTPN11) is a gene that encodes for the protein tyrosine phosphatase SHP-2. This enzyme regulates various cellular processes, including cell growth, differentiation, and migration, by controlling the balance of phosphorylation and dephosphorylation of proteins involved in signal transduction pathways. Mutations in PTPN11 have been associated with several human diseases, most notably Noonan syndrome and its related disorders, as well as certain types of leukemia.

CDC25 phosphatases are a group of enzymes that play crucial roles in the regulation of the cell cycle, which is the series of events that cells undergo as they grow and divide. Specifically, CDC25 phosphatases function to remove inhibitory phosphates from certain cyclin-dependent kinases (CDKs), thereby activating them and allowing the cell cycle to progress.

There are three main types of CDC25 phosphatases in humans, known as CDC25A, CDC25B, and CDC25C. These enzymes are named after the original yeast homolog, called Cdc25, which was discovered to be essential for cell cycle progression.

CDC25 phosphatases are tightly regulated during the cell cycle, with their activity being controlled by various mechanisms such as phosphorylation, protein-protein interactions, and subcellular localization. Dysregulation of CDC25 phosphatases has been implicated in several human diseases, including cancer, where they can contribute to uncontrolled cell growth and division. Therefore, understanding the functions and regulation of CDC25 phosphatases is an important area of research in molecular biology and medicine.

Protein Tyrosine Phosphatase, Non-Receptor Type 1 (PTPN1) is a type of enzyme that belongs to the protein tyrosine phosphatase (PTP) family. PTPs play crucial roles in regulating various cellular processes by removing phosphate groups from phosphorylated tyrosine residues on proteins, thereby controlling the activity of many proteins involved in signal transduction pathways.

PTPN1, also known as PTP1B, is a non-receptor type PTP that is localized to the endoplasmic reticulum and cytosol of cells. It has been extensively studied due to its important role in regulating various cellular signaling pathways, including those involved in metabolism, cell growth, differentiation, and survival.

PTPN1 dephosphorylates several key signaling molecules, such as the insulin receptor, epidermal growth factor receptor (EGFR), and Janus kinase 2 (JAK2). By negatively regulating these signaling pathways, PTPN1 acts as a tumor suppressor and plays a role in preventing excessive cell growth and survival. However, dysregulation of PTPN1 has been implicated in various diseases, including diabetes, obesity, and cancer.

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.

Phosphates, in a medical context, refer to the salts or esters of phosphoric acid. Phosphates play crucial roles in various biological processes within the human body. They are essential components of bones and teeth, where they combine with calcium to form hydroxyapatite crystals. Phosphates also participate in energy transfer reactions as phosphate groups attached to adenosine diphosphate (ADP) and adenosine triphosphate (ATP). Additionally, they contribute to buffer systems that help maintain normal pH levels in the body.

Abnormal levels of phosphates in the blood can indicate certain medical conditions. High phosphate levels (hyperphosphatemia) may be associated with kidney dysfunction, hyperparathyroidism, or excessive intake of phosphate-containing products. Low phosphate levels (hypophosphatemia) might result from malnutrition, vitamin D deficiency, or certain diseases affecting the small intestine or kidneys. Both hypophosphatemia and hyperphosphatemia can have significant impacts on various organ systems and may require medical intervention.

Protein Tyrosine Phosphatase, Non-Receptor Type 6 (PTPN6) is a protein encoded by the PTPN6 gene in humans. It belongs to the family of protein tyrosine phosphatases (PTPs), which are enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. This regulation of protein phosphorylation is critical for various cellular processes, including signal transduction, cell growth, and differentiation.

PTPN6, also known as SHP-1 (Src Homology 2 domain-containing Protein Tyrosine Phosphatase-1), is a non-receptor type PTP, meaning it does not have a transmembrane domain and is found in the cytosol. It contains two SH2 domains at its N-terminus, which allow it to bind to specific phosphotyrosine-containing motifs on target proteins, and a catalytic PTP domain at its C-terminus, responsible for its enzymatic activity.

PTPN6 plays essential roles in hematopoiesis, immune responses, and cancer. It negatively regulates various signaling pathways, including those downstream of cytokine receptors, growth factor receptors, and T-cell receptors. Dysregulation of PTPN6 has been implicated in several diseases, such as leukemia, lymphoma, and autoimmune disorders.

Okadaic acid is a type of toxin that is produced by certain species of marine algae, including Dinophysis and Prorocentrum. It is a potent inhibitor of protein phosphatases 1 and 2A, which are important enzymes that help regulate cellular processes in the body.

Okadaic acid can accumulate in shellfish that feed on these algae, and consumption of contaminated seafood can lead to a serious illness known as diarrhetic shellfish poisoning (DSP). Symptoms of DSP include nausea, vomiting, diarrhea, and abdominal cramps. In severe cases, it can also cause neurological symptoms such as dizziness, disorientation, and tingling or numbness in the lips, tongue, and fingers.

It is important to note that okadaic acid is not only a marine toxin but also used in scientific research as a tool to study the role of protein phosphatases in cellular processes. However, exposure to this compound should be avoided due to its toxic effects.

Myosin-Light-Chain Phosphatase (MLCP) is an enzyme complex that plays a crucial role in the regulation of muscle contraction and relaxation. It is responsible for dephosphorylating the myosin light chains, which are key regulatory components of the contractile apparatus in muscles.

The phosphorylation state of the myosin light chains regulates the interaction between actin and myosin filaments, which is necessary for muscle contraction. When the myosin light chains are phosphorylated, they bind more strongly to actin, leading to increased contractile force. Conversely, when the myosin light chains are dephosphorylated by MLCP, the interaction between actin and myosin is weakened, allowing for muscle relaxation.

MLCP is composed of three subunits: a catalytic subunit (PP1cδ), a regulatory subunit (MYPT1), and a small subunit (M20). The regulatory subunit contains binding sites for various signaling molecules that can modulate the activity of MLCP, such as calcium/calmodulin, protein kinase C, and Rho-associated protein kinase (ROCK). Dysregulation of MLCP has been implicated in various muscle disorders, including hypertrophic cardiomyopathy, dilated cardiomyopathy, and muscle atrophy.

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.

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.

Alkaline phosphatase (ALP) is an enzyme found in various body tissues, including the liver, bile ducts, digestive system, bones, and kidneys. It plays a role in breaking down proteins and minerals, such as phosphate, in the body.

The medical definition of alkaline phosphatase refers to its function as a hydrolase enzyme that removes phosphate groups from molecules at an alkaline pH level. In clinical settings, ALP is often measured through blood tests as a biomarker for various health conditions.

Elevated levels of ALP in the blood may indicate liver or bone diseases, such as hepatitis, cirrhosis, bone fractures, or cancer. Therefore, physicians may order an alkaline phosphatase test to help diagnose and monitor these conditions. However, it is essential to interpret ALP results in conjunction with other diagnostic tests and clinical findings for accurate diagnosis and treatment.

Protein Tyrosine Phosphatases, Non-Receptor (PTPNs) are a type of enzymes that play a crucial role in the regulation of various cellular processes by removing phosphate groups from tyrosine residues of proteins. Unlike receptor protein tyrosine phosphatases, PTPNs do not have a transmembrane domain and are located in the cytoplasm. They are involved in several signaling pathways that control cell growth, differentiation, migration, and survival. Dysregulation of PTPN function has been implicated in various diseases, including cancer, diabetes, and neurological disorders.

Phosphorylase phosphatase is an enzyme that plays a role in the regulation of glycogen metabolism. It works by removing phosphate groups from glycogen phosphorylase, which is an enzyme that breaks down glycogen into glucose-1-phosphate. The dephosphorylation of glycogen phosphorylase by phosphorylase phosphatase leads to the inactivation of the enzyme and therefore slows down the breakdown of glycogen. Phosphorylase phosphatase is itself regulated by various hormones and signaling molecules, allowing for fine-tuning of glycogen metabolism in response to changes in energy demand.

Bone resorption is the process by which bone tissue is broken down and absorbed into the body. It is a normal part of bone remodeling, in which old or damaged bone tissue is removed and new tissue is formed. However, excessive bone resorption can lead to conditions such as osteoporosis, in which bones become weak and fragile due to a loss of density. This process is carried out by cells called osteoclasts, which break down the bone tissue and release minerals such as calcium into the bloodstream.

Glucuronidase is an enzyme that catalyzes the hydrolysis of glucuronic acid from various substrates, including molecules that have been conjugated with glucuronic acid as part of the detoxification process in the body. This enzyme plays a role in the breakdown and elimination of certain drugs, toxins, and endogenous compounds, such as bilirubin. It is found in various tissues and organisms, including humans, bacteria, and insects. In clinical contexts, glucuronidase activity may be measured to assess liver function or to identify the presence of certain bacterial infections.

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.

Receptor-like protein tyrosine phosphatases, class 2 (RPTPs-Class 2) are a subfamily of receptor-like protein tyrosine phosphatases that play crucial roles in various cellular processes, including cell growth, differentiation, and migration. These transmembrane enzymes are characterized by the presence of two extracellular fibronectin type III domains, a single membrane-spanning region, and one or two intracellular protein tyrosine phosphatase (PTP) domains.

RPTPs-Class 2 include four members in humans: PTPRD, PTPRF, PTPRG, and PTPRH. These enzymes can dephosphorylate and modulate the activity of various proteins involved in signal transduction pathways by removing phosphate groups from tyrosine residues. By doing so, RPTPs-Class 2 help regulate the balance between kinase-mediated phosphorylation and phosphatase-mediated dephosphorylation events, which is essential for proper cellular function.

Mutations in RPTPs-Class 2 genes have been associated with various human diseases, including cancer, neurological disorders, and developmental abnormalities. Therefore, understanding the structure, regulation, and functions of these enzymes can provide valuable insights into disease mechanisms and potential therapeutic strategies.

Cyclic ethers are a type of organic compound that contain an ether functional group (-O-) within a cyclic (ring-shaped) structure. In a cyclic ether, one or more oxygen atoms are part of the ring, which can consist of various numbers of carbon atoms. The simplest example of a cyclic ether is oxirane, also known as ethylene oxide, which contains a three-membered ring with two carbon atoms and one oxygen atom.

Cyclic ethers have diverse applications in the chemical industry, including their use as building blocks for the synthesis of other chemicals, pharmaceuticals, and materials. Some cyclic ethers, like tetrahydrofuran (THF), are common solvents due to their ability to dissolve a wide range of organic compounds. However, some cyclic ethers can be hazardous or toxic, so they must be handled with care during laboratory work and industrial processes.

Dual Specificity Phosphatase 1 (DUSP1), also known as MAP Kinase Phosphatase 1 (MKP-1), is a protein that plays a crucial role in the negative regulation of cell signaling pathways. It is a member of the dual specificity phosphatase family, which can dephosphorylate both tyrosine and serine/threonine residues on its target proteins.

DUSP1 specifically dephosphorylates and inactivates members of the mitogen-activated protein kinase (MAPK) family, including extracellular signal-regulated kinases (ERKs), c-Jun N-terminal kinases (JNKs), and p38 MAPKs. These MAPK signaling pathways are involved in various cellular processes such as proliferation, differentiation, survival, and apoptosis.

DUSP1 is rapidly induced in response to various stimuli, including growth factors, cytokines, and stress signals. Its expression helps maintain the balance of MAPK signaling, preventing excessive or prolonged activation that could lead to cellular dysfunction and diseases such as cancer, inflammation, and neurodegeneration.

In summary, Dual Specificity Phosphatase 1 (DUSP1) is a protein that negatively regulates MAPK signaling pathways by dephosphorylating and inactivating ERKs, JNKs, and p38 MAPKs. Its expression is critical for maintaining the proper balance of cell signaling and preventing the development of various diseases.

REceptor Activator of NF-kB (RANK) Ligand is a type of protein that plays a crucial role in the immune system and bone metabolism. It belongs to the tumor necrosis factor (TNF) superfamily and is primarily produced by osteoblasts, which are cells responsible for bone formation.

RANK Ligand binds to its receptor RANK, which is found on the surface of osteoclasts, a type of cell involved in bone resorption or breakdown. The binding of RANK Ligand to RANK activates signaling pathways that promote the differentiation, activation, and survival of osteoclasts, thereby increasing bone resorption.

Abnormalities in the RANKL-RANK signaling pathway have been implicated in various bone diseases, such as osteoporosis, rheumatoid arthritis, and certain types of cancer that metastasize to bones. Therefore, targeting this pathway with therapeutic agents has emerged as a promising approach for the treatment of these conditions.

Electron microscopy (EM) is a type of microscopy that uses a beam of electrons to create an image of the sample being examined, resulting in much higher magnification and resolution than light microscopy. There are several types of electron microscopy, including transmission electron microscopy (TEM), scanning electron microscopy (SEM), and reflection electron microscopy (REM).

In TEM, a beam of electrons is transmitted through a thin slice of the sample, and the electrons that pass through the sample are focused to form an image. This technique can provide detailed information about the internal structure of cells, viruses, and other biological specimens, as well as the composition and structure of materials at the atomic level.

In SEM, a beam of electrons is scanned across the surface of the sample, and the electrons that are scattered back from the surface are detected to create an image. This technique can provide information about the topography and composition of surfaces, as well as the structure of materials at the microscopic level.

REM is a variation of SEM in which the beam of electrons is reflected off the surface of the sample, rather than scattered back from it. This technique can provide information about the surface chemistry and composition of materials.

Electron microscopy has a wide range of applications in biology, medicine, and materials science, including the study of cellular structure and function, disease diagnosis, and the development of new materials and technologies.

4-Nitrophenylphosphatase is an enzyme that catalyzes the hydrolysis of 4-nitrophenyl phosphate, producing 4-nitrophenol and phosphate. This enzyme is commonly used in laboratory assays to measure enzyme activity or to determine the presence of certain metals, such as aluminum and lead, which can inhibit its activity. The hydrolysis reaction results in the formation of yellow 4-nitrophenol, which can be easily measured spectrophotometrically at a wavelength of 405 nm. The activity of 4-nitrophenylphosphatase is often used as an indicator of the functional status of certain organelles, such as lysosomes, in biological systems.

Thymolphthalein is not typically considered a medical term, but it is a chemical compound that is used in some medical contexts. It is primarily used as an acid-base indicator in laboratory settings and in chemical tests. When thymolphthalein is added to a solution, it changes color depending on the pH of the solution. Specifically, it turns from clear or colorless to blue in basic solutions (pH above 9.3) and remains colorless in acidic or neutral solutions.

In medical testing, thymolphthalein may be used as a component of certain urine tests to help determine the pH level of the urine or to detect the presence of certain substances in the urine. However, it is not a substance that is typically used for direct medical treatment or diagnosis.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Nitrophenols are organic compounds that contain a hydroxyl group (-OH) attached to a phenyl ring (aromatic hydrocarbon) and one or more nitro groups (-NO2). They have the general structure R-C6H4-NO2, where R represents the hydroxyl group.

Nitrophenols are known for their distinctive yellow to brown color and can be found in various natural sources such as plants and microorganisms. Some common nitrophenols include:

* p-Nitrophenol (4-nitrophenol)
* o-Nitrophenol (2-nitrophenol)
* m-Nitrophenol (3-nitrophenol)

These compounds are used in various industrial applications, including dyes, pharmaceuticals, and agrochemicals. However, they can also be harmful to human health and the environment, as some nitrophenols have been identified as potential environmental pollutants and may pose risks to human health upon exposure.

"Bone" is the hard, dense connective tissue that makes up the skeleton of vertebrate animals. It provides support and protection for the body's internal organs, and serves as a attachment site for muscles, tendons, and ligaments. Bone is composed of cells called osteoblasts and osteoclasts, which are responsible for bone formation and resorption, respectively, and an extracellular matrix made up of collagen fibers and mineral crystals.

Bones can be classified into two main types: compact bone and spongy bone. Compact bone is dense and hard, and makes up the outer layer of all bones and the shafts of long bones. Spongy bone is less dense and contains large spaces, and makes up the ends of long bones and the interior of flat and irregular bones.

The human body has 206 bones in total. They can be further classified into five categories based on their shape: long bones, short bones, flat bones, irregular bones, and sesamoid bones.

Esterases are a group of enzymes that catalyze the hydrolysis of ester bonds in esters, producing alcohols and carboxylic acids. They are widely distributed in plants, animals, and microorganisms and play important roles in various biological processes, such as metabolism, digestion, and detoxification.

Esterases can be classified into several types based on their substrate specificity, including carboxylesterases, cholinesterases, lipases, and phosphatases. These enzymes have different structures and mechanisms of action but all share the ability to hydrolyze esters.

Carboxylesterases are the most abundant and diverse group of esterases, with a wide range of substrate specificity. They play important roles in the metabolism of drugs, xenobiotics, and lipids. Cholinesterases, on the other hand, specifically hydrolyze choline esters, such as acetylcholine, which is an important neurotransmitter in the nervous system. Lipases are a type of esterase that preferentially hydrolyzes triglycerides and plays a crucial role in fat digestion and metabolism. Phosphatases are enzymes that remove phosphate groups from various molecules, including esters, and have important functions in signal transduction and other cellular processes.

Esterases can also be used in industrial applications, such as in the production of biodiesel, detergents, and food additives. They are often produced by microbial fermentation or extracted from plants and animals. The use of esterases in biotechnology is an active area of research, with potential applications in biofuel production, bioremediation, and medical diagnostics.

Vanadates are salts or esters of vanadic acid (HVO3), which contains the vanadium(V) ion. They contain the vanadate ion (VO3-), which consists of one vanadium atom and three oxygen atoms. Vanadates have been studied for their potential insulin-mimetic and antidiabetic effects, as well as their possible cardiovascular benefits. However, more research is needed to fully understand their mechanisms of action and potential therapeutic uses in medicine.

Hydrolases are a class of enzymes that help facilitate the breakdown of various types of chemical bonds through a process called hydrolysis, which involves the addition of water. These enzymes catalyze the cleavage of bonds in substrates by adding a molecule of water, leading to the formation of two or more smaller molecules.

Hydrolases play a crucial role in many biological processes, including digestion, metabolism, and detoxification. They can act on a wide range of substrates, such as proteins, lipids, carbohydrates, and nucleic acids, breaking them down into smaller units that can be more easily absorbed or utilized by the body.

Examples of hydrolases include:

1. Proteases: enzymes that break down proteins into smaller peptides or amino acids.
2. Lipases: enzymes that hydrolyze lipids, such as triglycerides, into fatty acids and glycerol.
3. Amylases: enzymes that break down complex carbohydrates, like starches, into simpler sugars, such as glucose.
4. Nucleases: enzymes that cleave nucleic acids, such as DNA or RNA, into smaller nucleotides or oligonucleotides.
5. Phosphatases: enzymes that remove phosphate groups from various substrates, including proteins and lipids.
6. Esterases: enzymes that hydrolyze ester bonds in a variety of substrates, such as those found in some drugs or neurotransmitters.

Hydrolases are essential for maintaining proper cellular function and homeostasis, and their dysregulation can contribute to various diseases and disorders.

Hexosaminidases are a group of enzymes that play a crucial role in the breakdown of complex carbohydrates, specifically glycoproteins and glycolipids, in the human body. These enzymes are responsible for cleaving the terminal N-acetyl-D-glucosamine (GlcNAc) residues from these molecules during the process of glycosidase digestion.

There are several types of hexosaminidases, including Hexosaminidase A and Hexosaminidase B, which are encoded by different genes and have distinct functions. Deficiencies in these enzymes can lead to serious genetic disorders, such as Tay-Sachs disease and Sandhoff disease, respectively. These conditions are characterized by the accumulation of undigested glycolipids and glycoproteins in various tissues, leading to progressive neurological deterioration and other symptoms.

Receptor-like protein tyrosine phosphatases, class 3 (RPTPs, Class 3) are a subfamily of receptor-like protein tyrosine phosphatases that play crucial roles in various cellular processes, including cell growth, differentiation, and migration. These transmembrane enzymes are characterized by the presence of two extracellular carbonic anhydrase-like domains (CA domains), a single transmembrane region, and one or two intracellular protein tyrosine phosphatase (PTP) domains.

The RPTPs, Class 3 subfamily includes three members: PTPRG (also known as RPTPγ), PTPRD (RPTPδ), and PTPRS (RPTPσ). These proteins have been implicated in the regulation of neuronal development, synaptic plasticity, and tumorigenesis. They are involved in cell-cell adhesion and signaling through homophilic interactions between their extracellular CA domains and heterophilic interactions with various ligands, such as semaphorins, plexins, and collapsin response mediator proteins (CRMPs).

Upon activation, the intracellular PTP domains of RPTPs, Class 3 dephosphorylate specific tyrosine residues on their target proteins, thereby modulating various signaling pathways. Dysregulation of these phosphatases has been associated with several neurological disorders and cancers.

Enzyme repression is a type of gene regulation in which the production of an enzyme is inhibited or suppressed, thereby reducing the rate of catalysis of the chemical reaction that the enzyme facilitates. This process typically occurs when the end product of the reaction binds to the regulatory protein, called a repressor, which then binds to the operator region of the operon (a group of genes that are transcribed together) and prevents transcription of the structural genes encoding for the enzyme. Enzyme repression helps maintain homeostasis within the cell by preventing the unnecessary production of enzymes when they are not needed, thus conserving energy and resources.

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.

Organophosphorus compounds are a class of chemical substances that contain phosphorus bonded to organic compounds. They are used in various applications, including as plasticizers, flame retardants, pesticides (insecticides, herbicides, and nerve gases), and solvents. In medicine, they are also used in the treatment of certain conditions such as glaucoma. However, organophosphorus compounds can be toxic to humans and animals, particularly those that affect the nervous system by inhibiting acetylcholinesterase, an enzyme that breaks down the neurotransmitter acetylcholine. Exposure to these compounds can cause symptoms such as nausea, vomiting, muscle weakness, and in severe cases, respiratory failure and death.

Semen is a complex, whitish fluid that is released from the male reproductive system during ejaculation. It is produced by several glands, including the seminal vesicles, prostate gland, and bulbourethral glands. Semen contains several components, including sperm (the male reproductive cells), as well as various proteins, enzymes, vitamins, and minerals. Its primary function is to transport sperm through the female reproductive tract during sexual intercourse, providing nutrients and aiding in the protection of the sperm as they travel toward the egg for fertilization.

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.

Arylsulfatases are a group of enzymes that play a role in the breakdown and recycling of complex molecules in the body. Specifically, they catalyze the hydrolysis of sulfate ester bonds in certain types of large sugar molecules called glycosaminoglycans (GAGs).

There are several different types of arylsulfatases, each of which targets a specific type of sulfate ester bond. For example, arylsulfatase A is responsible for breaking down sulfate esters in a GAG called cerebroside sulfate, while arylsulfatase B targets a different GAG called dermatan sulfate.

Deficiencies in certain arylsulfatases can lead to genetic disorders. For example, a deficiency in arylsulfatase A can cause metachromatic leukodystrophy, a progressive neurological disorder that affects the nervous system and causes a range of symptoms including muscle weakness, developmental delays, and cognitive decline. Similarly, a deficiency in arylsulfatase B can lead to Maroteaux-Lamy syndrome, a rare genetic disorder that affects the skeleton, eyes, ears, heart, and other organs.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

"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.

Receptor-like protein tyrosine phosphatases, class 4 (RPTPs, Class 4) are a subfamily of transmembrane receptor proteins that possess tyrosine-specific phosphatase activity. They play crucial roles in various cellular processes, including cell growth, differentiation, and migration, by regulating the balance of protein tyrosine phosphorylation.

Class 4 RPTPs are characterized by the presence of two extracellular carbonic anhydrase-like domains (CA domains), a single transmembrane region, and one intracellular catalytic domain with tyrosine phosphatase activity. The extracellular CA domains are involved in mediating protein-protein interactions, while the intracellular domain regulates signaling pathways through dephosphorylation of specific tyrosine residues on target proteins.

There are four members in this class: RPTP-μ (PTPRM), RPTP-π (PTPRS), RPTP-ε (PTPRE), and RPTP-δ (PTPRD). Mutations in these genes have been associated with various human diseases, including neurological disorders, cancer, and immune dysfunction.

In summary, Receptor-like protein tyrosine phosphatases, class 4 are a group of transmembrane receptors that regulate cellular signaling through tyrosine dephosphorylation, with important roles in various physiological processes and disease states.

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.

Mitogen-Activated Protein Kinase Phosphatases (MAPK Phosphatases or MAPKPs) are a group of enzymes that play a crucial role in the regulation of Mitogen-Activated Protein Kinase (MAPK) signaling pathways. MAPKs are serine/threonine protein kinases involved in various cellular processes, including proliferation, differentiation, and apoptosis.

MAPK Phosphatases dephosphorylate and inactivate both the threonine and tyrosine residues of MAPKs, thereby acting as negative regulators of MAPK signaling cascades. There are three major subfamilies of MAPK Phosphatases:

1. DUSPs (Dual Specificity Phosphatases) - also known as MKPs (MAP Kinase Phosphatases)
2. CDC14s
3. PTENs (Phosphatase and Tensin Homologs)

Each subfamily has distinct substrate specificities, cellular localizations, and regulatory mechanisms. Dysregulation of MAPK Phosphatases can lead to various pathological conditions, such as cancer, inflammation, and neurodegenerative diseases. Therefore, understanding the function and regulation of MAPK Phosphatases is essential for developing novel therapeutic strategies targeting MAPK signaling pathways.

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.

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.

Nucleotidases are a class of enzymes that catalyze the hydrolysis of nucleotides into nucleosides and phosphate groups. Nucleotidases play important roles in various biological processes, including the regulation of nucleotide concentrations within cells, the salvage pathways for nucleotide synthesis, and the breakdown of nucleic acids during programmed cell death (apoptosis).

There are several types of nucleotidases that differ in their substrate specificity and subcellular localization. These include:

1. Nucleoside monophosphatases (NMPs): These enzymes hydrolyze nucleoside monophosphates (NMPs) into nucleosides and inorganic phosphate.
2. Nucleoside diphosphatases (NDPs): These enzymes hydrolyze nucleoside diphosphates (NDPs) into nucleoside monophosphates (NMPs) and inorganic phosphate.
3. Nucleoside triphosphatases (NTPs): These enzymes hydrolyze nucleoside triphosphates (NTPs) into nucleoside diphosphates (NDPs) and inorganic phosphate.
4. 5'-Nucleotidase: This enzyme specifically hydrolyzes the phosphate group from the 5' position of nucleoside monophosphates, producing nucleosides.
5. Pyrophosphatases: These enzymes hydrolyze pyrophosphates into two phosphate groups and play a role in regulating nucleotide metabolism.

Nucleotidases are widely distributed in nature and can be found in various tissues, organs, and biological fluids, including blood, urine, and cerebrospinal fluid. Dysregulation of nucleotidase activity has been implicated in several diseases, such as cancer, neurodegenerative disorders, and infectious diseases.

Organophosphates are a group of chemicals that include insecticides, herbicides, and nerve gases. They work by inhibiting an enzyme called acetylcholinesterase, which normally breaks down the neurotransmitter acetylcholine in the synapse between nerves. This leads to an overaccumulation of acetylcholine, causing overstimulation of the nervous system and resulting in a wide range of symptoms such as muscle twitching, nausea, vomiting, diarrhea, sweating, confusion, and potentially death due to respiratory failure. Organophosphates are highly toxic and their use is regulated due to the risks they pose to human health and the environment.

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.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

Thiamine pyrophosphatase (TPP) is an enzyme that catalyzes the hydrolysis of thiamine pyrophosphate (TPP), which is a cofactor involved in several important metabolic pathways, including carbohydrate metabolism and neurotransmitter synthesis.

The reaction catalyzed by TPP is:

thiamine pyrophosphate + H2O → thiamine + phosphate

TPP is also known as thiamine diphosphatase or vitamin B1 diphosphatase. Deficiency of this enzyme can lead to thiamine deficiency disorders such as beriberi and Wernicke-Korsakoff syndrome, which are characterized by neurological and cardiovascular symptoms.

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.

Organoids are 3D tissue cultures grown from stem cells that mimic the structure and function of specific organs. They are used in research to study development, disease, and potential treatments. The term "organoid" refers to the fact that these cultures can organize themselves into structures that resemble rudimentary organs, with differentiated cell types arranged in a pattern similar to their counterparts in the body. Organoids can be derived from various sources, including embryonic stem cells, induced pluripotent stem cells (iPSCs), or adult stem cells, and they provide a valuable tool for studying complex biological processes in a controlled laboratory setting.

Dual specificity phosphatase 6 (DUSP6), also known as MAP kinase phosphatase 3 (MKP3), is a type of enzyme that belongs to the dual specificity phosphatase family. These enzymes are capable of removing phosphate groups from both tyrosine and threonine/serine residues on their target proteins, including mitogen-activated protein kinases (MAPKs).

DUSP6 specifically dephosphorylates and inactivates extracellular signal-regulated kinase 1 and 2 (ERK1/2), which are MAPKs that play crucial roles in various cellular processes such as proliferation, differentiation, and survival. By negatively regulating ERK1/2 signaling, DUSP6 helps maintain the balance of this pathway and prevents excessive or aberrant activation, which can contribute to diseases like cancer.

DUSP6 is primarily localized in the nucleus and is involved in various cellular responses, including the negative feedback regulation of ERK1/2 signaling upon growth factor stimulation. Dysregulation of DUSP6 has been implicated in several pathological conditions, including cancer and neurological disorders.

Protein Tyrosine Phosphatase, Non-Receptor Type 2 (PTPN2) is a type of enzyme that belongs to the protein tyrosine phosphatase (PTP) family. PTPs play a crucial role in regulating various cellular processes by removing phosphate groups from phosphorylated tyrosine residues on proteins, thereby controlling their activity.

PTPN2 is a non-receptor type of PTP, meaning it does not have a transmembrane domain and is found in the cytoplasm of cells. It specifically dephosphorylates and regulates the activity of various signaling proteins, including receptor tyrosine kinases (RTKs), JAK kinases, and STAT transcription factors.

PTPN2 has been implicated in several cellular processes, such as regulation of immune responses, insulin signaling, and cell growth and differentiation. Mutations in the PTPN2 gene have been associated with various diseases, including autoimmune disorders, cancer, and diabetes.

I'm sorry for any confusion, but "Oxazoles" is not a medical term, it is a chemical term. Oxazoles are heterocyclic aromatic organic compounds that contain a five-membered ring made up of one nitrogen atom, one oxygen atom, and three carbon atoms. They have the molecular formula C4H4NO.

Oxazoles do not have specific medical relevance, but they can be found in some natural and synthetic substances, including certain drugs and bioactive molecules. Some oxazole-containing compounds have been studied for their potential medicinal properties, such as anti-inflammatory, antimicrobial, and anticancer activities. However, these studies are primarily within the field of chemistry and pharmacology, not medicine itself.

Prostatic neoplasms refer to abnormal growths in the prostate gland, which can be benign or malignant. The term "neoplasm" simply means new or abnormal tissue growth. When it comes to the prostate, neoplasms are often referred to as tumors.

Benign prostatic neoplasms, such as prostate adenomas, are non-cancerous overgrowths of prostate tissue. They usually grow slowly and do not spread to other parts of the body. While they can cause uncomfortable symptoms like difficulty urinating, they are generally not life-threatening.

Malignant prostatic neoplasms, on the other hand, are cancerous growths. The most common type of prostate cancer is adenocarcinoma, which arises from the glandular cells in the prostate. Prostate cancer often grows slowly and may not cause any symptoms for many years. However, some types of prostate cancer can be aggressive and spread quickly to other parts of the body, such as the bones or lymph nodes.

It's important to note that while prostate neoplasms can be concerning, early detection and treatment can significantly improve outcomes for many men. Regular check-ups with a healthcare provider are key to monitoring prostate health and catching any potential issues early on.

Metalloproteins are proteins that contain one or more metal ions as a cofactor, which is required for their biological activity. These metal ions play crucial roles in the catalytic function, structural stability, and electron transfer processes of metalloproteins. The types of metals involved can include iron, zinc, copper, magnesium, calcium, or manganese, among others. Examples of metalloproteins are hemoglobin (contains heme-bound iron), cytochrome c (contains heme-bound iron and functions in electron transfer), and carbonic anhydrase (contains zinc and catalyzes the conversion between carbon dioxide and bicarbonate).

SH2 (Src homology 2) domain-containing protein tyrosine phosphatases (PTPs) are a family of enzymes that play crucial roles in regulating various cellular processes, including cell growth, differentiation, and survival. These enzymes are characterized by the presence of SH2 domains, which bind to specific phosphorylated tyrosine residues on other proteins, and protein tyrosine phosphatase (PTP) domains, which catalyze the removal of phosphate groups from tyrosine residues.

SH2 domain-containing PTPs can be further divided into two subfamilies: the SH2 domain-containing PTP1 (PTP1B) family and the SH2 domain-containing PTP2 (SHP) family. The PTP1B family includes PTP1B, TCPTP (T-cell protein tyrosine phosphatase), and MEG2 (Megakaryocyte-associated tyrosine phosphatase). These enzymes primarily function as negative regulators of various signaling pathways by dephosphorylating activated receptor tyrosine kinases, such as the insulin receptor and epidermal growth factor receptor.

The SHP family includes SHP1 (PTPN6) and SHP2 (PTPN11). These enzymes contain two SH2 domains and a PTP domain. They play essential roles in regulating various signaling pathways, including those involved in hematopoiesis, immune cell function, and cancer. Unlike the PTP1B family members, SHP1 and SHP2 can act as both positive and negative regulators of signaling pathways, depending on the context.

Dysregulation of SH2 domain-containing PTPs has been implicated in various diseases, including diabetes, cancer, and immune disorders. Therefore, these enzymes represent potential targets for therapeutic intervention.

Leucyl aminopeptidase (LAP) is an enzyme that plays a role in the metabolism and breakdown of proteins. It is found in various tissues and organs throughout the body, including the small intestine, liver, and kidneys. LAP specifically catalyzes the removal of leucine, a type of amino acid, from the N-terminus (the beginning) of peptides and proteins. This enzyme is important for the proper digestion and absorption of dietary proteins, as well as for the regulation of various physiological processes in the body. Abnormal levels or activity of LAP have been implicated in certain diseases, such as cancer and liver disease.

Calcineurin is a calcium-calmodulin-activated serine/threonine protein phosphatase that plays a crucial role in signal transduction pathways involved in immune response and neuronal development. It consists of two subunits: the catalytic A subunit (calcineurin A) and the regulatory B subunit (calcineurin B). Calcineurin is responsible for dephosphorylating various substrates, including transcription factors, which leads to changes in their activity and ultimately affects gene expression. In the immune system, calcineurin plays a critical role in T-cell activation by dephosphorylating the nuclear factor of activated T-cells (NFAT), allowing it to translocate into the nucleus and induce the expression of cytokines and other genes involved in the immune response. Inhibitors of calcineurin, such as cyclosporine A and tacrolimus, are commonly used as immunosuppressive drugs to prevent organ rejection after transplantation.

6-Phytase is an enzyme that catalyzes the hydrolysis of phytic acid (myo-inositol hexakisphosphate), a major storage form of phosphorus in plants, into inorganic phosphate and lower molecular weight myo-inositol phosphates. This enzymatic reaction releases phosphate and micronutrients, making them more available for absorption in the gastrointestinal tract of monogastric animals, such as pigs, poultry, and fish. The "6" in 6-Phytase refers to the position of the phosphate group that is cleaved from the myo-inositol ring. This enzyme has significant applications in animal nutrition and feed industry to improve nutrient utilization and reduce phosphorus pollution in the environment.

Macrophages are a type of white blood cell that are an essential part of the immune system. They are large, specialized cells that engulf and destroy foreign substances, such as bacteria, viruses, parasites, and fungi, as well as damaged or dead cells. Macrophages are found throughout the body, including in the bloodstream, lymph nodes, spleen, liver, lungs, and connective tissues. They play a critical role in inflammation, immune response, and tissue repair and remodeling.

Macrophages originate from monocytes, which are a type of white blood cell produced in the bone marrow. When monocytes enter the tissues, they differentiate into macrophages, which have a larger size and more specialized functions than monocytes. Macrophages can change their shape and move through tissues to reach sites of infection or injury. They also produce cytokines, chemokines, and other signaling molecules that help coordinate the immune response and recruit other immune cells to the site of infection or injury.

Macrophages have a variety of surface receptors that allow them to recognize and respond to different types of foreign substances and signals from other cells. They can engulf and digest foreign particles, bacteria, and viruses through a process called phagocytosis. Macrophages also play a role in presenting antigens to T cells, which are another type of immune cell that helps coordinate the immune response.

Overall, macrophages are crucial for maintaining tissue homeostasis, defending against infection, and promoting wound healing and tissue repair. Dysregulation of macrophage function has been implicated in a variety of diseases, including cancer, autoimmune disorders, and chronic inflammatory conditions.

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.

Acetylglucosaminidase (ACG) is an enzyme that catalyzes the hydrolysis of N-acetyl-beta-D-glucosaminides, which are found in glycoproteins and glycolipids. This enzyme plays a crucial role in the degradation and recycling of these complex carbohydrates within the body.

Deficiency or malfunction of Acetylglucosaminidase can lead to various genetic disorders, such as mucolipidosis II (I-cell disease) and mucolipidosis III (pseudo-Hurler polydystrophy), which are characterized by the accumulation of glycoproteins and glycolipids in lysosomes, resulting in cellular dysfunction and progressive damage to multiple organs.

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).

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

"Escherichia" is a genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that are commonly found in the intestines of warm-blooded organisms. The most well-known species in this genus is "Escherichia coli," or "E. coli," which is a normal inhabitant of the human gut and is often used as an indicator of fecal contamination in water and food. Some strains of E. coli can cause illness, however, including diarrhea, urinary tract infections, and meningitis. Other species in the genus "Escherichia" are less well-known and are not typically associated with disease.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Cathepsin K is a proteolytic enzyme, which belongs to the family of papain-like cysteine proteases. It is primarily produced by osteoclasts, which are specialized cells responsible for bone resorption. Cathepsin K plays a crucial role in the degradation and remodeling of the extracellular matrix, particularly in bone tissue.

This enzyme is capable of breaking down various proteins, including collagen, elastin, and proteoglycans, which are major components of the bone matrix. By doing so, cathepsin K helps osteoclasts to dissolve and remove mineralized and non-mineralized bone matrix during the process of bone resorption.

Apart from its function in bone metabolism, cathepsin K has also been implicated in several pathological conditions, such as osteoporosis, rheumatoid arthritis, and tumor metastasis to bones. Inhibitors of cathepsin K are being investigated as potential therapeutic agents for the treatment of these disorders.

Clinical enzyme tests are laboratory tests that measure the amount or activity of certain enzymes in biological samples, such as blood or bodily fluids. These tests are used to help diagnose and monitor various medical conditions, including organ damage, infection, inflammation, and genetic disorders.

Enzymes are proteins that catalyze chemical reactions in the body. Some enzymes are found primarily within specific organs or tissues, so elevated levels of these enzymes in the blood can indicate damage to those organs or tissues. For example, high levels of creatine kinase (CK) may suggest muscle damage, while increased levels of aspartate aminotransferase (AST) and alanine aminotransferase (ALT) can indicate liver damage.

There are several types of clinical enzyme tests, including:

1. Serum enzyme tests: These measure the level of enzymes in the blood serum, which is the liquid portion of the blood after clotting. Examples include CK, AST, ALT, alkaline phosphatase (ALP), and lactate dehydrogenase (LDH).
2. Urine enzyme tests: These measure the level of enzymes in the urine. An example is N-acetyl-β-D-glucosaminidase (NAG), which can indicate kidney damage.
3. Enzyme immunoassays (EIAs): These use antibodies to detect and quantify specific enzymes or proteins in a sample. They are often used for the diagnosis of infectious diseases, such as HIV or hepatitis.
4. Genetic enzyme tests: These can identify genetic mutations that cause deficiencies in specific enzymes, leading to inherited metabolic disorders like phenylketonuria (PKU) or Gaucher's disease.

It is important to note that the interpretation of clinical enzyme test results should be done by a healthcare professional, taking into account the patient's medical history, symptoms, and other diagnostic tests.

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.

PTEN phosphohydrolase, also known as PTEN protein or phosphatase and tensin homolog deleted on chromosome ten, is a tumor suppressor protein that plays a crucial role in regulating cell growth and division. It works by dephosphorylating (removing a phosphate group from) the lipid second messenger PIP3, which is involved in signaling pathways that promote cell proliferation and survival. By negatively regulating these pathways, PTEN helps to prevent uncontrolled cell growth and tumor formation. Mutations in the PTEN gene can lead to a variety of cancer types, including breast, prostate, and endometrial cancer.

Cell differentiation is the process by which a less specialized cell, or stem cell, becomes a more specialized cell type with specific functions and structures. This process involves changes in gene expression, which are regulated by various intracellular signaling pathways and transcription factors. Differentiation results in the development of distinct cell types that make up tissues and organs in multicellular organisms. It is a crucial aspect of embryonic development, tissue repair, and maintenance of homeostasis in the body.

In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.

For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.

Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.

Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.

Glycogen Synthase-D Phosphatase is not a commonly used medical term, but I can provide you with some information about Glycogen Synthase and Phosphatases that might help.

Glycogen synthase is an enzyme that plays a crucial role in the synthesis of glycogen, which is a form of energy storage in the body, mainly in the liver and muscles. The activity of this enzyme is regulated by phosphorylation and dephosphorylation, which are chemical reactions that add or remove phosphate groups to/from the enzyme, respectively.

Phosphatases are a group of enzymes that catalyze the removal of phosphate groups from various substrates, including proteins like glycogen synthase. Specifically, Glycogen Synthase-D Phosphatase refers to a type of phosphatase that dephosphorylates and activates glycogen synthase by removing phosphate groups from it. This activation leads to increased glycogen synthesis in the body.

Therefore, Glycogen Synthase-D Phosphatase is an enzyme responsible for dephosphorylating and activating glycogen synthase, thereby promoting glycogen storage in the body.

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.

The Golgi apparatus, also known as the Golgi complex or simply the Golgi, is a membrane-bound organelle found in the cytoplasm of most eukaryotic cells. It plays a crucial role in the processing, sorting, and packaging of proteins and lipids for transport to their final destinations within the cell or for secretion outside the cell.

The Golgi apparatus consists of a series of flattened, disc-shaped sacs called cisternae, which are stacked together in a parallel arrangement. These stacks are often interconnected by tubular structures called tubules or vesicles. The Golgi apparatus has two main faces: the cis face, which is closest to the endoplasmic reticulum (ER) and receives proteins and lipids directly from the ER; and the trans face, which is responsible for sorting and dispatching these molecules to their final destinations.

The Golgi apparatus performs several essential functions in the cell:

1. Protein processing: After proteins are synthesized in the ER, they are transported to the cis face of the Golgi apparatus, where they undergo various post-translational modifications, such as glycosylation (the addition of sugar molecules) and sulfation. These modifications help determine the protein's final structure, function, and targeting.
2. Lipid modification: The Golgi apparatus also modifies lipids by adding or removing different functional groups, which can influence their properties and localization within the cell.
3. Protein sorting and packaging: Once proteins and lipids have been processed, they are sorted and packaged into vesicles at the trans face of the Golgi apparatus. These vesicles then transport their cargo to various destinations, such as lysosomes, plasma membrane, or extracellular space.
4. Intracellular transport: The Golgi apparatus serves as a central hub for intracellular trafficking, coordinating the movement of vesicles and other transport carriers between different organelles and cellular compartments.
5. Cell-cell communication: Some proteins that are processed and packaged in the Golgi apparatus are destined for secretion, playing crucial roles in cell-cell communication and maintaining tissue homeostasis.

In summary, the Golgi apparatus is a vital organelle involved in various cellular processes, including post-translational modification, sorting, packaging, and intracellular transport of proteins and lipids. Its proper functioning is essential for maintaining cellular homeostasis and overall organismal health.

Receptor Activator of Nuclear Factor-kappa B (RANK) is a type I transmembrane protein and a member of the tumor necrosis factor receptor superfamily. It plays a crucial role in the regulation of bone metabolism through the activation of osteoclasts, which are cells responsible for bone resorption.

When RANK binds to its ligand, RANKL (Receptor Activator of Nuclear Factor-kappa B Ligand), it triggers a series of intracellular signaling events that lead to the activation and differentiation of osteoclast precursors into mature osteoclasts. This process is essential for maintaining bone homeostasis, as excessive osteoclast activity can result in bone loss and diseases such as osteoporosis.

In addition to its role in bone metabolism, RANK has also been implicated in the regulation of immune responses, as it is involved in the activation and differentiation of dendritic cells and T cells. Dysregulation of RANK signaling has been associated with various pathological conditions, including autoimmune diseases and cancer.

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.

Microcystins are a type of toxin produced by certain species of blue-green algae (cyanobacteria) that can contaminate freshwater bodies. They are cyclic peptides consisting of seven amino acids, and their structure varies among different microcystin variants. These toxins can have negative effects on the liver and other organs in humans and animals upon exposure through ingestion, inhalation, or skin contact with contaminated water. They are a concern for both public health and environmental safety, particularly in relation to drinking water supplies, recreational water use, and aquatic ecosystems.

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.

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.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

Tyrosine is an non-essential amino acid, which means that it can be synthesized by the human body from another amino acid called phenylalanine. Its name is derived from the Greek word "tyros," which means cheese, as it was first isolated from casein, a protein found in cheese.

Tyrosine plays a crucial role in the production of several important substances in the body, including neurotransmitters such as dopamine, norepinephrine, and epinephrine, which are involved in various physiological processes, including mood regulation, stress response, and cognitive functions. It also serves as a precursor to melanin, the pigment responsible for skin, hair, and eye color.

In addition, tyrosine is involved in the structure of proteins and is essential for normal growth and development. Some individuals may require tyrosine supplementation if they have a genetic disorder that affects tyrosine metabolism or if they are phenylketonurics (PKU), who cannot metabolize phenylalanine, which can lead to elevated tyrosine levels in the blood. However, it is important to consult with a healthcare professional before starting any supplementation regimen.

Receptor-like protein tyrosine phosphatases, class 5 (RPTPs-Class 5), also known as R7 family or PTP receptor type R, are a subfamily of receptor-like protein tyrosine phosphatases (RPTPs) that play crucial roles in various cellular processes, including cell growth, differentiation, and migration. These transmembrane enzymes are characterized by the presence of two extracellular carbonic anhydrase-like domains (CA domains), a single membrane-spanning region, and one intracellular protein tyrosine phosphatase domain.

The RPTPs-Class 5 includes four members in humans: PTPRF (also known as LAR), PTPRF-B (or LAR2), PTPRJ (or PTP receptor type J), and PTPRK (or PTP receptor type K). These phosphatases have the ability to dephosphorylate tyrosine residues on their target proteins, thereby regulating various signaling pathways. Dysregulation of RPTPs-Class 5 has been implicated in several diseases, including cancer and neurological disorders.

In summary, Receptor-like protein tyrosine phosphatases, class 5 are a group of transmembrane enzymes that regulate cellular processes by dephosphorylating tyrosine residues on target proteins, playing essential roles in maintaining proper cell function and homeostasis.

Vacuoles are membrane-bound organelles found in the cells of most eukaryotic organisms. They are essentially fluid-filled sacs that store various substances, such as enzymes, waste products, and nutrients. In plants, vacuoles often contain water, ions, and various organic compounds, while in fungi, they may store lipids or pigments. Vacuoles can also play a role in maintaining the turgor pressure of cells, which is critical for cell shape and function.

In animal cells, vacuoles are typically smaller and less numerous than in plant cells. Animal cells have lysosomes, which are membrane-bound organelles that contain digestive enzymes and break down waste materials, cellular debris, and foreign substances. Lysosomes can be considered a type of vacuole, but they are more specialized in their function.

Overall, vacuoles are essential for maintaining the health and functioning of cells by providing a means to store and dispose of various substances.

"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.

Intracellular signaling peptides and proteins are molecules that play a crucial role in transmitting signals within cells, which ultimately lead to changes in cell behavior or function. These signals can originate from outside the cell (extracellular) or within the cell itself. Intracellular signaling molecules include various types of peptides and proteins, such as:

1. G-protein coupled receptors (GPCRs): These are seven-transmembrane domain receptors that bind to extracellular signaling molecules like hormones, neurotransmitters, or chemokines. Upon activation, they initiate a cascade of intracellular signals through G proteins and secondary messengers.
2. Receptor tyrosine kinases (RTKs): These are transmembrane receptors that bind to growth factors, cytokines, or hormones. Activation of RTKs leads to autophosphorylation of specific tyrosine residues, creating binding sites for intracellular signaling proteins such as adapter proteins, phosphatases, and enzymes like Ras, PI3K, and Src family kinases.
3. Second messenger systems: Intracellular second messengers are small molecules that amplify and propagate signals within the cell. Examples include cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP), diacylglycerol (DAG), inositol triphosphate (IP3), calcium ions (Ca2+), and nitric oxide (NO). These second messengers activate or inhibit various downstream effectors, leading to changes in cellular responses.
4. Signal transduction cascades: Intracellular signaling proteins often form complex networks of interacting molecules that relay signals from the plasma membrane to the nucleus. These cascades involve kinases (protein kinases A, B, C, etc.), phosphatases, and adapter proteins, which ultimately regulate gene expression, cell cycle progression, metabolism, and other cellular processes.
5. Ubiquitination and proteasome degradation: Intracellular signaling pathways can also control protein stability by modulating ubiquitin-proteasome degradation. E3 ubiquitin ligases recognize specific substrates and conjugate them with ubiquitin molecules, targeting them for proteasomal degradation. This process regulates the abundance of key signaling proteins and contributes to signal termination or amplification.

In summary, intracellular signaling pathways involve a complex network of interacting proteins that relay signals from the plasma membrane to various cellular compartments, ultimately regulating gene expression, metabolism, and other cellular processes. Dysregulation of these pathways can contribute to disease development and progression, making them attractive targets for therapeutic intervention.

Osteocalcin is a protein that is produced by osteoblasts, which are the cells responsible for bone formation. It is one of the most abundant non-collagenous proteins found in bones and plays a crucial role in the regulation of bone metabolism. Osteocalcin contains a high affinity for calcium ions, making it essential for the mineralization of the bone matrix.

Once synthesized, osteocalcin is secreted into the extracellular matrix, where it binds to hydroxyapatite crystals, helping to regulate their growth and contributing to the overall strength and integrity of the bones. Osteocalcin also has been found to play a role in other physiological processes outside of bone metabolism, such as modulating insulin sensitivity, energy metabolism, and male fertility.

In summary, osteocalcin is a protein produced by osteoblasts that plays a critical role in bone formation, mineralization, and turnover, and has been implicated in various other physiological processes.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Glycoproteins are complex proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. These glycans are linked to the protein through asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycoproteins play crucial roles in various biological processes, including cell recognition, cell-cell interactions, cell adhesion, and signal transduction. They are widely distributed in nature and can be found on the outer surface of cell membranes, in extracellular fluids, and as components of the extracellular matrix. The structure and composition of glycoproteins can vary significantly depending on their function and location within an organism.

Cantharidin is a toxic substance that is produced by several species of beetles, including the blister beetle. It has been used in medicine as a topical vesicant or blistering agent to treat warts and other skin conditions. Cantharidin works by causing irritation and inflammation of the skin, which leads to the formation of a blister. This can help to remove the affected skin and promote healing.

It is important to note that cantharidin is a potent toxic substance and should only be used under the supervision of a qualified healthcare professional. It can cause serious side effects if it is not used properly, including severe burns, scarring, and allergic reactions. Cantharidin is not approved for use in the United States, and its use is generally discouraged due to the risks associated with it.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Cytoplasmic granules are small, membrane-bound organelles or inclusions found within the cytoplasm of cells. They contain various substances such as proteins, lipids, carbohydrates, and genetic material. Cytoplasmic granules have diverse functions depending on their specific composition and cellular location. Some examples include:

1. Secretory granules: These are found in secretory cells and store hormones, neurotransmitters, or enzymes before they are released by exocytosis.
2. Lysosomes: These are membrane-bound organelles that contain hydrolytic enzymes for intracellular digestion of waste materials, foreign substances, and damaged organelles.
3. Melanosomes: Found in melanocytes, these granules produce and store the pigment melanin, which is responsible for skin, hair, and eye color.
4. Weibel-Palade bodies: These are found in endothelial cells and store von Willebrand factor and P-selectin, which play roles in hemostasis and inflammation.
5. Peroxisomes: These are single-membrane organelles that contain enzymes for various metabolic processes, such as β-oxidation of fatty acids and detoxification of harmful substances.
6. Lipid bodies (also called lipid droplets): These are cytoplasmic granules that store neutral lipids, such as triglycerides and cholesteryl esters. They play a role in energy metabolism and intracellular signaling.
7. Glycogen granules: These are cytoplasmic inclusions that store glycogen, a polysaccharide used for energy storage in animals.
8. Protein bodies: Found in plants, these granules store excess proteins and help regulate protein homeostasis within the cell.
9. Electron-dense granules: These are found in certain immune cells, such as mast cells and basophils, and release mediators like histamine during an allergic response.
10. Granules of unknown composition or function may also be present in various cell types.

Protein kinases are a group of enzymes that play a crucial role in many cellular processes by adding phosphate groups to other proteins, a process known as phosphorylation. This modification can activate or deactivate the target protein's function, thereby regulating various signaling pathways within the cell. Protein kinases are essential for numerous biological functions, including metabolism, signal transduction, cell cycle progression, and apoptosis (programmed cell death). Abnormal regulation of protein kinases has been implicated in several diseases, such as cancer, diabetes, and neurological disorders.

Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.

Protein Tyrosine Phosphatase, Non-Receptor Type 12 (PTPN12) is a protein belonging to the family of protein tyrosine phosphatases (PTPs), which are enzymes that regulate various cellular processes by removing phosphate groups from phosphorylated tyrosine residues on proteins. PTPN12, specifically, is a non-receptor type PTP, meaning it does not have a transmembrane domain and is found in the cytosol of the cell.

PTPN12 plays crucial roles in several signaling pathways that regulate cell growth, differentiation, migration, and survival. It has been shown to dephosphorylate and negatively regulate various proteins, including Src family kinases (SFKs), receptor tyrosine kinases (RTKs), and adaptor proteins. Dysregulation of PTPN12 has been implicated in several diseases, such as cancer, where its expression is often reduced or lost, leading to increased activation of oncogenic signaling pathways.

Dual Specificity Phosphatase 3 (DUSP3), also known as Phosphatase of Regenerating Liver-3 (PRL-3), is a protein that belongs to the dual specificity phosphatase family. These enzymes are capable of dephosphorylating both tyrosine and serine/threonine residues on their target proteins, thereby regulating various cellular processes such as signal transduction, cell growth, differentiation, and survival.

DUSP3 specifically dephosphorylates and inactivates members of the mitogen-activated protein kinase (MAPK) family, including extracellular signal-regulated kinases (ERKs), c-Jun N-terminal kinases (JNKs), and p38 MAPKs. These MAPKs play crucial roles in various cellular responses to external stimuli, such as growth factors, hormones, and stress. By negatively regulating MAPK signaling, DUSP3 helps maintain the balance of these pathways and prevents excessive or aberrant activation.

Dysregulation of DUSP3 has been implicated in several diseases, including cancer. Overexpression of DUSP3 has been observed in various tumor types, where it may contribute to tumor progression by promoting cell proliferation, survival, and metastasis. On the other hand, loss or downregulation of DUSP3 has also been associated with tumorigenesis, suggesting a complex role for this phosphatase in cancer development and progression.

A catalytic domain is a portion or region within a protein that contains the active site, where the chemical reactions necessary for the protein's function are carried out. This domain is responsible for the catalysis of biological reactions, hence the name "catalytic domain." The catalytic domain is often composed of specific amino acid residues that come together to form the active site, creating a unique three-dimensional structure that enables the protein to perform its specific function.

In enzymes, for example, the catalytic domain contains the residues that bind and convert substrates into products through chemical reactions. In receptors, the catalytic domain may be involved in signal transduction or other regulatory functions. Understanding the structure and function of catalytic domains is crucial to understanding the mechanisms of protein function and can provide valuable insights for drug design and therapeutic interventions.

Peroxidases are a group of enzymes that catalyze the oxidation of various substrates using hydrogen peroxide (H2O2) as the electron acceptor. These enzymes contain a heme prosthetic group, which plays a crucial role in their catalytic activity. Peroxidases are widely distributed in nature and can be found in plants, animals, and microorganisms. They play important roles in various biological processes, including defense against oxidative stress, lignin degradation, and host-pathogen interactions. Some common examples of peroxidases include glutathione peroxidase, which helps protect cells from oxidative damage, and horseradish peroxidase, which is often used in laboratory research.

Osteoblasts are specialized bone-forming cells that are derived from mesenchymal stem cells. They play a crucial role in the process of bone formation and remodeling. Osteoblasts synthesize, secrete, and mineralize the organic matrix of bones, which is mainly composed of type I collagen.

These cells have receptors for various hormones and growth factors that regulate their activity, such as parathyroid hormone, vitamin D, and transforming growth factor-beta. When osteoblasts are not actively producing bone matrix, they can become trapped within the matrix they produce, where they differentiate into osteocytes, which are mature bone cells that play a role in maintaining bone structure and responding to mechanical stress.

Abnormalities in osteoblast function can lead to various bone diseases, such as osteoporosis, osteogenesis imperfecta, and Paget's disease of bone.

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.

Receptor-like protein tyrosine phosphatases (RPTPs) are a subclass of protein tyrosine phosphatases that possess an extracellular domain, a transmembrane domain, and an intracellular domain with tyrosine phosphatase activity. They play crucial roles in various cellular processes, including cell growth, differentiation, migration, and survival, by regulating the balance of protein tyrosine phosphorylation. RPTPs can act as receptors, interacting with extracellular ligands to initiate intracellular signaling cascades. Dysregulation of RPTPs has been implicated in several human diseases, including cancer and neurological disorders.

Phosphorus is an essential mineral that is required by every cell in the body for normal functioning. It is a key component of several important biomolecules, including adenosine triphosphate (ATP), which is the primary source of energy for cells, and deoxyribonucleic acid (DNA) and ribonucleic acid (RNA), which are the genetic materials in cells.

Phosphorus is also a major constituent of bones and teeth, where it combines with calcium to provide strength and structure. In addition, phosphorus plays a critical role in various metabolic processes, including energy production, nerve impulse transmission, and pH regulation.

The medical definition of phosphorus refers to the chemical element with the atomic number 15 and the symbol P. It is a highly reactive non-metal that exists in several forms, including white phosphorus, red phosphorus, and black phosphorus. In the body, phosphorus is primarily found in the form of organic compounds, such as phospholipids, phosphoproteins, and nucleic acids.

Abnormal levels of phosphorus in the body can lead to various health problems. For example, high levels of phosphorus (hyperphosphatemia) can occur in patients with kidney disease or those who consume large amounts of phosphorus-rich foods, and can contribute to the development of calcification of soft tissues and cardiovascular disease. On the other hand, low levels of phosphorus (hypophosphatemia) can occur in patients with malnutrition, vitamin D deficiency, or alcoholism, and can lead to muscle weakness, bone pain, and an increased risk of infection.

"Morganella morganii" is a species of gram-negative, facultatively anaerobic, rod-shaped bacteria that is commonly found in the environment, including in soil, water, and associated with various animals. In humans, it can be part of the normal gut flora but can also cause infections, particularly in immunocompromised individuals or following surgical procedures. It is known to cause a variety of infections, such as urinary tract infections, wound infections, pneumonia, and bacteremia (bloodstream infection). The bacteria can produce a number of virulence factors, including enzymes that help it evade the host's immune system and cause tissue damage. It is resistant to many antibiotics, which can make treatment challenging.

Phenolphthalein is not strictly a medical term, but it is a chemical compound that has been used in medical contexts. It's primarily known for its use as an acid-base indicator in chemistry and medical laboratory tests. Here's the general definition:

Phenolphthalein is a crystalline compound, commonly available as a colorless powder or clear liquid. It is used as a pH indicator, turning pink to purple in basic solutions (pH above 8.2) and colorless in acidic solutions (pH below 8.2). This property makes it useful in various applications, such as titrations and monitoring the pH of chemical reactions or solutions.

In a medical context, phenolphthalein has historically been used as an active ingredient in certain over-the-counter laxatives. However, due to concerns about potential carcinogenicity and other side effects, its use in pharmaceuticals has been largely discontinued or restricted in many countries, including the United States.

Phosphotyrosine is not a medical term per se, but rather a biochemical term used in the field of medicine and life sciences.

Phosphotyrosine is a post-translational modification of tyrosine residues in proteins, where a phosphate group is added to the hydroxyl side chain of tyrosine by protein kinases. This modification plays a crucial role in intracellular signaling pathways and regulates various cellular processes such as cell growth, differentiation, and apoptosis. Abnormalities in phosphotyrosine-mediated signaling have been implicated in several diseases, including cancer and diabetes.

Cell biology is the branch of biology that deals with the study of cells, which are the basic units of life. It involves understanding the structure, function, and behavior of cells, as well as their interactions with one another and with their environment. Cell biologists may study various aspects of cellular processes, such as cell growth and division, metabolism, gene expression, signal transduction, and intracellular transport. They use a variety of techniques, including microscopy, biochemistry, genetics, and molecular biology, to investigate the complex and dynamic world inside cells. The ultimate goal of cell biology is to gain a deeper understanding of how cells work, which can have important implications for human health and disease.

Osteoprotegerin (OPG) is a soluble decoy receptor for the receptor activator of nuclear factor kappa-B ligand (RANKL). It is a member of the tumor necrosis factor (TNF) receptor superfamily and plays a crucial role in regulating bone metabolism. By binding to RANKL, OPG prevents it from interacting with its signaling receptor RANK on the surface of osteoclast precursor cells, thereby inhibiting osteoclast differentiation, activation, and survival. This results in reduced bone resorption and increased bone mass.

In addition to its role in bone homeostasis, OPG has also been implicated in various physiological and pathological processes, including immune regulation, cancer progression, and cardiovascular disease.

Ion exchange chromatography is a type of chromatography technique used to separate and analyze charged molecules (ions) based on their ability to exchange bound ions in a solid resin or gel with ions of similar charge in the mobile phase. The stationary phase, often called an ion exchanger, contains fixed ated functional groups that can attract counter-ions of opposite charge from the sample mixture.

In this technique, the sample is loaded onto an ion exchange column containing the charged resin or gel. As the sample moves through the column, ions in the sample compete for binding sites on the stationary phase with ions already present in the column. The ions that bind most strongly to the stationary phase will elute (come off) slower than those that bind more weakly.

Ion exchange chromatography can be performed using either cation exchangers, which exchange positive ions (cations), or anion exchangers, which exchange negative ions (anions). The pH and ionic strength of the mobile phase can be adjusted to control the binding and elution of specific ions.

Ion exchange chromatography is widely used in various applications such as water treatment, protein purification, and chemical analysis.

Hairy cell leukemia (HCL) is a rare, slow-growing type of cancer in which the bone marrow makes too many B cells (a type of white blood cell). These excess B cells are often referred to as "hairy cells" because they look abnormal under the microscope, with fine projections or "hair-like" cytoplasmic protrusions.

In HCL, these abnormal B cells can build up in the bone marrow and spleen, causing both of them to enlarge. The accumulation of hairy cells in the bone marrow can crowd out healthy blood cells, leading to a shortage of red blood cells (anemia), platelets (thrombocytopenia), and normal white blood cells (leukopenia). This can result in fatigue, increased risk of infection, and easy bruising or bleeding.

HCL is typically an indolent disease, meaning that it progresses slowly over time. However, some cases may require treatment to manage symptoms and prevent complications. Treatment options for HCL include chemotherapy, immunotherapy, targeted therapy, and stem cell transplantation. Regular follow-up with a healthcare provider is essential to monitor the disease's progression and adjust treatment plans as needed.

... testicular acid phosphatase Tissue acid phosphatase, or lysosomal acid phosphatase Alkaline phosphatase Henneberry MO, Engel G ... is acid-phosphatase negative , T-ALL (originating instead from T Lymphocytes) is acid-phosphatase positive . Acid phosphatase ... Minkin C (May 1982). "Bone acid phosphatase: tartrate-resistant acid phosphatase as a marker of osteoclast function". Calcified ... prostatic acid phosphatase ACP5, tartrate-resistant acid phosphatase ACP6 ACPT, ...
... (PAP), also prostatic specific acid phosphatase (PSAP), is an enzyme produced by the prostate. It ... "Prostatic acid phosphatase in serum of patients with prostatic cancer is a specific phosphotyrosine acid phosphatase". Clin. ... "Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase". ... "Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone". Nucleic Acids Res. 18 (16): ...
... (TRAP or TRAPase), also called acid phosphatase 5, tartrate resistant (ACP5), is a ... Minkin C (May 1982). "Bone acid phosphatase: tartrate-resistant acid phosphatase as a marker of osteoclast function". Calcified ... tartrate-resistant+acid+phosphatase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ... Klabunde T, Sträter N, Fröhlich R, Witzel H, Krebs B (June 1996). "Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on ...
PPAP2C phosphatidic acid phosphatase type 2C". Nanjundan M, Possmayer F (2003). "Pulmonary phosphatidic acid phosphatase and ... The protein encoded by this gene is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid ... Hooks SB, Ragan SP, Lynch KR (Jun 1998). "Identification of a novel human phosphatidic acid phosphatase type 2 isoform". FEBS ... This protein is similar to phosphatidic acid phosphatase type 2A (PPAP2A) and type 2B (PPAP2B). All three proteins contain 6 ...
Acid phosphatase Prostatic acid phosphatase Lysophosphatidic acid Lipid metabolism Tartrate-resistant acid phosphatase Alkaline ... Lysophosphatidic acid phosphatase type 6 is an acid phosphatase enzyme that is encoded in humans by the ACP6 gene. It acts as a ... Lysophosphatidic acid phosphatase has several roles. Although lysophosphatidic acid phosphatase is found ubiquitously ... Lysophosphatidic acid phosphatase is also responsible for the digestion of lysophosphatidic acids when the cell enters a state ...
... (PAPs) (EC 3.1.3.2) are metalloenzymes that hydrolyse phosphate esters and anhydrides under acidic ... PAPs are highly conserved within eukaryotic species, with >80% amino acid homology in mammalian PAPs, and >70% sequence ...
Tsuboi KK, Wiener G, Hudson PB (1957). "Acid phosphatase. VII. Yeast phosphomonoesterase; isolation procedure and stability ... Other names in common use include β-glycerophosphatase, β-glycerophosphate phosphatase, and 2-glycerophosphatase. Boyer, P.D., ... The enzyme glycerol-2-phosphatase (EC 3.1.3.19) catalyzes the reaction glycerol 2-phosphate + H2O ⇌ {\displaystyle \ ...
Richardson KE, Tolbert NE (May 1961). "Phosphoglycolic acid phosphatase". The Journal of Biological Chemistry. 236 (5): 1285-90 ... 2-phosphoglycolate phosphatase, P-glycolate phosphatase, and phosphoglycollate phosphatase, is an enzyme responsible for ... a feature consistent with other acid phosphatases. In addition, electrostatic surface analysis indicates a relatively acidic ... One of the is a knockout mutant that is devoid of 2PG phosphatase (PGLP). A high level of CO2 (1%), for example, is required ...
N-acylneuraminic acid 9-phosphate phosphatase, and N-acylneuraminic (sialic) acid 9-phosphatase. This enzyme participates in ... Jourdian GW, Swanson A, Watson D, Roseman S (1966). "N-Acetylneuraminic (sialic) acid 9-phosphatase". Methods Enzymol. 8: 205- ... The enzyme N-acylneuraminate-9-phosphatase (EC 3.1.3.29) catalyzes the reaction N-acylneuraminate 9-phosphate + H2O ⇌ {\ ... Other names in common use include acylneuraminate 9-phosphatase, ...
... phosphatidic acid phosphatase type 2A PPAP2B (LPP3) - phosphatidic acid phosphatase type 2B PPAP2C (LPP2) - phosphatidic acid ... phosphatidic acid phosphatase (PAP), 3-sn-phosphatidate phosphohydrolase, acid phosphatidyl phosphatase, phosphatidic acid ... phosphatidic acid phosphatase type 2 domain containing 1B PPAPDC2 - phosphatidic acid phosphatase type 2 domain containing 2 ... phosphatidic acid phosphatase type 2 domain containing 3 LPPR2 - lipid phosphate phosphatase-related protein type 2 LPIN1 - ...
Adrian GS, Keenan RW (1979). "A dolichyl phosphate-cleaving acid phosphatase from Tetrahymena pyriformis". Biochim. Biophys. ... dolichyl phosphate phosphatase, polyisoprenyl phosphate phosphatase, polyprenylphosphate phosphatase, and Dol-P phosphatase. ... Other names in common use include dolichol phosphate phosphatase, dolichol phosphatase, dolichol monophosphatase, dolichyl ... Rip JW, Rupar CA, Chaudhary N, Carroll KK (1981). "Localization of a dolichyl phosphate phosphatase in plasma membranes of rat ...
A member of a new class of Mg2+-dependent acid phosphatases". Eur. J. Biochem. 268 (19): 5176-88. doi:10.1046/j.0014-2956.2001. ... Other names in common use include (2R)-phosphosulfolactate phosphohydrolase, and ComB phosphatase. As of late 2007, only one ... Graham DE, Graupner M, Xu H, White RH (2001). "Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. ... The enzyme 2-phosphosulfolactate phosphatase (EC 3.1.3.71) catalyzes the reaction (2R)-2-phospho-3-sulfolactate + H2O ⇌ {\ ...
... and glycerophosphate phosphatase. Fallon HJ, Byrne WL (1965). "2-phosphoglyceric acid phosphatase: identification and ... The enzyme phosphoglycerate phosphatase (EC 3.1.3.20) catalyzes the reaction D-glycerate 2-phosphate + H2O ⇌ {\displaystyle \ ... Other names in common use include D-2-phosphoglycerate phosphatase, ...
LMW (low-molecular-weight) phosphatases, or acid phosphatases, act on tyrosine phosphorylated proteins, low-MW aryl phosphates ... and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase". J. Biol. Chem. 267 ( ... "Identification of the adipocyte acid phosphatase as a PAO-sensitive tyrosyl phosphatase". Protein Sci. 1 (6): 710-721. doi: ... The class II PTPs contain only one member, low-molecular-weight phosphotyrosine phosphatase (LMPTP). Cdc25 phosphatases (dTyr ...
SLC7A7 Lysosomal acid phosphatase deficiency; 200950; ACP2 Lysyl hydroxylase 3 deficiency; 612394; PLOD3 Machado-Joseph disease ... FREM1 Bile acid malabsorption, primary; 613291; SLC10A2 Bile acid synthesis defect, congenital, 2; 235555; AKR1D1 Bile acid ... SBDS Sialic acid storage disorder, infantile; 269920; SLC17A5 Sialidosis, type I; 256550; NEU1 Sialidosis, type II; 256550; ... DLAT Pyruvate dehydrogenase phosphatase deficiency; 608782; PDP1 Pyruvate kinase deficiency; 266200; PKLR Rabson-Mendenhall ...
Mycotoxins, Phosphatase inhibitors, Acid anhydrides). ... Rubratoxins are also known as protein phosphatase 2A (PP2A) ... "Rubratoxin A specifically and potently inhibits protein phosphatase 2A and suppresses cancer metastasis". Cancer Science. 101 ( ...
In the case of Provenge, this disease related protein is prostatic acid phosphatase and the signalling component is GM-CSF. ... October 2008). "Prostatic acid phosphatase is an ectonucleotidase and suppresses pain by generating adenosine". Neuron. 60 (1 ... Erbas H, Erten O, Irfanoglu ME (December 2007). "Prostatic acid phosphatase in breast cyst fluid". The Malaysian Journal of ... February 2009). "Glycomic Characterization of Prostate Specific Antigen and Prostatic Acid Phosphatase in Prostate Cancer and ...
A histochemical study with acid phosphatase. Gaton DD, Gaton E, Wolman M, Cellular Molecular Biology. 1987; 33 (5): 619-24. ... She also recognized the great importance of the acid-esterase enzyme and its activity in the vascular wall. In addition, she ...
These granules can contain acid phosphatase. Acid phosphatase is only found in larger secretory granules, 400 to 900 nm in ... This acid phosphatase is also present in the Golgi apparatus of the chief cell. However, the Golgi apparatus areas associated ... Chief cells in parathyroid adenomas also display acid phosphatase activity. It is a benign tumor of the gland that requires ... Shannon, W. Allen; Roth, Sanford I. (1974-12-01). "An Ultrastructural Study of Acid Phosphatase Activity in Normal, Adenomatous ...
Brightwell R, Tappel AL (1968). "Lysosomal acid pyrophosphatase and acid phosphatase". Arch. Biochem. Biophys. 124 (1): 333-43 ... This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing ...
A histochemical study with acid phosphatase. Gaton DD, Gaton E, Wolman M. Cellular Molecular Biology. 1987;33(5):619-624. The ...
Kong, HY; Byun, J (January 2013). "Emerging roles of human prostatic Acid phosphatase". Biomolecules & Therapeutics. 21 (1): 10 ... The secretions of the prostate include proteolytic enzymes, prostatic acid phosphatase, fibrinolysin, zinc, and prostate- ... and the Prostatic acid phosphatase. In the developing embryo, at the hind end lies an inpouching called the cloaca. This, over ... and of prostate-specific acid phosphatase, the Skene's gland is sometimes referred to as the "female prostate". Although ...
This permits characterization of osteoclasts by their staining for high expression of tartrate resistant acid phosphatase (TRAP ... These vacuoles include lysosomes filled with acid phosphatase. ... Energy-dependent acid transport was verified and the postulated ... Attachment to the bone matrix is facilitated by integrin receptors, such as αvβ3, via the specific amino acid motif Arg-Gly-Asp ... The osteoclast disassembles and digests the composite of hydrated protein and mineral at a molecular level by secreting acid ...
Richardson CC, Lehman IR, Kornberg A (January 1964). "A Deoxyribonucleic Acid Phosphatase-Exonuclease from Escherichia coli. II ... Linxweiler W, Hörz W (August 1982). "Sequence specificity of exonuclease III from E. coli". Nucleic Acids Research. 10 (16): ... phosphatase and AP-endonuclease activities. There are many different exonucleases and many are still to be discovered in ...
"Entrez Gene: PPAP2B phosphatidic acid phosphatase type 2B". "PLPP3 - Phospholipid phosphatase 3 - Homo sapiens (Human) - PLPP3 ... Lipid phosphate phosphohydrolase 3 (LPP3), also known as phospholipid phosphatase 3 (PLPP3) and phosphatidic acid phosphatase ... Ishikawa T, Kai M, Wada I, Kanoh H (April 2000). "Cell surface activities of the human type 2b phosphatidic acid phosphatase". ... Ishikawa T, Kai M, Wada I, Kanoh H (April 2000). "Cell surface activities of the human type 2b phosphatidic acid phosphatase". ...
Dullard dephosphorylates the mammalian phospatidic acid phosphatase, lipin. Dullard participates in a unique phosphatase ... which stands for CTD nuclear envelope phosphatase 1. This gene is relatively small and only contains 244 amino acids. Dullard ... which include phosphatase activity and protein serine/threonine phosphatase activity. This gene is relatively small and only ... It is a member of DXDX(T/V) phosphatase family and is a potential regulator of neural tube development in Xenopus. The gene ...
Richardson CC, Lehman IR, Kornberg A (January 1964). "A deoxyribonucleic acid phosphatase-exonuclease from Escherichia coli. II ... Richardson CC, Kornberg A (January 1964). "A deoxyribonucleic acid phosphatase-exonuclease from Escherichia coli. I. ... Purification of the enzyme and characterization of the phosphatase activity". The Journal of Biological Chemistry. 239: 242-50 ...
Lipid phosphate phosphohydrolase 1 also known as phosphatidic acid phosphatase 2a is an enzyme that in humans is encoded by the ... Ulrix W, Swinnen JV, Heyns W, Verhoeven G (1998). "Identification of the phosphatidic acid phosphatase type 2a isozyme as an ... "Entrez Gene: PPAP2A phosphatidic acid phosphatase type 2A". Kanoh H, Kai M, Wada I (1999). "Molecular characterization of the ... Hooks SB, Ragan SP, Lynch KR (1998). "Identification of a novel human phosphatidic acid phosphatase type 2 isoform". FEBS Lett ...
Acid phosphatase Liver function tests PDB: 1ALK​: Kim EE, Wyckoff HW (March 1991). "Reaction mechanism of alkaline phosphatase ... Alkaline phosphatase is a zinc-containing dimeric enzyme with the MW: 86,000 Da, each subunit containing 429 amino acids with ... Another known example of an alkaline phosphatase inhibitor is [(4-Nitrophenyl)methyl]phosphonic acid. In metal contaminated ... High alkaline phosphatase levels can occur if the bile ducts are obstructed. Also, the level of alkaline phosphatase increases ...
The acid phosphatase reaction can be used for diagnosis. Acanthocheilonema reconditum (syn. Dipetalonema reconditum) occurs in ...
... testicular acid phosphatase Tissue acid phosphatase, or lysosomal acid phosphatase Alkaline phosphatase Henneberry MO, Engel G ... is acid-phosphatase negative , T-ALL (originating instead from T Lymphocytes) is acid-phosphatase positive . Acid phosphatase ... Minkin C (May 1982). "Bone acid phosphatase: tartrate-resistant acid phosphatase as a marker of osteoclast function". Calcified ... prostatic acid phosphatase ACP5, tartrate-resistant acid phosphatase ACP6 ACPT, ...
The reference value for acid phosphatase is 2 ng/mL or less. . ... encoded search term (Acid Phosphatase) and Acid Phosphatase ... Acid phosphatases are enzymes that are capable of hydrolyzing phosphate esters in an acidic environment. Prostatic acid ... The reference value for acid phosphatase is 2 ng/mL or less. ... Acid Phosphatase Updated: Mar 19, 2014 * Author: Anas K Gremida ... phosphatase (PAP), which is produced in the prostate, was the first major serum marker for prostate cancer, and was used widely ...
The reference value for acid phosphatase is 2 ng/mL or less. . ... encoded search term (Acid Phosphatase) and Acid Phosphatase ... Acid phosphatases are enzymes that are capable of hydrolyzing phosphate esters in an acidic environment. Prostatic acid ... The reference value for acid phosphatase is 2 ng/mL or less. ... Acid Phosphatase Updated: Mar 19, 2014 * Author: Anas K Gremida ... phosphatase (PAP), which is produced in the prostate, was the first major serum marker for prostate cancer, and was used widely ...
Phosphatase (Acid) (E. coli) (E-ACPEC) Data Sheet Modified on: Tue, 20 Apr, 2021 at 10:21 AM ...
Test for estimation of Acid phosphatase activity in serum / plasma using α-Naphathylphosphate Kinetic method. ... Increased activities of total and prostate specific acid phosphatase are associated with prostate gland disorders (cancer). ... Test for estimation of Acid phosphatase activity in serum / plasma using α-Naphathylphosphate Kinetic method. ... It is a reagent set for quantitative determination of Acid phosphate activity based on kinetic method using naphthylphosphate. ...
Explore the 1 paper that mention a possible interaction between Alkaline Phosphatase and Conjugated Linoleic Acid. ... alkaline phosphatase (ALP), promoted the formation of mineralized nodules, and alleviated the oxidative damage induced by UVB. ... Conjugated linoleic acid prompts bone formation in ovariectomized osteoporotic rats and weakens osteoclast formation after ...
CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE ... ACID PHOSPHATASE: ABCDEF. SMTL:PDB. SMTL Chain Id:. PDB Chain ... CRYSTAL STRUCTURE OF ACID PHOSPHATASE FROM ESCHERICHIA BLATTAE Coordinates. PDB Format Method. X-RAY DIFFRACTION 1.90 Å. Oligo ... Ishikawa, K. et al., X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition- ...
Väänänen HK 1998 Studies on the protein tyrosine phosphatase activity of tartrate-resistant acid phosphatase. Arch Biochem ...
Extraction of acid phosphatase from mung bean sprouts and determination of its enzymatic properties Authors. * Lei Chen Weifang ... Acid Phosphatase, Enzymatic Properties, Optimum Condition, Mung Bean Sprouts, Enzyme activity Abstract. To investigate the ... 2024). Extraction of acid phosphatase from mung bean sprouts and determination of its enzymatic properties. Global Academic ... It was found that the activity of acid phosphatase in 1ml of mung bean sprout enzyme solution was 8.68, the optimal pH was 5.4 ...
Figure 1. Activity of β-glucosidase, chitinase and acid phosphatase in pM mm−2 h−1 determined on the flow cells sampled at ... Figure 1. Activity of β-glucosidase, chitinase and acid phosphatase in pM mm−2 h−1 determined on the flow cells sampled at ... Figure 4. Mean changes of enzyme activities of β-glucosidase, chitinase and acid phosphatase in non-hotspots given as % of ... Figure 4. Mean changes of enzyme activities of β-glucosidase, chitinase and acid phosphatase in non-hotspots given as % of ...
Acid phosphatase. -. -. Alkaline phosphatase. -. -. Pyrrolidonylarylamidase. -. -. API Strep code. 4640473 high degree (97%) ...
Measurements of alanine transaminase (ALT), aspartate transaminase (AST), and alkaline phosphatase.. Table 3. Indication for ...
ACP5: acid phosphatase 5, tartrate resistant. *ACSF3: acyl-CoA synthetase family member 3 ... ABHD5: abhydrolase domain containing 5, lysophosphatidic acid acyltransferase. *ABL1: ABL proto-oncogene 1, non-receptor ...
Anti-Prostate Specific Acid Phosphatase (PSAP). $268.00. - $885.00. Select options. * Anti-Adenovirus. $345.00. - $868.00. ... a high molecular weight glycoprotein that plays a major role in epithelial cyto-protection of gastrointestinal tract from acid ...
LPG, lipophosphoglycan; ACP, tartrate-resistant acid phosphatase; LCF, Leishmania chemotactic factor; LTB4, leukotriene B4; LXA ... Sialic acids in the parasite surface bind to Siglecs receptors on macrophages to dampen the immune response. Sialic acids ... like tartrate-resistant acid phosphatase (ACP) and Leishmania chemotactic factor (LCF) inhibit the respiratory burst, (Figure ... Remaley, A. T., Kuhns, D. B., Basford, R. E., Glew, R. H., and Kaplan, S. S. (1984). Leishmanial phosphatase blocks neutrophil ...
Rat TRACP-5b (Tartrate-Resistant Acid Phosphatase 5b) CLIA Kit , G-EC-02108 ... Rat FABP3 (Fatty Acid Binding Protein 3, Muscle and Heart) CLIA Kit , G-EC-02087 ...
Acid phosphatase Chemical pathology - Investigation of malabsorption - Quantitation of solid tissue enzymes Intestinal tissue ... 4-Hydroxy-3-methoxymethamphetamine (HMMA); 5-Hydroxyindoleacetic acid (5-HIAA); Homovanillic acid (HVA) ... Anti-gamma aminobutyric acid (GABA); Anti-glutamic acid decarboxylase 65 (GAD65); Anti-leucine rich glioma inactivated protein ... Nucleic acid analysis for specific variants Molecular genetics - Investigation of constitutional genetic variants - Diagnostic ...
Acid phosphatase: A new kind of particle 133 06:01 40. Experimenting with acid phosphatase 117 04:41 ...
Alkaline Phosphatase ................................................... 459 Uric Acid ... Uric Acid (xx.x) 465 007-125 - As given 6651 *** 777 - Unacceptable data 63 888 - Blank, but applicable 2 999 - Test not done ... Alkaline Phosphatase (xxx.x) 462 0048-5800 - As given 6364 *** 7777 - Unacceptable data 360 8888 - Blank, but applicable 2 9999 ...
... monounsaturated fatty acid; PTP1B, protein tyrosine phosphatase 1B; SCD, stearoyl-CoA desaturase; TG, triglyceride. ... Stearoyl-CoA desaturase-1 (SCD1) catalyzes the synthesis of monounsaturated fatty acids from saturated fatty acids. Mice with a ... However, the levels of the lipogenic enzymes ACC and fatty acid synthase were not increased and tended to be lowered by Scd1- ... The overfed SCD1 ASO group displayed increased Akt phosphorylation and dramatic suppression of glucose-6-phosphatase and ...
... acid phosphatase activity; NAG, β-1, 4-N-Acetylglucosaminida activity; LAP, L-leucine aminopeptidase; POX, Polyphenol oxidase ... 1996), and the P concentration by molybdovanadate method (Lu, 1999). The Lignin concentrations were determined using the acid ...
... in situ hybridisation and tartrate-resistant acid phosphatase (TRAP) staining. TRAP histochemistry and TRAP-positive regions ... ethylenediaminetetraacetic acid (EDTA) with one change of solution at day 7. Serial, 6 μm thick paraffin sections were prepared ... Statin-induced bone formation is associated with increased osteoblast differentiation as measured by alkaline phosphatase, bone ... buffer supplemented with protease and phosphatase inhibitors using tissue homogeniser (Fisher Scentific). Homogenates were ...
N-acetylneuraminic acid phosphatase. protein-coding. NUDT17. nudix hydrolase 17. protein-coding. ...
Protein and total lipid content, lecithin, triglycerides, cholesterol, uric acid, alkaline and acid phosphatases and cathepsin ... Open the PDF for Biochemical Membrane Constituents and Activities of Alkaline and Acid Phosphatase and Cathepsin in Cortical ... View article titled, Biochemical Membrane Constituents and Activities of Alkaline and Acid Phosphatase and Cathepsin in ... Biochemical Membrane Constituents and Activities of Alkaline and Acid Phosphatase and Cathepsin in Cortical and Subcortical ...
Lysophosphatidic acid phosphatase type 6 Show on y-axis - References (HTP + LTP). References (LTP). References (HTP). ...
Voltage-dependent motion of the catalytic region of voltage-sensing phosphatase monitored by a fluorescent amino acid. Sakata S ... Phosphatase activity of the voltage-sensing phosphatase, VSP, shows graded dependence on the extent of activation of the ... 3 Phosphatase activity toward phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2] by voltage-sensing phosphatase (VSP). 2012, ... Voltage-sensing phosphatase: actions and potentials. 2009, Pubmed Okamura, Voltage-sensing phosphatase: its molecular ...
Serotonin is derived from the amino acid tryptophan, which also serves as a precursor to niacin and several proteins. Increased ... Carcinoids arising in the stomach are usually associated with low gastric acid production, a condition termed hypochlorhydria ... Scintigraphy with indium-111 diethylenetriamine pentaacetic acid (DTPA) octreotide (In-111 DTPA Octr), or OctreoScan, localizes ... in the platelets while the excesses are inactivated in the liver and lung and transformed into 5-hydroxyindoleacetic acid (5- ...
  • Tartrate-resistant acid phosphatase may be used as a biochemical marker of osteoclast function during the process of bone resorption. (wikipedia.org)
  • The following genes encode the polypeptide components for various acid phosphatase isoenzymes:[citation needed] ACP1 ACP2 ACPP (ACP3), prostatic acid phosphatase ACP5, tartrate-resistant acid phosphatase ACP6 ACPT, testicular acid phosphatase Tissue acid phosphatase, or lysosomal acid phosphatase Alkaline phosphatase Henneberry MO, Engel G, Grayhack JT (October 1979). (wikipedia.org)
  • Halleen JM, Kaija H, Stepan JJ, Vihko P, Väänänen HK 1998 Studies on the protein tyrosine phosphatase activity of tartrate-resistant acid phosphatase . (oncobone.com)
  • The purpose of this study was to investigate the activities of the total acid phosphatase (TAP), tartrate-resistant acid phosphatase (TRAP), low molecular weight protein tyrosine phosphatase (LMW-PTP) and alkaline phosphatase (ALP) enzymes, as well as the possible correlation in the serum and in unstimulated whole saliva of children. (bvsalud.org)
  • Osteoclasts were enumerated after tartrate-resistant acid phosphatase staining. (bvsalud.org)
  • Prostatic acid phosphatase (PAP), which is produced in the prostate, was the first major serum marker for prostate cancer, and was used widely for screening, staging, and post-treatment monitoring. (medscape.com)
  • Increased activities of total and prostate specific acid phosphatase are associated with prostate gland disorders (cancer). (anamollabs.com)
  • 2023).Molecular cloning and tissue distribution of glucokinase and glucose-6-phosphatase catalytic subunit paralogs in largemouth bass Micropterus salmoides: Regulation by dietary starch levels and a glucose load. (gafj.org)
  • Downregulation of Scd1 also led to increased Akt phosphorylation and marked decreases in the expression of glucose-6-phosphatase (Glc-6-Pase) and phosphoenolpyruvate carboxykinase (PEPCK). (jci.org)
  • Acid phosphatase (EC 3.1.3.2, systematic name phosphate-monoester phosphohydrolase (acid optimum)) is an enzyme that frees attached phosphoryl groups from other molecules during digestion. (wikipedia.org)
  • Different forms of acid phosphatase are found in different organs, and their serum levels are used to evaluate the success of the surgical treatment of prostate cancer. (wikipedia.org)
  • Test for estimation of Acid phosphatase activity in serum / plasma using α-Naphathylphosphate Kinetic method. (anamollabs.com)
  • Acid phosphatase catalyzes the following reaction at an optimal acidic pH (below 7): a phosphate monoester + H2O = an alcohol + phosphate Phosphatase enzymes are also used by soil microorganisms to access organically bound phosphate nutrients. (wikipedia.org)
  • It is a reagent set for quantitative determination of Acid phosphate activity based on kinetic method using naphthylphosphate. (anamollabs.com)
  • Acid phosphatases are enzymes that are capable of hydrolyzing phosphate esters in an acidic environment. (medscape.com)
  • Allosteric substrate switching in a voltage-sensing lipid phosphatase. (xenbase.org)
  • Crystal structure of the cytoplasmic phosphatase and tensin homolog (PTEN)-like region of Ciona intestinalis voltage-sensing phosphatase provides insight into substrate specificity and redox regulation of the phosphoinositide phosphatase activity. (xenbase.org)
  • Stearoyl-CoA desaturase-1 (SCD1) catalyzes the synthesis of monounsaturated fatty acids from saturated fatty acids. (jci.org)
  • Stearoyl-CoA desaturase (SCD) is the central lipogenic enzyme catalyzing in vivo reactions in the synthesis of monounsaturated fatty acids (MUFAs), particularly oleate (C18:1n-9) and palmitoleate (C16:1n-7), which are the major MUFAs of membrane phospholipids, triglycerides (TGs), wax esters, and cholesteryl esters. (jci.org)
  • Voltage-dependent motion of the catalytic region of voltage-sensing phosphatase monitored by a fluorescent amino acid. (xenbase.org)
  • The cytoplasmic region of voltage-sensing phosphatase (VSP) derives the voltage dependence of its catalytic activity from coupling to a voltage sensor homologous to that of voltage-gated ion channels. (xenbase.org)
  • To assess the conformational changes in the cytoplasmic region upon activation of the voltage sensor, we genetically incorporated a fluorescent unnatural amino acid, 3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid (Anap), into the catalytic region of Ciona intestinalis VSP (Ci-VSP). (xenbase.org)
  • 2023).Predicting the allergenic risk of Phosphite-NADsup+/sup-Oxidoreductase and purple acid phosphatase 17 proteins in genetically modified canola using bioinformatic approaches. (gafj.org)
  • Interactions of phosphatase and tensin homologue (PTEN) proteins with phosphatidylinositol phosphates: insights from molecular dynamics simulations of PTEN and voltage sensitive phosphatase. (xenbase.org)
  • Some plant roots, especially cluster roots, exude carboxylates that perform acid phosphatase activity, helping to mobilise phosphorus in nutrient-deficient soils. (wikipedia.org)
  • It was found that the activity of acid phosphatase in 1ml of mung bean sprout enzyme solution was 8.68, the optimal pH was 5.4, and the temperature at which the activity was highest was 50 degrees Celsius. (gafj.org)
  • 3' Phosphatase activity toward phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2] by voltage-sensing phosphatase (VSP). (xenbase.org)
  • Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. (xenbase.org)
  • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. (xenbase.org)
  • Semen acid- phosphatase activity was increased in the 45mg/kg group. (cdc.gov)
  • MUC 6 also designated Mucin 6 and gastric mucin, is a high molecular weight glycoprotein that plays a major role in epithelial cyto-protection of gastrointestinal tract from acid, proteases, pathogenic microorganisms, and mechanical trauma. (biogenex.com)
  • Phosphoinositide 5- and 3-phosphatase activities of a voltage-sensing phosphatase in living cells show identical voltage dependence. (xenbase.org)
  • Conjugated linoleic acid prompts bone formation in ovariectomized osteoporotic rats and weakens osteoclast formation after treatment with ultraviolet B. (supp.ai)
  • To investigate the enzymatic properties of acid phosphatase from mung bean sprouts and explore the optimal reaction conditions for this enzyme. (gafj.org)
  • A glutamate switch controls voltage-sensitive phosphatase function. (xenbase.org)
  • The reference value for acid phosphatase is 2 ng/mL or less. (medscape.com)
  • This study extracted phosphatase from fresh mung bean sprouts and determined its enzymatic properties. (gafj.org)
  • Voltage-sensing phosphatase modulation by a C2 domain. (xenbase.org)
  • Most of these tumors produce 5-hydroxytryptamine, which, in physiologic conditions, is taken up and stored in the platelets while the excesses are inactivated in the liver and lung and transformed into 5-hydroxyindoleacetic acid (5-HIAA). (medscape.com)
  • 1985. The effects of dietary L-ascorbic acid on the absorption and utilization of Na75Se03 of silver-treated rats. (cdc.gov)
  • Results: The tissue nonspecific alkaline phosphatase activity was similar in hypertrophied tonsils in the recurrent infection group and in the obstructive sleep apnoea group (3.437 ± 1.226 and 3.978 ± 0.762 U/mg of protein, respectively). (northwestern.edu)
  • In patients with hypertrophied tonsils similar tissue nonspecific alkaline phosphatase activity suggests preserved B cell tonsil immune activity, regardless of the pathology. (northwestern.edu)
  • Patients with atrophied tonsils had significantly lower alkaline phosphatase activity, indicating relative tonsil B cell immune deficiency. (northwestern.edu)
  • Prostatic acid phosphatase (PAP), which is produced in the prostate, was the first major serum marker for prostate cancer. (medscape.com)
  • They are also exposed to a protein called prostatic acid phosphatase (PAP), which should produce an immune response against prostate cancer cells. (oralcancerfoundation.org)
  • The lipin phosphatidic acid phosphatase (PAP) enzymes are required for triacylglycerol (TAG) synthesis from glycerol 3-phosphate in most mammalian tissues. (nih.gov)
  • Protein tyrosine phosphatase, non-receptor type 2 (PTPN2), is one of the most abundant mammalian tyrosine phosphatase. (sigmaaldrich.com)
  • By virtue of protein tyrosine phosphatase activity, PTPN2 is known to be a signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation involved in cell communication and signal transduction. (sigmaaldrich.com)
  • It is also very likely that protein kinases and protein phosphatases are involved in signal transduction in plants. (scialert.net)
  • 1985. The effects of dietary L-ascorbic acid on the absorption and utilization of Na75Se03 of silver-treated rats. (cdc.gov)
  • Lysosomes are membrane-bound organelles containing digestive enzymes that can break down proteins, lipids, carbohydrates and nucleic acids. (cellimagelibrary.org)
  • Acid phosphatases are enzymes that are capable of hydrolyzing phosphate esters in an acidic environment. (medscape.com)
  • To see if acidosomes contain hydrolases (digestive enzymes) we incubated cells in Gomori's medium which in the presence of acid phosphatase and lead will form an electron-opaque reaction product. (cellimagelibrary.org)
  • The protein-tyrosine/dual-specificity phosphatases and rhodanese domains constitute a sprawling superfamily of Rossmannoid domains that use a conserved active site with a cysteine to catalyze a range of phosphate-transfer, thiotransfer, selenotransfer and redox activities. (nih.gov)
  • The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. (sigmaaldrich.com)
  • The effect of cation size on the enzymatic reaction of acid phosphatase with PNPP was further examined using the Hanes transformation of the Michaelis-Menten equation of enzyme kinetics. (bridgewater.edu)
  • Metastasis of prostate cancer beyond the capsule, particularly to the bone, causes a rise in acid phosphatase level, with the level increasing in correspondence to the extent of the disease. (medscape.com)
  • One region is centrally located between amino acids 368 and 605 and within or adjacent to a DNA binding repressor domain. (nih.gov)
  • Furthermore, here we have successfully reconstituted ABA-induced activation of SLAC1 channels in oocytes using the ABA receptor pyrabactin resistant 1 (PYR1) and PP2C phosphatases with two alternate signaling cores including either CPK6 or OST1. (elsevierpure.com)
  • Acid phosphatases and other tumour markers in the management of prostate cancer. (spcg.se)
  • The levels of lysophosphatidic acid (LPA) are consistently elevated in the ascites of ovarian cancer patients, suggesting that ovarian cancer cells are exposed to an LPA replete environment. (nih.gov)
  • All adherent cell cultures were recovered using Gibco 0.25% trypsin-ethylenediaminetetraacetic acid (Life Technologies GmbH) before seeding and waiting until cells reached confluency before commencement of treatments. (medscape.com)
  • Acid phosphatase activities exist in GERL region and in side-cisternae which are mature and also in vacuoles which are condensing.GERL was examined with cytochemical markers, two enzyme markers (TPPase) and (ACPase) and osmium impregnation in the ameloblasts. (careers360.com)
  • Contrary to this, no significant differences were noticed for tonsil and adenoid acid phosphatase activities among the groups. (northwestern.edu)
  • Can we put the towel under ultraviolet light and if anything shows up run an Acid Phosphatase Test on the stains. (capitolhillblue.com)
  • The terms "Acid phosphatase deficiency" returned 2 free, full-text research articles on human participants. (diseaseinfosearch.org)
  • Following organizations serve the condition "Acid phosphatase deficiency" for support, advocacy or research. (diseaseinfosearch.org)
  • Option 1 is incorrect because the cytochemical marker acid phosphatase does not act on the cis-region of the Golgi complex. (careers360.com)