A calbindin protein found in many mammalian tissues, including the UTERUS, PLACENTA, BONE, PITUITARY GLAND, and KIDNEYS. In intestinal ENTEROCYTES it mediates intracellular calcium transport from apical to basolateral membranes via calcium binding at two EF-HAND MOTIFS. Expression is regulated in some tissues by VITAMIN D.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
Calcium-binding proteins that are found in DISTAL KIDNEY TUBULES, INTESTINES, BRAIN, and other tissues where they bind, buffer and transport cytoplasmic calcium. Calbindins possess a variable number of EF-HAND MOTIFS which contain calcium-binding sites. Some isoforms are regulated by VITAMIN D.
A calcium-binding protein that mediates calcium HOMEOSTASIS in KIDNEYS, BRAIN, and other tissues. It is found in well-defined populations of NEURONS and is involved in CALCIUM SIGNALING and NEURONAL PLASTICITY. It is regulated in some tissues by VITAMIN D.
A calbindin protein that is differentially expressed in distinct populations of NEURONS throughout the vertebrate and invertebrate NERVOUS SYSTEM, and modulates intrinsic neuronal excitability and influences LONG-TERM POTENTIATION. It is also found in LUNG, TESTIS, OVARY, KIDNEY, and BREAST, and is expressed in many tumor types found in these tissues. It is often used as an immunohistochemical marker for MESOTHELIOMA.
Low molecular weight, calcium binding muscle proteins. Their physiological function is possibly related to the contractile process.
A family of highly acidic calcium-binding proteins found in large concentration in the brain and believed to be glial in origin. They are also found in other organs in the body. They have in common the EF-hand motif (EF HAND MOTIFS) found on a number of calcium binding proteins. The name of this family derives from the property of being soluble in a 100% saturated ammonium sulfate solution.
Calcium-binding motifs composed of two helices (E and F) joined by a loop. Calcium is bound by the loop region. These motifs are found in many proteins that are regulated by calcium.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.
A neuronal calcium-sensor protein that is found in ROD PHOTORECEPTORS and CONE PHOTORECEPTORS. It interacts with G-PROTEIN-COUPLED RECEPTOR KINASE 1 in a Ca2+ dependent manner and plays an important role in PHOTOTRANSDUCTION.
A 13.2-kDa member of the S-100 family of calcium-binding proteins that can form homo- or heterocomplexes with CALGRANULIN A and a variety of other proteins. The calgranulin A/B heterodimer is known as LEUKOCYTE L1 ANTIGEN COMPLEX. Calgranulin B is expressed at high concentrations in GRANULOCYTES during early monocyte differentiation, and serum calgranulin B levels are elevated in many inflammatory disorders such as CYSTIC FIBROSIS.
Acidic protein found in SARCOPLASMIC RETICULUM that binds calcium to the extent of 700-900 nmoles/mg. It plays the role of sequestering calcium transported to the interior of the intracellular vesicle.
A 10.8-kDa member of the S-100 family of calcium-binding proteins that can form homo- or heterocomplexes with CALGRANULIN B and a variety of other proteins. The calgranulin A/B heterodimer is known as LEUKOCYTE L1 ANTIGEN COMPLEX. Calgranulin A is found in many cell types including GRANULOCYTES; KERATINOCYTES; and myelomonocytes, and has been shown to act as a chemotactic substance for NEUTROPHILS. Because it is present in acute inflammation but absent in chronic inflammation, it is a useful biological marker for a number of pathological conditions.
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.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A genus of European newts in the Salamandridae family. The two species of this genus are Salamandra salamandra (European "fire" salamander) and Salamandra atra (European alpine salamander).
A nonfluorescent reagent for the detection of primary amines, peptides and proteins. The reaction products are highly fluorescent.
Signal transduction mechanisms whereby calcium mobilization (from outside the cell or from intracellular storage pools) to the cytoplasm is triggered by external stimuli. Calcium signals are often seen to propagate as waves, oscillations, spikes, sparks, or puffs. The calcium acts as an intracellular messenger by activating calcium-responsive proteins.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A nitrocellulose solution in ether and alcohol. Collodion has a wide range of uses in industry including applications in the manufacture of photographic film, in fibers, in lacquers, and in engraving and lithography. In medicine it is used as a drug solvent and a wound sealant.
Unstable isotopes of calcium that decay or disintegrate emitting radiation. Ca atoms with atomic weights 39, 41, 45, 47, 49, and 50 are radioactive calcium isotopes.
A species of parasitic protozoa causing ENTAMOEBIASIS and amebic dysentery (DYSENTERY, AMEBIC). Characteristics include a single nucleus containing a small central karyosome and peripheral chromatin that is finely and regularly beaded.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Voltage-dependent cell membrane glycoproteins selectively permeable to calcium ions. They are categorized as L-, T-, N-, P-, Q-, and R-types based on the activation and inactivation kinetics, ion specificity, and sensitivity to drugs and toxins. The L- and T-types are present throughout the cardiovascular and central nervous systems and the N-, P-, Q-, & R-types are located in neuronal tissue.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A chelating agent relatively more specific for calcium and less toxic than EDETIC ACID.
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.
A network of tubules and sacs in the cytoplasm of SKELETAL MUSCLE FIBERS that assist with muscle contraction and relaxation by releasing and storing calcium ions.
Calcium compounds used as food supplements or in food to supply the body with calcium. Dietary calcium is needed during growth for bone development and for maintenance of skeletal integrity later in life to prevent osteoporosis.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
'Nerve tissue proteins' are specialized proteins found within the nervous system's biological tissue, including neurofilaments, neuronal cytoskeletal proteins, and neural cell adhesion molecules, which facilitate structural support, intracellular communication, and synaptic connectivity essential for proper neurological function.
Contractile tissue that produces movement in animals.
Measurement of the intensity and quality of fluorescence.
Proteins that bind to the 3' polyadenylated region of MRNA. When complexed with RNA the proteins serve an array of functions such as stabilizing the 3' end of RNA, promoting poly(A) synthesis and stimulating mRNA translation.
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.
Stable calcium atoms that have the same atomic number as the element calcium, but differ in atomic weight. Ca-42-44, 46, and 48 are stable calcium isotopes.
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.
One of the three polypeptide chains that make up the TROPONIN complex of skeletal muscle. It is a calcium-binding protein.
The sum of the weight of all the atoms in a molecule.
Transport proteins that carry specific substances in the blood or across cell membranes.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The rate dynamics in chemical or physical systems.
The physiologically active form of vitamin D. It is formed primarily in the kidney by enzymatic hydroxylation of 25-hydroxycholecalciferol (CALCIFEDIOL). Its production is stimulated by low blood calcium levels and parathyroid hormone. Calcitriol increases intestinal absorption of calcium and phosphorus, and in concert with parathyroid hormone increases bone resorption.
A calcium-binding protein that is 92 AA long, contains 2 EF-hand domains, and is concentrated mainly in GLIAL CELLS. Elevation of S100B levels in brain tissue correlates with a role in neurological disorders.
Proteins found in any species of bacterium.
Established cell cultures that have the potential to propagate indefinitely.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
A salt used to replenish calcium levels, as an acid-producing diuretic, and as an antidote for magnesium poisoning.
A protein present in the cell wall of most Staphylococcus aureus strains. The protein selectively binds to the Fc region of human normal and myeloma-derived IMMUNOGLOBULIN G. It elicits antibody activity and may cause hypersensitivity reactions due to histamine release; has also been used as cell surface antigen marker and in the clinical assessment of B lymphocyte function.
Carbonic acid calcium salt (CaCO3). An odorless, tasteless powder or crystal that occurs in nature. It is used therapeutically as a phosphate buffer in hemodialysis patients and as a calcium supplement.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
A ubiquitously expressed family of heterotrimeric GTP-binding protein alpha subunits that signal through interactions with a variety of second messengers as GTPASE-ACTIVATING PROTEINS; GUANINE NUCLEOTIDE EXCHANGE FACTORS; and HEAT SHOCK PROTEINS. The G12-G13 part of the name is also spelled G12/G13.
Proteins prepared by recombinant DNA technology.
Terbium. An element of the rare earth family of metals. It has the atomic symbol Tb, atomic number 65, and atomic weight 158.92.
A genus of gram-positive, coccoid bacteria whose organisms occur in pairs or chains. No endospores are produced. Many species exist as commensals or parasites on man or animals with some being highly pathogenic. A few species are saprophytes and occur in the natural environment.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
One of the minor protein components of skeletal muscle. Its function is to serve as the calcium-binding component in the troponin-tropomyosin B-actin-myosin complex by conferring calcium sensitivity to the cross-linked actin and myosin filaments.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
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.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Calcium salts of phosphoric acid. These compounds are frequently used as calcium supplements.
A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-
NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.
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)
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
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 family of heterotrimeric GTP-binding protein alpha subunits that were originally identified by their ability to inhibit ADENYLYL CYCLASES. Members of this family can couple to beta and gamma G-protein subunits that activate POTASSIUM CHANNELS. The Gi-Go part of the name is also spelled Gi/Go.
A poly(A) binding protein that has a variety of functions such as mRNA stabilization and protection of RNA from nuclease activity. Although poly(A) binding protein I is considered a major cytoplasmic RNA-binding protein it is also found in the CELL NUCLEUS and may be involved in transport of mRNP particles.
The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B.
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 rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)
Long-lasting voltage-gated CALCIUM CHANNELS found in both excitable and nonexcitable tissue. They are responsible for normal myocardial and vascular smooth muscle contractility. Five subunits (alpha-1, alpha-2, beta, gamma, and delta) make up the L-type channel. The alpha-1 subunit is the binding site for calcium-based antagonists. Dihydropyridine-based calcium antagonists are used as markers for these binding sites.
A neuronal calcium-sensor protein that was initially found in the NEURONS of the HIPPOCAMPUS. It interacts with NEURONAL APOPTOSIS-INHIBITORY PROTEIN.
A family of soluble proteins that bind insulin-like growth factors and modulate their biological actions at the cellular level. (Int J Gynaecol Obstet 1992;39(1):3-9)
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
The calcium salt of oxalic acid, occurring in the urine as crystals and in certain calculi.
'Zoo animals' are various species of captive wild animals, housed and displayed in a facility for the purpose of public education, conservation, research, and recreation.
Chemicals that bind to and remove ions from solutions. Many chelating agents function through the formation of COORDINATION COMPLEXES with METALS.
Ytterbium. An element of the rare earth family of metals. It has the atomic symbol Yb, atomic number 70, and atomic weight 173. Ytterbium has been used in lasers and as a portable x-ray source.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Lanthanum. The prototypical element in the rare earth family of metals. It has the atomic symbol La, atomic number 57, and atomic weight 138.91. Lanthanide ion is used in experimental biology as a calcium antagonist; lanthanum oxide improves the optical properties of glass.
The calcium salt of gluconic acid. The compound has a variety of uses, including its use as a calcium replenisher in hypocalcemic states.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.
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.

Energy-based de novo protein folding by conformational space annealing and an off-lattice united-residue force field: application to the 10-55 fragment of staphylococcal protein A and to apo calbindin D9K. (1/989)

The conformational space annealing (CSA) method for global optimization has been applied to the 10-55 fragment of the B-domain of staphylococcal protein A (protein A) and to a 75-residue protein, apo calbindin D9K (PDB ID code), by using the UNRES off-lattice united-residue force field. Although the potential was not calibrated with these two proteins, the native-like structures were found among the low-energy conformations, without the use of threading or secondary-structure predictions. This is because the CSA method can find many distinct families of low-energy conformations. Starting from random conformations, the CSA method found that there are two families of low-energy conformations for each of the two proteins, the native-like fold and its mirror image. The CSA method converged to the same low-energy folds in all cases studied, as opposed to other optimization methods. It appears that the CSA method with the UNRES force field, which is based on the thermodynamic hypothesis, can be used in prediction of protein structures in real time.  (+info)

Expression of calcium binding protein D-9k messenger RNA in the mouse uterine endometrium during implantation. (2/989)

To investigate the molecular mechanisms of implantation, we constructed a cDNA library of mouse uteri enriched with pregnancy-induced genes by subtractive hybridization and polymerase chain reaction (PCR). One of the isolated clones was the cDNA for the calcium binding protein D-9k (Cabp9k), which is considered to regulate intracytoplasmic concentration and transport of free calcium ions. Northern blot and in-situ hybridization analyses demonstrated that the Cabp9k mRNA was expressed in the endometrial epithelia, both luminal and glandular, in the uterus at the time of implantation. On pregnancy day 5 it was detected in the luminal, but not in the glandular, epithelia. In the oophorectomized adult mice, progesterone enhanced Cabp9k mRNA expression in the uterus, whereas oestrogen did not. Consistent with this, a nucleotide change was identified in the first intron of mouse Cabp9k gene corresponding to the oestrogen responsive element in the rat Cabp9k gene. Transfer of embryos into the uterine cavity of pseudopregnant mice reduced the expression of Cabp9k mRNA in the glandular epithelium, suggesting that Cabp9k mRNA expression is also regulated by embryonal signal(s). These findings demonstrated that Cabp9k mRNA is expressed in the endometrial epithelia during the implantation period under the control of progesterone and the presence of embryo, and suggest that CaBP9k plays a role in implantation by regulating the local calcium concentrations.  (+info)

Distribution of cholinergic contacts on Renshaw cells in the rat spinal cord: a light microscopic study. (3/989)

1. Cholinergic terminals in the rat spinal cord were revealed by immunohistochemical detection of the vesicular acetycholine transporter (VAChT). In order to determine the relationships of these terminals to Renshaw cells, we used dual immunolabelling with antibodies against gephyrin or calbindin D28k to provide immunohistochemical identification of Renshaw cells in lamina VII of the ventral horn. 2. A total of 50 Renshaw cells were analysed quantitatively using a computer-aided reconstruction system to provide accurate localization of contact sites and determination of somatic and dendritic surface area. Dendrites could be traced for up to 413 microm from the soma in calbindin D28k-identified Renshaw cells and up to 184 microm in gephyrin-identified cells. 3. A total of 3330 cholinergic terminals were observed on 50 Renshaw cells, with a range of 21-138 terminal appositions per cell (mean 66.6 +/- 25.56 contacts per cell). The vast majority (83.5 %) of the terminals were apposed to dendrites rather than the soma. The overall density of cholinergic contacts increased from a little above 1 per 100 microm2 on the soma and initial 25 microm of proximal dendrites to 4-5 per 100 microm2 on the surface of dendritic segments located 50-250 microm from the soma. Single presynaptic fibres frequently formed multiple contacts with the soma and/or dendrites of individual Renshaw cells. 4. VAChT-immunoreactive terminals apposed to Renshaw cells varied in size from 0.6 to 6.9 microm in diameter (mean 2.26 +/- 0.94; n = 986) and were on average smaller than the cholinergic C-terminals apposed to motoneurones, but larger than VAChT-immunoreactive terminals contacting other ventral horn interneurones. 5. The high density and relatively large size of many cholinergic terminals on Renshaw cells presumably correlates with the strong synaptic connection between motoneurones and Renshaw cells. The fact that the majority of contacts are distributed over the dendrites makes the motoneurone axon collateral input susceptible to inhibition by the prominent glycinergic inhibitory synapses located on the soma and proximal dendrites. The relative positions and structural features of the excitatory cholinergic and inhibitory glycinergic synapses may explain why Renshaw cells, although capable of firing at very high frequency following motor axon stimulation, appear to fire at relatively low rates during locomotor activity.  (+info)

Characterization of nodular neuronal heterotopia in children. (4/989)

Neuronal heterotopia are seen in various pathologies and are associated with intractable epilepsy. We examined brain tissue from four children with subcortical or periventricular nodular heterotopia of different aetiologies: one with severe epilepsy following focal brain trauma at 17 weeks gestation, one with hemimegalencephaly and intractable epilepsy, one with focal cortical dysplasia and intractable epilepsy, and one dysmorphic term infant with associated hydrocephalus and polymicrogyria. The connectivity of nodules was investigated using histological and carbocyanine dye (DiI) tracing techniques. DiI crystal placement adjacent to heterotopic nodules revealed numerous DiI-labelled fibres within a 2-3 mm radius of the crystals. Although we observed labelled fibres closely surrounding nodules, the majority did not penetrate them. Placement of DiI crystals within nodules also identified a limited number of projections out of the nodules and in one case there was evidence for connectivity between adjacent nodules. The cellular and neurochemical composition of nodules was also examined using immunohistochemistry for calretinin and neuropeptide Y (NPY), which are normally expressed in GABAergic cortical interneurons. Within heterotopic nodules from all cases, numerous calretinin-positive neurons were identified, along with a few cell bodies and many processes positive for NPY. Calretinin-positive neurons within nodules were less morphologically complex than those in the cortex, which may reflect incomplete differentiation into an inhibitory neuronal phenotype. There were also abnormal clusters of calretinin-positive cells in the overlying cortical plate, indicating that the migratory defect which produces heterotopic nodules also affects development of the cortex itself. Thus, heterotopic nodules consisting of multiple neuronal cell types are associated with malformation in the overlying cortical plate, and have limited connectivity with other brain regions. This abnormal development of connectivity may affect neuronal maturation and consequently the balance of excitation and inhibition in neuronal circuits, leading to their epileptogenic potential.  (+info)

Measurements of [Ca2+] using fura-2 in glioma C6 cells expressing calretinin with GFP as a marker of transfection: no Ca2+-buffering provided by calretinin. (5/989)

Glioma C6 cells were transfected with a plasmid containing the calretinin (CR) and green fluorescent protein (GFP) coding regions to analyze the effect of CR's presence on [Ca2+]i. Positive transfectants were identified by the detection of GFP and [Ca2+]i was measured using fura-2 as a probe. We found that neither the basic [Ca2+]i nor activated [Ca2+]i achieved by exposure to ionomycin, ADP or thapsigargin were affected by CR's presence in transfected cells, despite the ability of CR to bind Ca2+ as part of fusion protein. The level of expressed CR was estimated as at least 1 microM. The presented results suggest that CR's function is unlikely to be an intracellular Ca2+-buffer and support the hypothesis that CR might be involved in a specific Ca2+-dependent process. The results of this work also show that the S65T mutant of GFP is compatible with fura-2 measurements of intracellular [Ca2+]. We have demonstrated that the presence of GFP, as a transfection marker of glioma C6 cells, does not disturb fura-2 fluorescence, the basal or activated [Ca2+]i in these cells.  (+info)

Molecular identification of the apical Ca2+ channel in 1, 25-dihydroxyvitamin D3-responsive epithelia. (6/989)

In mammals, the extracellular calcium concentration is maintained within a narrow range despite large variations in daily dietary input and body demand. The small intestine and kidney constitute the influx pathways into the extracellular Ca2+ pool and, therefore, play a primary role in Ca2+ homeostasis. We identified an apical Ca2+ influx channel, which is expressed in proximal small intestine, the distal part of the nephron and placenta. This novel epithelial Ca2+ channel (ECaC) of 730 amino acids contains six putative membrane-spanning domains with an additional hydrophobic stretch predicted to be the pore region. ECaC resembles the recently cloned capsaicin receptor and the transient receptor potential-related ion channels with respect to its predicted topology but shares less than 30% sequence homology with these channels. In kidney, ECaC is abundantly present in the apical membrane of Ca2+ transporting cells and colocalizes with 1,25-dihydroxyvitamin D3-dependent calbindin-D28K. ECaC expression in Xenopus oocytes confers Ca2+ influx with properties identical to those observed in distal renal cells. Thus, ECaC has the expected properties for being the gatekeeper of 1,25-dihydroxyvitamin D3-dependent active transepithelial Ca2+ transport.  (+info)

Immunohistological studies of metabotropic glutamate receptor subtype 6-deficient mice show no abnormality of retinal cell organization and ganglion cell maturation. (7/989)

Immature retinal ganglion cells (RGCs) initially show a multistratified dendritic pattern, and, during the postnatal period, these dendrites gradually monostratify into ON and OFF sublaminae. The selective agonist of group III metabotropic glutamate receptors (mGluR), L-2-amino-4-phosphonobutyrate (L-AP-4), hyperpolarizes ON bipolar cells and reduces glutamate release. On the basis of L-AP-4-evoked inhibitory effects on ON-OFF segregation of developing RGCs, it has been hypothesized that glutamate-mediated synaptic activity is crucial for formation of the ON-OFF network. Gene-targeted ablation of mGluR6 specifically expressed in ON bipolar cells blocks normal ON responses but has been predicted to enhance glutamate release from ON bipolar cells. The mGluR6 knock-out mouse therefore provides a unique opportunity to investigate whether glutamate release and ON responses are important factors in the development of ON-OFF segregation. The combination of several different morphological analyses indicates that ON bipolar cells, as well as several distinct amacrine cells, in mGluR6 knock-out mice are normally distributed and correctly extend their terminals to defined retinal laminae. Importantly, both alpha and delta RGCs in adult mGluR6 knock-out mice are found monostratified into cell type-specific layers. Furthermore, no difference between wild-type and mGluR6 knock-out mice is observed in the maturation and dendritic stratification of developing RGCs. Hence, despite a deficit in normal ON responses, mGluR6 deficiency causes no abnormality in the retinal cellular organization nor in the stratifications of both ON bipolar cells and developing and mature RGCs. Based on these findings, we discuss several possible mechanisms that may underlie ON-OFF segregation of RGCs.  (+info)

Expression of type 2 iodothyronine deiodinase in hypothyroid rat brain indicates an important role of thyroid hormone in the development of specific primary sensory systems. (8/989)

Thyroid hormone is an important epigenetic factor in brain development, acting by modulating rates of gene expression. The active form of thyroid hormone, 3,5,3'-triiodothyronine (T3) is produced in part by the thyroid gland but also after 5'-deiodination of thyroxine (T4) in target tissues. In brain, approximately 80% of T3 is formed locally from T4 through the activity of the 5'-deiodinase type 2 (D2), an enzyme that is expressed mostly by glial cells, tanycytes in the third ventricle, and astrocytes throughout the brain. D2 activity is an important point of control of thyroid hormone action because it increases in situations of low T4, thus preserving brain T3 concentrations. In this work, we have studied the expression of D2 by quantitative in situ hybridization in hypothyroid animals during postnatal development. Our hypothesis was that those regions that are most dependent on thyroid hormone should present selective increases of D2 as a protection against hypothyroidism. D2 mRNA concentration was increased severalfold over normal levels in relay nuclei and cortical targets of the primary somatosensory and auditory pathways. The results suggest that these pathways are specifically protected against thyroid failure and that T3 has a role in the development of these structures. At the cellular level, expression was observed mainly in glial cells, although some interneurons of the cerebral cortex were also labeled. Therefore, the T3 target cells, mostly neurons, are dependent on local astrocytes for T3 supply.  (+info)

S100 calcium binding protein G, also known as calgranulin A or S100A8, is a member of the S100 family of proteins. These proteins are characterized by their ability to bind calcium ions and play a role in intracellular signaling and regulation of various cellular processes.

S100 calcium binding protein G forms a heterodimer with S100 calcium binding protein B (S100A9) and is involved in the inflammatory response, immune function, and tumor growth and progression. The S100A8/A9 heterocomplex has been shown to play a role in neutrophil activation and recruitment, as well as the regulation of cytokine production and cell proliferation.

Elevated levels of S100 calcium binding protein G have been found in various inflammatory conditions, such as rheumatoid arthritis, Crohn's disease, and psoriasis, as well as in several types of cancer, including breast, lung, and colon cancer. Therefore, it has been suggested that S100 calcium binding protein G may be a useful biomarker for the diagnosis and prognosis of these conditions.

Calcium-binding proteins (CaBPs) are a diverse group of proteins that have the ability to bind calcium ions (Ca^2+^) with high affinity and specificity. They play crucial roles in various cellular processes, including signal transduction, muscle contraction, neurotransmitter release, and protection against oxidative stress.

The binding of calcium ions to these proteins induces conformational changes that can either activate or inhibit their functions. Some well-known CaBPs include calmodulin, troponin C, S100 proteins, and parvalbumins. These proteins are essential for maintaining calcium homeostasis within cells and for mediating the effects of calcium as a second messenger in various cellular signaling pathways.

Calbindins are a family of calcium-binding proteins that are widely distributed in various tissues, including the gastrointestinal tract, brain, and kidney. They play important roles in regulating intracellular calcium levels and modulating calcium-dependent signaling pathways. Calbindin D28k, one of the major isoforms, is particularly abundant in the central nervous system and has been implicated in neuroprotection, neuronal plasticity, and regulation of neurotransmitter release. Deficiencies or alterations in calbindins have been associated with various pathological conditions, including neurological disorders and cancer.

Calbindin 1 is a calcium-binding protein that belongs to the family of EF-hand proteins. It is also known as calbindin D-28k, due to its molecular weight of approximately 28 kilodaltons. This protein is widely distributed in various tissues and organisms but is particularly abundant in the nervous system, where it plays crucial roles in calcium homeostasis, neuroprotection, and signal transduction.

In neurons, calbindin 1 is primarily located in the cytoplasm and dendrites, with lower concentrations found in the axons and nerve terminals. It helps regulate intracellular calcium levels by binding to calcium ions (Ca2+) with high affinity and capacity, thereby preventing rapid fluctuations in Ca2+ concentration that could trigger cellular damage or dysfunction.

Calbindin 1 has been implicated in several neuronal processes, including neurotransmitter release, synaptic plasticity, and neuronal excitability. Additionally, it is believed to provide neuroprotection against various insults, such as oxidative stress, glutamate excitotoxicity, and calcium overload, which are associated with neurological disorders like Alzheimer's disease, Parkinson's disease, and epilepsy.

In summary, calbindin 1 is a calcium-binding protein that plays essential roles in maintaining calcium homeostasis, neuroprotection, and neuronal signaling within the nervous system.

Calbindin 2 is a calcium-binding protein that belongs to the calbindin family and is found in various tissues, including the brain and intestines. It has a molecular weight of approximately 28 kDa and plays a crucial role in regulating intracellular calcium levels, neurotransmitter release, and protecting neurons from excitotoxicity. Calbindin 2 is also known as calbindin D-28k or calbindin-D9k, depending on the species and its molecular weight. It has multiple isoforms generated by alternative splicing and is involved in various physiological processes, including muscle contraction, hormone secretion, and cell proliferation. In the nervous system, calbindin 2 is expressed in specific populations of neurons and glial cells, where it functions as a neuroprotective agent and modulates synaptic plasticity.

Parvalbumins are a group of calcium-binding proteins that are primarily found in muscle and nerve tissues. They belong to the EF-hand superfamily, which is characterized by a specific structure containing helix-loop-helix motifs that bind calcium ions. Parvalbumins have a high affinity for calcium and play an essential role in regulating intracellular calcium concentrations during muscle contraction and nerve impulse transmission.

In muscle tissue, parvalbumins are found in fast-twitch fibers and help to facilitate rapid relaxation after muscle contraction by binding calcium ions and removing them from the cytoplasm. In nerve tissue, parvalbumins are expressed in inhibitory interneurons and modulate neuronal excitability by regulating intracellular calcium concentrations during synaptic transmission.

Parvalbumins have also been identified as potential allergens in certain foods, such as fish and shellfish, and may cause allergic reactions in sensitive individuals.

S100 proteins are a family of calcium-binding proteins that are involved in the regulation of various cellular processes, including cell growth and differentiation, intracellular signaling, and inflammation. They are found in high concentrations in certain types of cells, such as nerve cells (neurons), glial cells (supporting cells in the nervous system), and skin cells (keratinocytes).

The S100 protein family consists of more than 20 members, which are divided into several subfamilies based on their structural similarities. Some of the well-known members of this family include S100A1, S100B, S100 calcium-binding protein A8 (S100A8), and S100 calcium-binding protein A9 (S100A9).

Abnormal expression or regulation of S100 proteins has been implicated in various pathological conditions, such as neurodegenerative diseases, cancer, and inflammatory disorders. For example, increased levels of S100B have been found in the brains of patients with Alzheimer's disease, while overexpression of S100A8 and S100A9 has been associated with the development and progression of certain types of cancer.

Therefore, understanding the functions and regulation of S100 proteins is important for developing new diagnostic and therapeutic strategies for various diseases.

"EF hand motifs" are structural domains found in proteins that bind calcium ions. The name "EF hand" comes from the initials of the parvalbumin protein, where these structures were first identified, and the shape of the domain, which resembles the capital letters 'E' and 'F' lying on their sides when viewed in a certain orientation.

Each EF hand motif is composed of a helix-loop-helix structure, with the calcium-binding site located in the loop region. When calcium binds to the EF hand, it causes a conformational change in the protein, which can then activate or inhibit various cellular processes.

EF hand motifs are found in many different types of proteins, including calmodulin, troponin C, and S100 proteins. They play important roles in calcium signaling pathways, muscle contraction, and other physiological processes.

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

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

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

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

Calmodulin is a small, ubiquitous calcium-binding protein that plays a critical role in various intracellular signaling pathways. It functions as a calcium sensor, binding to and regulating the activity of numerous target proteins upon calcium ion (Ca^2+^) binding. Calmodulin is expressed in all eukaryotic cells and participates in many cellular processes, including muscle contraction, neurotransmitter release, gene expression, metabolism, and cell cycle progression.

The protein contains four EF-hand motifs that can bind Ca^2+^ ions. Upon calcium binding, conformational changes occur in the calmodulin structure, exposing hydrophobic surfaces that facilitate its interaction with target proteins. Calmodulin's targets include enzymes (such as protein kinases and phosphatases), ion channels, transporters, and cytoskeletal components. By modulating the activity of these proteins, calmodulin helps regulate essential cellular functions in response to changes in intracellular Ca^2+^ concentrations.

Calmodulin's molecular weight is approximately 17 kDa, and it consists of a single polypeptide chain with 148-150 amino acid residues. The protein can be found in both the cytoplasm and the nucleus of cells. In addition to its role as a calcium sensor, calmodulin has been implicated in various pathological conditions, including cancer, neurodegenerative diseases, and cardiovascular disorders.

Recoverin is a protein found in the retina of the eye that plays a role in protecting photoreceptor cells from light-induced damage. It is a member of the neuronal calcium sensor family and functions as a calmodulin-binding protein, which means it can bind to calcium ions and regulate various cellular processes.

Recoverin is particularly important for the regulation of visual transduction, the process by which light is converted into electrical signals in the eye. When exposed to light, photoreceptor cells release calcium ions, which then bind to recoverin and cause it to change shape. This shape change allows recoverin to inhibit a key enzyme involved in the visual transduction cascade, helping to prevent excessive signaling and protect the photoreceptor cells from damage.

Mutations in the gene that encodes recoverin have been associated with certain inherited eye diseases, such as congenital stationary night blindness and retinitis pigmentosa. These mutations can disrupt the normal function of recoverin and lead to progressive vision loss.

Calgranulin B is also known as S100 calcium-binding protein B or S100A9. It is a calcium-binding protein that plays a role in inflammation and immune response. Calgranulin B can be found in granulocytes, monocytes, and some epithelial cells. It forms heterocomplexes with calgranulin A (S100A8) and these complexes are involved in the regulation of innate immunity and inflammation. They can act as damage-associated molecular patterns (DAMPs) and contribute to the pathogenesis of various inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and certain types of cancer.

Calsequestrin is a protein found primarily in the sarcoplasmic reticulum of muscle cells, including both cardiac and skeletal muscles. It plays a crucial role in muscle function by binding calcium ions (Ca²+) and regulating calcium release during muscle contraction and relaxation cycles.

There are two main types of calsequestrin:

1. Calsequestrin 1 (CSQ1): This form is predominantly found in the sarcoplasmic reticulum of fast-twitch skeletal muscle fibers, which have a higher contraction speed and fatigability. CSQ1 has a high capacity for calcium binding but a lower affinity compared to calsequestrin 2.
2. Calsequestrin 2 (CSQ2): This form is primarily found in the sarcoplasmic reticulum of cardiac and slow-twitch skeletal muscle fibers, which have a lower contraction speed and fatigability. CSQ2 has a lower capacity for calcium binding but a higher affinity compared to calsequestrin 1.

Calsequestrin's ability to bind large amounts of calcium ions helps maintain low cytoplasmic calcium concentrations during muscle relaxation, while also serving as a reservoir for rapid calcium release during muscle contraction. Dysregulation of calsequestrin function has been implicated in several muscle disorders, including certain forms of cardiomyopathy and neuromuscular diseases.

Calgranulin A is also known as S100A8 or MRP-14. It is a calcium-binding protein that belongs to the S100 family of proteins. Calgranulin A is primarily found in the cytoplasm of neutrophils, a type of white blood cell involved in inflammation and immune response.

Calgranulin A can be released from neutrophils during inflammation and has been implicated in various biological processes, including regulation of innate immunity, inflammation, and cancer progression. It can also interact with other proteins to form heterodimers or multimers, such as calprotectin (S100A8/S100A9), which has been associated with several pathological conditions, including autoimmune diseases, infections, and cancer.

In medical research, Calgranulin A is often used as a biomarker for various inflammatory conditions, such as rheumatoid arthritis, inflammatory bowel disease, and chronic obstructive pulmonary disease (COPD). Elevated levels of Calgranulin A in body fluids, such as blood or sputum, may indicate the presence of an ongoing inflammatory response.

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.

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.

"Salamandra" is a term that refers to a genus of amphibians commonly known as fire salamanders. However, in a medical context, it is specifically used to refer to a homeopathic remedy made from the secretions of this animal. The homeopathic preparation is believed to stimulate the body's natural healing abilities and is used to treat various conditions such as skin disorders, respiratory issues, and psychological problems. Please note that the effectiveness and safety of homeopathic remedies are not widely accepted by the mainstream medical community and more research is needed to confirm their benefits.

Fluorescamine is not a medical term itself, but it is a chemical compound that is often used in laboratory settings for various biological and medical assays. Here is the general definition:

Fluorescamine (4-phenylspiro[furan-2(3H),1'-phthalan]-3,3'-dione) is a fluorogenic compound that reacts with primary amines, including the side chains of lysine residues in proteins, to produce highly fluorescent products. This reaction is commonly used for the detection and quantification of proteins or peptides in solution. The intensity of the fluorescence is proportional to the amount of protein or amine-containing compound present in the sample. Fluorescamine itself is non-fluorescent, but upon reacting with a primary amine, it forms a fluorescent isoindole derivative that can be easily detected and measured using various analytical techniques such as fluorometry or fluorescence microscopy.

Calcium signaling is the process by which cells regulate various functions through changes in intracellular calcium ion concentrations. Calcium ions (Ca^2+^) are crucial second messengers that play a critical role in many cellular processes, including muscle contraction, neurotransmitter release, gene expression, and programmed cell death (apoptosis).

Intracellular calcium levels are tightly regulated by a complex network of channels, pumps, and exchangers located on the plasma membrane and intracellular organelles such as the endoplasmic reticulum (ER) and mitochondria. These proteins control the influx, efflux, and storage of calcium ions within the cell.

Calcium signaling is initiated when an external signal, such as a hormone or neurotransmitter, binds to a specific receptor on the plasma membrane. This interaction triggers the opening of ion channels, allowing extracellular Ca^2+^ to flow into the cytoplasm. In some cases, this influx of calcium ions is sufficient to activate downstream targets directly. However, in most instances, the increase in intracellular Ca^2+^ serves as a trigger for the release of additional calcium from internal stores, such as the ER.

The release of calcium from the ER is mediated by ryanodine receptors (RyRs) and inositol trisphosphate receptors (IP3Rs), which are activated by specific second messengers generated in response to the initial external signal. The activation of these channels leads to a rapid increase in cytoplasmic Ca^2+^, creating a transient intracellular calcium signal known as a "calcium spark" or "calcium puff."

These localized increases in calcium concentration can then propagate throughout the cell as waves of elevated calcium, allowing for the spatial and temporal coordination of various cellular responses. The duration and amplitude of these calcium signals are finely tuned by the interplay between calcium-binding proteins, pumps, and exchangers, ensuring that appropriate responses are elicited in a controlled manner.

Dysregulation of intracellular calcium signaling has been implicated in numerous pathological conditions, including neurodegenerative diseases, cardiovascular disorders, and cancer. Therefore, understanding the molecular mechanisms governing calcium homeostasis and signaling is crucial for the development of novel therapeutic strategies targeting these diseases.

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.

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.

Collodion is a clear, colorless, viscous solution that is used in medicine and photography. Medically, collodion is often used as a temporary protective dressing for wounds, burns, or skin abrasions. When applied to the skin, it dries to form a flexible, waterproof film that helps to prevent infection and promote healing. Collodion is typically made from a mixture of nitrocellulose, alcohol, and ether.

In photography, collodion was historically used as a medium for wet plate photography, which was popular in the mid-19th century. The photographer would coat a glass plate with a thin layer of collodion, then sensitize it with silver salts before exposing and developing the image while the collodion was still wet. This process required the photographer to carry a portable darkroom and develop the plates immediately after exposure. Despite its challenges, the wet plate collodion process was able to produce highly detailed images, making it a popular technique for portrait photography during its time.

Calcium radioisotopes are radioactive isotopes of the element calcium. An isotope is a variant of an element that has the same number of protons in its atoms but a different number of neutrons, resulting in different mass numbers. Calcium has several radioisotopes, including calcium-41, calcium-45, calcium-47, and calcium-49.

These radioisotopes are used in various medical applications, such as in diagnostic imaging and research. For example, calcium-45 is commonly used in bone scans to help diagnose conditions like fractures, tumors, or infections. When administered to the patient, the calcium-45 is taken up by the bones, and a special camera can detect the gamma rays emitted by the radioisotope, providing images of the skeleton.

Similarly, calcium-47 is used in research to study calcium metabolism and bone physiology. The short half-life and low energy of the radiation emitted by these radioisotopes make them relatively safe for medical use, with minimal risk of harm to patients. However, as with any medical procedure involving radiation, appropriate precautions must be taken to ensure safety and minimize exposure.

'Entamoeba histolytica' is a species of microscopic, single-celled protozoan parasites that can cause a range of human health problems, primarily in the form of intestinal and extra-intestinal infections. The medical definition of 'Entamoeba histolytica' is as follows:

Entamoeba histolytica: A species of pathogenic protozoan parasites belonging to the family Entamoebidae, order Amoebida, and phylum Sarcomastigophora. These microorganisms are typically found in the form of cysts or trophozoites and can infect humans through the ingestion of contaminated food, water, or feces.

Once inside the human body, 'Entamoeba histolytica' parasites can colonize the large intestine, where they may cause a range of symptoms, from mild diarrhea to severe dysentery, depending on the individual's immune response and the location of the infection. In some cases, these parasites can also invade other organs, such as the liver, lungs, or brain, leading to more serious health complications.

The life cycle of 'Entamoeba histolytica' involves two main stages: the cyst stage and the trophozoite stage. The cysts are the infective form, which can be transmitted from person to person through fecal-oral contact or by ingesting contaminated food or water. Once inside the human body, these cysts excyst in the small intestine, releasing the motile and feeding trophozoites.

The trophozoites then migrate to the large intestine, where they can multiply by binary fission and cause tissue damage through their ability to phagocytize host cells and release cytotoxic substances. Some of these trophozoites may transform back into cysts, which are excreted in feces and can then infect other individuals.

Diagnosis of 'Entamoeba histolytica' infection typically involves the examination of stool samples for the presence of cysts or trophozoites, as well as serological tests to detect antibodies against the parasite. Treatment usually involves the use of antiparasitic drugs such as metronidazole or tinidazole, which can kill the trophozoites and help to control the infection. However, it is important to note that these drugs do not affect the cysts, so proper sanitation and hygiene measures are crucial to prevent the spread of the parasite.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

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.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Calcium channels are specialized proteins that span the membrane of cells and allow calcium ions (Ca²+) to flow in and out of the cell. They are crucial for many physiological processes, including muscle contraction, neurotransmitter release, hormone secretion, and gene expression.

There are several types of calcium channels, classified based on their biophysical and pharmacological properties. The most well-known are:

1. Voltage-gated calcium channels (VGCCs): These channels are activated by changes in the membrane potential. They are further divided into several subtypes, including L-type, P/Q-type, N-type, R-type, and T-type. VGCCs play a critical role in excitation-contraction coupling in muscle cells and neurotransmitter release in neurons.
2. Receptor-operated calcium channels (ROCCs): These channels are activated by the binding of an extracellular ligand, such as a hormone or neurotransmitter, to a specific receptor on the cell surface. ROCCs are involved in various physiological processes, including smooth muscle contraction and platelet activation.
3. Store-operated calcium channels (SOCCs): These channels are activated by the depletion of intracellular calcium stores, such as those found in the endoplasmic reticulum. SOCCs play a critical role in maintaining calcium homeostasis and signaling within cells.

Dysregulation of calcium channel function has been implicated in various diseases, including hypertension, arrhythmias, migraine, epilepsy, and neurodegenerative disorders. Therefore, calcium channels are an important target for drug development and therapy.

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

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

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

I apologize, but I am not able to provide a medical definition for "Egtazic Acid" because it is not a term that is recognized in the field of medicine or pharmacology. It is possible that you may have meant "Egтарic Acid," which also does not have a specific medical meaning, or "Ethylene Glycol Tetraacetic Acid (EGTA)," which is a chemical compound used in research and medicine for its ability to bind calcium ions. If you have any other questions, I would be happy to try to help answer them.

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.

The sarcoplasmic reticulum (SR) is a specialized type of smooth endoplasmic reticulum found in muscle cells, particularly in striated muscles such as skeletal and cardiac muscles. It is a complex network of tubules that surrounds the myofibrils, the contractile elements of the muscle fiber.

The primary function of the sarcoplasmic reticulum is to store calcium ions (Ca2+) and regulate their release during muscle contraction and uptake during muscle relaxation. The SR contains a high concentration of calcium-binding proteins, such as calsequestrin, which help to maintain this storage.

The release of calcium ions from the sarcoplasmic reticulum is triggered by an action potential that travels along the muscle fiber's sarcolemma and into the muscle fiber's interior (the sarcoplasm). This action potential causes the voltage-gated calcium channels in the SR membrane, known as ryanodine receptors, to open, releasing Ca2+ ions into the sarcoplasm.

The increased concentration of Ca2+ ions in the sarcoplasm triggers muscle contraction by binding to troponin, a protein associated with actin filaments, causing a conformational change that exposes the active sites on actin for myosin heads to bind and generate force.

After muscle contraction, the calcium ions must be actively transported back into the sarcoplasmic reticulum by Ca2+ ATPase pumps, also known as sarco(endo)plasmic reticulum calcium ATPases (SERCAs). This process helps to lower the concentration of Ca2+ in the sarcoplasm and allows the muscle fiber to relax.

Overall, the sarcoplasmic reticulum plays a crucial role in excitation-contraction coupling, the process by which action potentials trigger muscle contraction.

Dietary calcium is a type of calcium that is obtained through food sources. Calcium is an essential mineral that is necessary for many bodily functions, including bone formation and maintenance, muscle contraction, nerve impulse transmission, and blood clotting.

The recommended daily intake of dietary calcium varies depending on age, sex, and other factors. For example, the recommended daily intake for adults aged 19-50 is 1000 mg, while women over 50 and men over 70 require 1200 mg per day.

Good dietary sources of calcium include dairy products such as milk, cheese, and yogurt; leafy green vegetables like broccoli and kale; fortified cereals and juices; and certain types of fish, such as salmon and sardines. It is important to note that some foods can inhibit the absorption of calcium, including oxalates found in spinach and rhubarb, and phytates found in whole grains and legumes.

If a person is unable to get enough calcium through their diet, they may need to take calcium supplements. However, it is important to talk to a healthcare provider before starting any new supplement regimen, as excessive intake of calcium can lead to negative health effects.

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.

Nerve tissue proteins are specialized proteins found in the nervous system that provide structural and functional support to nerve cells, also known as neurons. These proteins include:

1. Neurofilaments: These are type IV intermediate filaments that provide structural support to neurons and help maintain their shape and size. They are composed of three subunits - NFL (light), NFM (medium), and NFH (heavy).

2. Neuronal Cytoskeletal Proteins: These include tubulins, actins, and spectrins that provide structural support to the neuronal cytoskeleton and help maintain its integrity.

3. Neurotransmitter Receptors: These are specialized proteins located on the postsynaptic membrane of neurons that bind neurotransmitters released by presynaptic neurons, triggering a response in the target cell.

4. Ion Channels: These are transmembrane proteins that regulate the flow of ions across the neuronal membrane and play a crucial role in generating and transmitting electrical signals in neurons.

5. Signaling Proteins: These include enzymes, receptors, and adaptor proteins that mediate intracellular signaling pathways involved in neuronal development, differentiation, survival, and death.

6. Adhesion Proteins: These are cell surface proteins that mediate cell-cell and cell-matrix interactions, playing a crucial role in the formation and maintenance of neural circuits.

7. Extracellular Matrix Proteins: These include proteoglycans, laminins, and collagens that provide structural support to nerve tissue and regulate neuronal migration, differentiation, and survival.

A muscle is a soft tissue in our body that contracts to produce force and motion. It is composed mainly of specialized cells called muscle fibers, which are bound together by connective tissue. There are three types of muscles: skeletal (voluntary), smooth (involuntary), and cardiac. Skeletal muscles attach to bones and help in movement, while smooth muscles are found within the walls of organs and blood vessels, helping with functions like digestion and circulation. Cardiac muscle is the specific type that makes up the heart, allowing it to pump blood throughout the body.

Fluorescence spectrometry is a type of analytical technique used to investigate the fluorescent properties of a sample. It involves the measurement of the intensity of light emitted by a substance when it absorbs light at a specific wavelength and then re-emits it at a longer wavelength. This process, known as fluorescence, occurs because the absorbed energy excites electrons in the molecules of the substance to higher energy states, and when these electrons return to their ground state, they release the excess energy as light.

Fluorescence spectrometry typically measures the emission spectrum of a sample, which is a plot of the intensity of emitted light versus the wavelength of emission. This technique can be used to identify and quantify the presence of specific fluorescent molecules in a sample, as well as to study their photophysical properties.

Fluorescence spectrometry has many applications in fields such as biochemistry, environmental science, and materials science. For example, it can be used to detect and measure the concentration of pollutants in water samples, to analyze the composition of complex biological mixtures, or to study the properties of fluorescent nanomaterials.

"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.

Calcium isotopes refer to variants of the chemical element calcium (ca) that have different numbers of neutrons in their atomic nuclei, and therefore differ in their atomic masses while having the same number of protons. The most common and stable calcium isotope is Calcium-40, which contains 20 protons and 20 neutrons. However, calcium has several other isotopes, including Calcium-42, Calcium-43, Calcium-44, and Calcium-46 to -52, each with different numbers of neutrons. Some of these isotopes are radioactive and decay over time. The relative abundances of calcium isotopes can vary in different environments and can provide information about geological and biological processes.

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.

Troponin C is a subunit of the troponin complex, which is a protein complex that plays a crucial role in muscle contraction. In the heart, the troponin complex is found in the myofibrils of cardiac muscle cells (cardiomyocytes). It is composed of three subunits: troponin C, troponin T, and troponin I.

Troponin C has the ability to bind calcium ions (Ca²+), which is essential for muscle contraction. When Ca²+ binds to troponin C, it causes a conformational change that leads to the exposure of binding sites on troponin I for another protein called actin. This interaction allows for the cross-bridge formation between actin and myosin, generating the force needed for muscle contraction.

In clinical settings, cardiac troponins (including troponin T and troponin I) are commonly measured in blood tests to diagnose and monitor heart damage, particularly in conditions like myocardial infarction (heart attack). However, Troponin C is not typically used as a biomarker for heart injury because it is less specific to the heart than troponin T and troponin I. Increased levels of Troponin C in the blood can be found in various conditions involving muscle damage or disease, making it less useful for diagnosing heart-specific issues.

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.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

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.

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.

Calcitriol is the active form of vitamin D, also known as 1,25-dihydroxyvitamin D. It is a steroid hormone that plays a crucial role in regulating calcium and phosphate levels in the body to maintain healthy bones. Calcitriol is produced in the kidneys from its precursor, calcidiol (25-hydroxyvitamin D), which is derived from dietary sources or synthesized in the skin upon exposure to sunlight.

Calcitriol promotes calcium absorption in the intestines, helps regulate calcium and phosphate levels in the kidneys, and stimulates bone cells (osteoblasts) to form new bone tissue while inhibiting the activity of osteoclasts, which resorb bone. This hormone is essential for normal bone mineralization and growth, as well as for preventing hypocalcemia (low calcium levels).

In addition to its role in bone health, calcitriol has various other physiological functions, including modulating immune responses, cell proliferation, differentiation, and apoptosis. Calcitriol deficiency or resistance can lead to conditions such as rickets in children and osteomalacia or osteoporosis in adults.

The S100 calcium binding protein beta subunit, also known as S100B, is a member of the S100 family of proteins. These proteins are characterized by their ability to bind calcium ions and play a role in intracellular signaling pathways. The S100B protein is made up of two subunits, alpha and beta, which form a homodimer. It is primarily expressed in astrocytes, a type of glial cell found in the central nervous system.

S100B has been shown to have both intracellular and extracellular functions. Inside cells, it regulates various processes such as the dynamics of cytoskeleton, calcium homeostasis and cell proliferation. Extracellularly, S100B acts as a damage-associated molecular pattern (DAMP) molecule, released from damaged or stressed cells, where it can interact with receptors on other cells to induce inflammatory responses, neuronal death and contribute to the pathogenesis of several neurological disorders.

Elevated levels of S100B in cerebrospinal fluid (CSF) or blood are associated with various central nervous system injuries such as traumatic brain injury, spinal cord injury, stroke, neurodegenerative diseases and some types of cancer. Therefore, it is considered a biomarker for these conditions.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

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.

Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.

"Chickens" is a common term used to refer to the domesticated bird, Gallus gallus domesticus, which is widely raised for its eggs and meat. However, in medical terms, "chickens" is not a standard term with a specific definition. If you have any specific medical concern or question related to chickens, such as food safety or allergies, please provide more details so I can give a more accurate answer.

Calcium chloride is an inorganic compound with the chemical formula CaCl2. It is a white, odorless, and tasteless solid that is highly soluble in water. Calcium chloride is commonly used as a de-icing agent, a desiccant (drying agent), and a food additive to enhance texture and flavor.

In medical terms, calcium chloride can be used as a medication to treat hypocalcemia (low levels of calcium in the blood) or hyperkalemia (high levels of potassium in the blood). It is administered intravenously and works by increasing the concentration of calcium ions in the blood, which helps to regulate various physiological processes such as muscle contraction, nerve impulse transmission, and blood clotting.

However, it is important to note that calcium chloride can have adverse effects if not used properly or in excessive amounts. It can cause tissue irritation, cardiac arrhythmias, and other serious complications. Therefore, its use should be monitored carefully by healthcare professionals.

Staphylococcal Protein A (SpA) is a cell wall-associated protein found on many strains of the bacterium Staphylococcus aureus. It plays an important role in the pathogenesis of staphylococcal infections. SpA has several domains that allow it to bind to various host proteins, including immunoglobulins (Igs), complement components, and fibrinogen.

The protein A's ability to bind to the Fc region of Igs, particularly IgG, enables it to inhibit phagocytosis by masking the antibodies' binding sites, thus helping the bacterium evade the host immune system. Additionally, SpA can activate complement component C1 and initiate the classical complement pathway, leading to the release of anaphylatoxins and the formation of the membrane attack complex, which can cause tissue damage.

Furthermore, SpA's binding to fibrinogen promotes bacterial adherence and colonization of host tissues, contributing to the establishment of infection. Overall, Staphylococcal Protein A is a crucial virulence factor in S. aureus infections, making it an important target for the development of novel therapeutic strategies.

Calcium carbonate is a chemical compound with the formula CaCO3. It is a common substance found in rocks and in the shells of many marine animals. As a mineral, it is known as calcite or aragonite.

In the medical field, calcium carbonate is often used as a dietary supplement to prevent or treat calcium deficiency. It is also commonly used as an antacid to neutralize stomach acid and relieve symptoms of heartburn, acid reflux, and indigestion.

Calcium carbonate works by reacting with hydrochloric acid in the stomach to form water, carbon dioxide, and calcium chloride. This reaction helps to raise the pH level in the stomach and neutralize excess acid.

It is important to note that excessive use of calcium carbonate can lead to hypercalcemia, a condition characterized by high levels of calcium in the blood, which can cause symptoms such as nausea, vomiting, constipation, confusion, and muscle weakness. Therefore, it is recommended to consult with a healthcare provider before starting any new supplement regimen.

'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.

Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.

Neurons, also known as nerve cells or neurocytes, are specialized cells that constitute the basic unit of the nervous system. They are responsible for receiving, processing, and transmitting information and signals within the body. Neurons have three main parts: the dendrites, the cell body (soma), and the axon. The dendrites receive signals from other neurons or sensory receptors, while the axon transmits these signals to other neurons, muscles, or glands. The junction between two neurons is called a synapse, where neurotransmitters are released to transmit the signal across the gap (synaptic cleft) to the next neuron. Neurons vary in size, shape, and structure depending on their function and location within the nervous system.

Sequence homology in nucleic acids refers to the similarity or identity between the nucleotide sequences of two or more DNA or RNA molecules. It is often used as a measure of biological relationship between genes, organisms, or populations. High sequence homology suggests a recent common ancestry or functional constraint, while low sequence homology may indicate a more distant relationship or different functions.

Nucleic acid sequence homology can be determined by various methods such as pairwise alignment, multiple sequence alignment, and statistical analysis. The degree of homology is typically expressed as a percentage of identical or similar nucleotides in a given window of comparison.

It's important to note that the interpretation of sequence homology depends on the biological context and the evolutionary distance between the sequences compared. Therefore, functional and experimental validation is often necessary to confirm the significance of sequence homology.

GTP-binding protein alpha subunits, G12-G13, are a type of heterotrimeric G proteins that play a crucial role in intracellular signaling pathways. These proteins are composed of three subunits: alpha, beta, and gamma. The alpha subunit of G12-G13 proteins is referred to as Gα12 or Gα13 and binds to guanosine triphosphate (GTP) and guanosine diphosphate (GDP).

When a G protein-coupled receptor (GPCR) is activated by an extracellular signal, it catalyzes the exchange of GDP for GTP on the alpha subunit. This leads to a conformational change in the alpha subunit, causing it to dissociate from the beta and gamma subunits and interact with downstream effectors.

Gα12 and Gα13 are unique among the heterotrimeric G proteins because they preferentially activate Rho guanine nucleotide exchange factors (RhoGEFs), which in turn activate Rho GTPases, leading to changes in the actin cytoskeleton and cellular responses such as cell migration, proliferation, and differentiation.

Dysregulation of GTP-binding protein alpha subunits, G12-G13, has been implicated in various diseases, including cancer and neurological disorders.

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.

Terbium is not a medical term, but a chemical element. It is a rare earth element with the symbol Tb and atomic number 65. It is soft, silvery-white, and has a metallic shine. Terbium is not used in medicine to treat or diagnose diseases directly. However, it does have some applications in medical technology such as in doping materials for magnetic resonance imaging (MRI) machines and in the creation of high-intensity gas discharge lamps that are used in medical lighting.

Streptococcus is a genus of Gram-positive, spherical bacteria that typically form pairs or chains when clustered together. These bacteria are facultative anaerobes, meaning they can grow in the presence or absence of oxygen. They are non-motile and do not produce spores.

Streptococcus species are commonly found on the skin and mucous membranes of humans and animals. Some strains are part of the normal flora of the body, while others can cause a variety of infections, ranging from mild skin infections to severe and life-threatening diseases such as sepsis, meningitis, and toxic shock syndrome.

The pathogenicity of Streptococcus species depends on various virulence factors, including the production of enzymes and toxins that damage tissues and evade the host's immune response. One of the most well-known Streptococcus species is Streptococcus pyogenes, also known as group A streptococcus (GAS), which is responsible for a wide range of clinical manifestations, including pharyngitis (strep throat), impetigo, cellulitis, necrotizing fasciitis, and rheumatic fever.

It's important to note that the classification of Streptococcus species has evolved over time, with many former members now classified as different genera within the family Streptococcaceae. The current classification system is based on a combination of phenotypic characteristics (such as hemolysis patterns and sugar fermentation) and genotypic methods (such as 16S rRNA sequencing and multilocus sequence typing).

Sprague-Dawley rats are a strain of albino laboratory rats that are widely used in scientific research. They were first developed by researchers H.H. Sprague and R.C. Dawley in the early 20th century, and have since become one of the most commonly used rat strains in biomedical research due to their relatively large size, ease of handling, and consistent genetic background.

Sprague-Dawley rats are outbred, which means that they are genetically diverse and do not suffer from the same limitations as inbred strains, which can have reduced fertility and increased susceptibility to certain diseases. They are also characterized by their docile nature and low levels of aggression, making them easier to handle and study than some other rat strains.

These rats are used in a wide variety of research areas, including toxicology, pharmacology, nutrition, cancer, and behavioral studies. Because they are genetically diverse, Sprague-Dawley rats can be used to model a range of human diseases and conditions, making them an important tool in the development of new drugs and therapies.

Circular dichroism (CD) is a technique used in physics and chemistry to study the structure of molecules, particularly large biological molecules such as proteins and nucleic acids. It measures the difference in absorption of left-handed and right-handed circularly polarized light by a sample. This difference in absorption can provide information about the three-dimensional structure of the molecule, including its chirality or "handedness."

In more technical terms, CD is a form of spectroscopy that measures the differential absorption of left and right circularly polarized light as a function of wavelength. The CD signal is measured in units of millidegrees (mdeg) and can be positive or negative, depending on the type of chromophore and its orientation within the molecule.

CD spectra can provide valuable information about the secondary and tertiary structure of proteins, as well as the conformation of nucleic acids. For example, alpha-helical proteins typically exhibit a strong positive band near 190 nm and two negative bands at around 208 nm and 222 nm, while beta-sheet proteins show a strong positive band near 195 nm and two negative bands at around 217 nm and 175 nm.

CD spectroscopy is a powerful tool for studying the structural changes that occur in biological molecules under different conditions, such as temperature, pH, or the presence of ligands or other molecules. It can also be used to monitor the folding and unfolding of proteins, as well as the binding of drugs or other small molecules to their targets.

Troponin is a protein complex found in cardiac and skeletal muscle cells that plays a critical role in muscle contraction. It consists of three subunits: troponin C, which binds calcium ions; troponin I, which inhibits the interaction between actin and myosin in the absence of calcium; and troponin T, which binds to tropomyosin and helps anchor the complex to the muscle filament.

In clinical medicine, "troponin" usually refers to cardiac-specific isoforms of these proteins (cTnI and cTnT) that are released into the bloodstream following damage to the heart muscle, such as occurs in myocardial infarction (heart attack). Measurement of troponin levels in the blood is a sensitive and specific biomarker for the diagnosis of acute myocardial infarction.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

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.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

Calcium phosphates are a group of minerals that are important components of bones and teeth. They are also found in some foods and are used in dietary supplements and medical applications. Chemically, calcium phosphates are salts of calcium and phosphoric acid, and they exist in various forms, including hydroxyapatite, which is the primary mineral component of bone tissue. Other forms of calcium phosphates include monocalcium phosphate, dicalcium phosphate, and tricalcium phosphate, which are used as food additives and dietary supplements. Calcium phosphates are important for maintaining strong bones and teeth, and they also play a role in various physiological processes, such as nerve impulse transmission and muscle contraction.

Magnesium is an essential mineral that plays a crucial role in various biological processes in the human body. It is the fourth most abundant cation in the body and is involved in over 300 enzymatic reactions, including protein synthesis, muscle and nerve function, blood glucose control, and blood pressure regulation. Magnesium also contributes to the structural development of bones and teeth.

In medical terms, magnesium deficiency can lead to several health issues, such as muscle cramps, weakness, heart arrhythmias, and seizures. On the other hand, excessive magnesium levels can cause symptoms like diarrhea, nausea, and muscle weakness. Magnesium supplements or magnesium-rich foods are often recommended to maintain optimal magnesium levels in the body.

Some common dietary sources of magnesium include leafy green vegetables, nuts, seeds, legumes, whole grains, and dairy products. Magnesium is also available in various forms as a dietary supplement, including magnesium oxide, magnesium citrate, magnesium chloride, and magnesium glycinate.

Tacrolimus binding proteins, also known as FK506 binding proteins (FKBPs), are a group of intracellular proteins that bind to the immunosuppressive drug tacrolimus (also known as FK506) and play a crucial role in its mechanism of action. Tacrolimus is primarily used in organ transplantation to prevent rejection of the transplanted organ.

FKBPs are a family of peptidyl-prolyl cis-trans isomerases (PPIases) that catalyze the conversion of proline residues from their cis to trans conformations in proteins, thereby regulating protein folding and function. FKBP12, a member of this family, has a high affinity for tacrolimus and forms a complex with it upon entry into the cell.

The formation of the tacrolimus-FKBP12 complex inhibits calcineurin, a serine/threonine phosphatase that plays a critical role in T-cell activation. Calcineurin inhibition prevents the dephosphorylation and nuclear translocation of the transcription factor NFAT (nuclear factor of activated T-cells), thereby blocking the expression of genes involved in T-cell activation, proliferation, and cytokine production.

In summary, tacrolimus binding proteins are intracellular proteins that bind to tacrolimus and inhibit calcineurin, leading to the suppression of T-cell activation and immune response, which is essential in organ transplantation and other immunological disorders.

Nuclear Magnetic Resonance (NMR) Biomolecular is a research technique that uses magnetic fields and radio waves to study the structure and dynamics of biological molecules, such as proteins and nucleic acids. This technique measures the magnetic properties of atomic nuclei within these molecules, specifically their spin, which can be influenced by the application of an external magnetic field.

When a sample is placed in a strong magnetic field, the nuclei absorb and emit electromagnetic radiation at specific frequencies, known as resonance frequencies, which are determined by the molecular structure and environment of the nuclei. By analyzing these resonance frequencies and their interactions, researchers can obtain detailed information about the three-dimensional structure, dynamics, and interactions of biomolecules.

NMR spectroscopy is a non-destructive technique that allows for the study of biological molecules in solution, which makes it an important tool for understanding the function and behavior of these molecules in their natural environment. Additionally, NMR can be used to study the effects of drugs, ligands, and other small molecules on biomolecular structure and dynamics, making it a valuable tool in drug discovery and development.

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.

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.

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

GTP-binding protein alpha subunits, Gi-Go, are a type of heterotrimeric G proteins that play a crucial role in signal transduction pathways associated with many hormones and neurotransmitters. These G proteins are composed of three subunits: alpha, beta, and gamma. The "Gi-Go" specifically refers to the alpha subunit of these G proteins, which can exist in two isoforms, Gi and Go.

When a G protein-coupled receptor (GPCR) is activated by an agonist, it undergoes a conformational change that allows it to act as a guanine nucleotide exchange factor (GEF). The GEF activity of the GPCR promotes the exchange of GDP for GTP on the alpha subunit of the heterotrimeric G protein. Once GTP is bound, the alpha subunit dissociates from the beta-gamma dimer and can then interact with downstream effectors to modulate various cellular responses.

The Gi-Go alpha subunits are inhibitory in nature, meaning that they typically inhibit the activity of adenylyl cyclase, an enzyme responsible for converting ATP to cAMP. This reduction in cAMP levels can have downstream effects on various cellular processes, such as gene transcription, ion channel regulation, and metabolic pathways.

In summary, GTP-binding protein alpha subunits, Gi-Go, are heterotrimeric G proteins that play an essential role in signal transduction pathways by modulating adenylyl cyclase activity upon GPCR activation, ultimately influencing various cellular responses through cAMP regulation.

Immunoglobulin G (IgG) is a type of antibody, which is a protective protein produced by the immune system in response to foreign substances like bacteria or viruses. IgG is the most abundant type of antibody in human blood, making up about 75-80% of all antibodies. It is found in all body fluids and plays a crucial role in fighting infections caused by bacteria, viruses, and toxins.

IgG has several important functions:

1. Neutralization: IgG can bind to the surface of bacteria or viruses, preventing them from attaching to and infecting human cells.
2. Opsonization: IgG coats the surface of pathogens, making them more recognizable and easier for immune cells like neutrophils and macrophages to phagocytose (engulf and destroy) them.
3. Complement activation: IgG can activate the complement system, a group of proteins that work together to help eliminate pathogens from the body. Activation of the complement system leads to the formation of the membrane attack complex, which creates holes in the cell membranes of bacteria, leading to their lysis (destruction).
4. Antibody-dependent cellular cytotoxicity (ADCC): IgG can bind to immune cells like natural killer (NK) cells and trigger them to release substances that cause target cells (such as virus-infected or cancerous cells) to undergo apoptosis (programmed cell death).
5. Immune complex formation: IgG can form immune complexes with antigens, which can then be removed from the body through various mechanisms, such as phagocytosis by immune cells or excretion in urine.

IgG is a critical component of adaptive immunity and provides long-lasting protection against reinfection with many pathogens. It has four subclasses (IgG1, IgG2, IgG3, and IgG4) that differ in their structure, function, and distribution in the body.

"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.

I'm sorry for any confusion, but "thermodynamics" is not a term that has a specific medical definition. It is a branch of physics that deals with the relationships between heat and other forms of energy. However, the principles of thermodynamics can be applied to biological systems, including those in the human body, such as in the study of metabolism or muscle function. But in a medical context, "thermodynamics" would not be a term used independently as a diagnosis, treatment, or any medical condition.

Calcium channels, L-type, are a type of voltage-gated calcium channel that are widely expressed in many excitable cells, including cardiac and skeletal muscle cells, as well as certain neurons. These channels play a crucial role in the regulation of various cellular functions, such as excitation-contraction coupling, hormone secretion, and gene expression.

L-type calcium channels are composed of five subunits: alpha-1, alpha-2, beta, gamma, and delta. The alpha-1 subunit is the pore-forming subunit that contains the voltage sensor and the selectivity filter for calcium ions. It has four repeated domains (I-IV), each containing six transmembrane segments (S1-S6). The S4 segment in each domain functions as a voltage sensor, moving outward upon membrane depolarization to open the channel and allow calcium ions to flow into the cell.

L-type calcium channels are activated by membrane depolarization and have a relatively slow activation and inactivation time course. They are also modulated by various intracellular signaling molecules, such as protein kinases and G proteins. L-type calcium channel blockers, such as nifedipine and verapamil, are commonly used in the treatment of hypertension, angina, and certain cardiac arrhythmias.

Hippocalcin is a type of neuronal calcium sensor protein, which is primarily expressed in the hippocampus region of the brain. It belongs to the family of EF-hand calcium-binding proteins and plays a crucial role in regulating intracellular calcium signaling pathways that are involved in various cellular processes such as neurotransmitter release, gene expression, and synaptic plasticity. Hippocalcin has been implicated in several neurological disorders, including epilepsy and Alzheimer's disease.

Insulin-like growth factor binding proteins (IGFBPs) are a family of proteins that bind to and regulate the biological activity of insulin-like growth factors (IGFs), specifically IGF-1 and IGF-2. There are six distinct IGFBPs (IGFBP-1 to IGFBP-6) in humans, each with unique structural features, expression patterns, and functions.

The primary function of IGFBPs is to modulate the interaction between IGFs and their cell surface receptors, thereby controlling IGF-mediated intracellular signaling pathways involved in cell growth, differentiation, and survival. IGFBPs can either enhance or inhibit IGF actions depending on the specific context, such as cell type, subcellular localization, and presence of other binding partners.

In addition to their role in IGF regulation, some IGFBPs have IGF-independent functions, including direct interaction with cell surface receptors, modulation of extracellular matrix composition, and participation in cell migration and apoptosis. Dysregulation of IGFBP expression and function has been implicated in various pathological conditions, such as cancer, diabetes, and cardiovascular diseases.

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

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

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

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

DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.

The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.

DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.

Calcium oxalate is a chemical compound with the formula CaC2O4. It is the most common type of stone found in kidneys, also known as kidney stones. Calcium oxalate forms when there is too much calcium or oxalate in the urine. This can occur due to various reasons such as dietary habits, dehydration, medical conditions like hyperparathyroidism, or genetic factors.

Calcium oxalate stones are hard and crystalline and can cause severe pain during urination or while passing through the urinary tract. They may also lead to other symptoms like blood in the urine, nausea, vomiting, or fever. Prevention strategies for calcium oxalate stones include staying hydrated, following a balanced diet, and taking prescribed medications to control the levels of calcium and oxalate in the body.

"Animals, Zoo" is not a medical term. However, it generally refers to a collection of various species of wild animals kept in enclosures or exhibits for the public to view and learn about. These animals are usually obtained from different parts of the world and live in environments that attempt to simulate their natural habitats. Zoos play an essential role in conservation efforts, education, and research. They provide a unique opportunity for people to connect with wildlife and understand the importance of preserving and protecting endangered species and their ecosystems.

Chelating agents are substances that can bind and form stable complexes with certain metal ions, preventing them from participating in chemical reactions. In medicine, chelating agents are used to remove toxic or excessive amounts of metal ions from the body. For example, ethylenediaminetetraacetic acid (EDTA) is a commonly used chelating agent that can bind with heavy metals such as lead and mercury, helping to eliminate them from the body and reduce their toxic effects. Other chelating agents include dimercaprol (BAL), penicillamine, and deferoxamine. These agents are used to treat metal poisoning, including lead poisoning, iron overload, and copper toxicity.

I'm sorry for any confusion, but "Ytterbium" is not a medical term. It is a chemical element with the symbol "Yb" and atomic number 70. Ytterbium is a rare earth metal that is silvery white, soft, malleable, and has many uses in scientific research, particularly in the field of laser technology.

If you have any medical questions or terms you would like me to define, please let me know!

Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.

Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.

Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

Lanthanum is not a medical term itself, but it is a chemical element with the symbol "La" and atomic number 57. It is a soft, ductile, silvery-white metal that belongs to the lanthanide series in the periodic table.

However, in medical contexts, lanthanum may be mentioned as a component of certain medications or medical devices. For example, lanthanum carbonate (trade name Fosrenol) is a medication used to treat hyperphosphatemia (elevated levels of phosphate in the blood) in patients with chronic kidney disease. Lanthanum carbonate works by binding to phosphate in the gastrointestinal tract, preventing its absorption into the bloodstream.

It is important to note that lanthanum compounds are not biologically active and do not have any specific medical effects on their own. Any medical uses of lanthanum are related to its physical or chemical properties, rather than its biological activity.

Calcium gluconate is a medical compound that is used primarily as a medication to treat conditions related to low calcium levels in the body (hypocalcemia) or to prevent calcium deficiency. It is also used as an antidote for treating poisoning from certain chemicals, such as beta-blockers and fluoride.

Calcium gluconate is a form of calcium salt, which is combined with gluconic acid, a natural organic acid found in various fruits and honey. This compound has a high concentration of calcium, making it an effective supplement for increasing calcium levels in the body.

In medical settings, calcium gluconate can be administered orally as a tablet or liquid solution, or it can be given intravenously (directly into a vein) by a healthcare professional. The intravenous route is typically used in emergency situations to quickly raise calcium levels and treat symptoms of hypocalcemia, such as muscle cramps, spasms, or seizures.

It's important to note that while calcium gluconate can be beneficial for treating low calcium levels, it should only be used under the guidance of a healthcare provider, as improper use or overdose can lead to serious side effects, including kidney damage and heart problems.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

RNA-binding proteins (RBPs) are a class of proteins that selectively interact with RNA molecules to form ribonucleoprotein complexes. These proteins play crucial roles in the post-transcriptional regulation of gene expression, including pre-mRNA processing, mRNA stability, transport, localization, and translation. RBPs recognize specific RNA sequences or structures through their modular RNA-binding domains, which can be highly degenerate and allow for the recognition of a wide range of RNA targets. The interaction between RBPs and RNA is often dynamic and can be regulated by various post-translational modifications of the proteins or by environmental stimuli, allowing for fine-tuning of gene expression in response to changing cellular needs. Dysregulation of RBP function has been implicated in various human diseases, including neurological disorders and cancer.

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.

S100A7, S100 calcium-binding protein A7. This disambiguation page lists articles associated with the title Psoriasin. If an ...
... is a protein that in humans is encoded by the S100A7A (alias: S100A15) gene. S100 proteins are a diverse calcium-binding family ... "Entrez Gene: S100 calcium binding protein A7A". Wolf R, Mirmohammadsadegh A, Walz M, Lysa B, Tartler U, Remus R, Hengge U, ... "Entrez Gene: S100a7a S100 calcium binding protein". Briso EM, Guinea-Viniegra J, Bakiri L, Rogon Z, Petzelbauer P, Eils R, Wolf ... The amino acid sequence reveals a conserved C-terminal and a variant N-terminal EF-hand typical for S100 proteins (101 amino ...
"Entrez Gene: S100 calcium binding protein A7A". Wolf, R; Voscopoulos, CJ; FitzGerald, PC; Goldsmith, P; Cataisson, C; Gunsior, ... The S100 calcium-binding protein mS100a7a15 is the murine ortholog of human S100A7 (Psoriasin) and human S100A15 (Koebnerisin ... S100 proteins are a diverse calcium-binding family that mediate fundamental cellular and extracellular processes including cell ... motifs corresponding to the for S100 proteins typical conserved C-terminal and a variant N-terminal EF-hand calcium binding ...
S100 calcium binding protein A14 (S100A14) is a protein that in humans is encoded by the S100A14 gene. This gene encodes a ... "Entrez Gene: S100 calcium binding protein A14". Wang HY, Zhang JY, Cui JT, Tan XH, Li WM, Gu J, Lu YY (Jan 2010). "Expression ... member of the S100 protein family which contains an EF-hand motif and binds calcium. The gene is located in a cluster of S100 ... rationale for a new nomenclature of the S100 calcium-binding protein family". Genomics. 25 (3): 638-43. doi:10.1016/0888-7543( ...
Protein S100-A1, also known as S100 calcium-binding protein A1 is a protein which in humans is encoded by the S100A1 gene. ... "Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), ... Donato R (July 1999). "Functional roles of S100 proteins, calcium-binding proteins of the EF-hand type". Biochimica et ... "Entrez Gene: S100A1 S100 calcium binding protein A1". Morii K, Tanaka R, Takahashi Y, Minoshima S, Fukuyama R, Shimizu N, ...
S100 calcium-binding protein A16 (S100A16) is a protein that in humans is encoded by the S100A16 gene. GRCh38: Ensembl release ... "Entrez Gene: S100A16 S100 calcium binding protein A16". Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. Bibcode: ... Marenholz I, Heizmann CW (2004). "S100A16, a ubiquitously expressed EF-hand protein which is up-regulated in tumors". Biochem. ...
S100 calcium-binding protein A2 (S100A2) is a protein that in humans is encoded by the S100A2 gene and it is located on ... "Entrez Gene: S100A2 S100 calcium binding protein A2". Suzuki F, Oridate N, Homma A, Nakamaru Y, Nagahashi T, Yagi K, et al. ( ... Groves P, Finn BE, Kuźnicki J, Forsén S (January 1998). "A model for target protein binding to calcium-activated S100 dimers". ... Schäfer BW, Heizmann CW (April 1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends in ...
S100 calcium-binding protein A11 (S100A11) is a protein that in humans is encoded by the S100A11 gene. The protein encoded by ... "Entrez Gene: S100A11 S100 calcium binding protein A11". Kanamori T, Takakura K, Mandai M, Kariya M, Fukuhara K, Sakaguchi M, et ... October 2004). "Increased expression of calcium-binding protein S100 in human uterine smooth muscle tumours". Molecular Human ... rationale for a new nomenclature of the S100 calcium-binding protein family". Genomics. 25 (3): 638-43. doi:10.1016/0888-7543( ...
... is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in ... This protein differs from the other S100 proteins of known structure in its lack of calcium binding ability in one EF-hand at ... S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the S100A7 gene. ... "Calcium-binding protein S100A7 and epidermal-type fatty acid-binding protein are associated in the cytosol of human ...
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 ... S100 calcium-binding protein A13 (S100A13) is a protein that in humans is encoded by the S100A13 gene. ... "Entrez Gene: S100A13 S100 calcium binding protein A13". Mouta Carreira C, LaVallee TM, Tarantini F, Jackson A, Lathrop JT, ... rationale for a new nomenclature of the S100 calcium-binding protein family". Genomics. 25 (3): 638-43. doi:10.1016/0888-7543( ...
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 ... S100 calcium-binding protein A8 (S100A8) is a protein that in humans is encoded by the S100A8 gene. It is also known as ... "Entrez Gene: S100A8 S100 calcium binding protein A8". Ryan FJ, Hope CM, Masavuli MG, Lynn MA, Mekonnen ZA, Yeow AE, et al. ( ... Schäfer BW, Heizmann CW (April 1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends in ...
... is a member of the S100 family of proteins containing 2 EF hand calcium-binding motifs. S100 proteins are localized in ... S100 calcium-binding protein A9 (S100A9) also known as migration inhibitory factor-related protein 14 (MRP14) or calgranulin B ... "Entrez Gene: S100A9 S100 calcium binding protein A9". Vogl T, Tenbrock K, Ludwig S, Leukert N, Ehrhardt C, van Zoelen MA, ... Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem ...
... S100 calcium binding protein A3". Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: ... S100 calcium-binding protein A3 (S100A3) is a protein that in humans is encoded by the S100A3 gene. The protein encoded by this ... "Purification and cation binding properties of the recombinant human S100 calcium-binding protein A3, an EF-hand motif protein ... gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the ...
S100 calcium-binding protein A6 (S100A6) is a protein that in humans is encoded by the S100A6 gene. The protein encoded by this ... gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the ... "Entrez Gene: S100A6 S100 calcium binding protein A6". Deloulme JC, Assard N, Mbele GO, Mangin C, Kuwano R, Baudier J (November ... Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem ...
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. ... S100 calcium-binding protein A12 (S100A12) is a protein that in humans is encoded by the S100A12 gene. Human S100A12, also ... "Entrez Gene: S100A12 S100 calcium binding protein A12". Wicki R, Marenholz I, Mischke D, Schäfer BW, Heizmann CW (December 1996 ... rationale for a new nomenclature of the S100 calcium-binding protein family". Genomics. 25 (3): 638-43. doi:10.1016/0888-7543( ...
S100A4 has been shown to interact with S100 calcium binding protein A1. S100A4, a member of the S100 calcium-binding protein ... The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 ... "Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin". J. Cell Biol. 124 (5): 757-68. ... "Entrez Gene: S100A4 S100 calcium binding protein A4". Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, ...
... S100 calcium binding protein G". Balmain N (1991). "Calbindin-D9k. A vitamin-D-dependent, calcium-binding protein in ... a vitamin D-dependent calcium-binding protein. This cytosolic protein belongs to a family of calcium-binding proteins that ... S100 calcium-binding protein G (S100G) is a protein that in humans is encoded by the S100G gene. This gene encodes calbindin ... and S100 protein. In the intestine, the protein is vitamin D-dependent and its expression correlates with calcium transport ...
... is a member of the S100 family of proteins containing two EF-hand calcium-binding motifs. S100 proteins are localized ... S100 calcium-binding protein A10 (S100A10), also known as p11, is a protein that is encoded by the S100A10 gene in humans and ... Unlike other S-100 proteins, the second EF-hand of protein p11 is incapable of binding calcium due to a series of mutations ... "Entrez Gene: S100A10 S100 calcium binding protein A10". Rosack J (2006). "Protein Discovery May Lead To New Psychiatric Drugs ...
S100 calcium-binding protein B (S100B) is a protein of the S-100 protein family. S100 proteins are localized in the cytoplasm ... "Entrez Gene: S100B S100 calcium binding protein B". Verma N, Karmakar M, Singh KP, Smita S (February 2013). "Structural and ... Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem ... rationale for a new nomenclature of the S100 calcium-binding protein family". Genomics. 25 (3): 638-43. doi:10.1016/0888-7543( ...
... S100 calcium binding protein A5". Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: ... S100 calcium-binding protein A5 (S100A5) is a protein that in humans is encoded by the S100A5 gene. The protein encoded by this ... gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the ... This protein also binds Zn2+ and Cu2+, and Cu2+ strongly which impairs the binding of Ca2+. This protein is expressed in very ...
"Calcium regulation of Ndr protein kinase mediated by S100 calcium-binding proteins". EMBO J. 17 (20): 5913-22. doi:10.1093/ ... 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation ... protein kinase by the hMOB1 protein". J. Biol. Chem. 279 (34): 35228-35. doi:10.1074/jbc.M404542200. PMID 15197186. Jin J, ... Serine/threonine-protein kinase 38 is an enzyme that in humans is encoded by the STK38 gene. GRCh38: Ensembl release 89: ...
S100 calcium-binding protein P (S100P) is a protein that in humans is encoded by the S100P gene. The protein encoded by this ... gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the ... S100P S100 calcium binding protein P". Koltzscher M, Neumann C, König S, Gerke V (Jun 2003). "Ca2+-dependent binding and ... Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem ...
"Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin". The Journal of Cell Biology. 124 ... Guy PM, Kenny DA, Gill GN (Jun 1999). "The PDZ domain of the LIM protein enigma binds to beta-tropomyosin". Molecular Biology ... "Protein sequence of human TPM2 (Uniprot ID: P07951)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Retrieved 1 July ... "Protein sequence of human TPM2 (Uniprot ID: P07951-2)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Retrieved 1 ...
... is an S100 calcium-binding protein that is expressed in multiple cell types, including renal epithelial cells and ... The proteins S100A8 and S100A9 form a heterodimer called calprotectin. S100A8 (calgranulin A) S100A9 (calgranulin B) S100A12 ( ... Thus, it may also function in vivo as an inhibitor of calcium oxalate kidney stone formation. However, the role of calgranulin ... calgranulin C) Some in vitro evidence suggests that calgranulin can inhibit the precipitation of calcium oxalate in a urine- ...
Some EF-hand calcium binding proteins such as S100 or NCS-1 are also able to bind zinc ions. The U.S. Institute of Medicine ( ... The theoretical and computational description of this zinc binding in proteins (as well as that of other transition metals) is ... A review from 2015 indicated that about 10% of human proteins (~3000) bind zinc, in addition to hundreds more that transport ... The human dopamine transporter contains a high affinity extracellular zinc binding site which, upon zinc binding, inhibits ...
Some EF-hand calcium binding proteins such as S100 or NCS-1 are also able to bind zinc ions. The U.S. Institute of Medicine ( ... The theoretical and computational description of this zinc binding in proteins (as well as that of other transition metals) is ... A review from 2015 indicated that about 10% of human proteins (~3000) bind zinc, in addition to hundreds more that transport ... The human dopamine transporter contains a high affinity extracellular zinc binding site which, upon zinc binding, inhibits ...
PSCs can be attributed to glial lineage by the presence of Calcium binding proteins S100, Glial fibrillary acidic protein (GFAP ... The observed increase in Calcium seen above is possible due to PSCs protein receptors: ACh receptors, ATP Receptors, G-coupled ... Calcium levels in response to the "burst" pattern oscillated and the Calcium levels in response to the "continuous" pattern ... and Protein 0. These proteins are seen in other glial cells such as Myelinating Schwann cells and Neural Crest cells. While the ...
1997). "P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85 ... Underwood KW, Song C, Kriz RW, Chang XJ, Knopf JL, Lin LL (Sep 1998). "A novel calcium-independent phospholipase A2, cPLA2- ... "Entrez Gene: PLA2G4C phospholipase A2, group IVC (cytosolic, calcium-independent)". Schröder HC, Perovic S, Kavsan V, et al. ( ... 2006). "Caspase-3-dependent activation of calcium-independent phospholipase A2 enhances cell migration in non-apoptotic ovarian ...
The first marker protein discovered in FS cells was S-100b, which is a calcium-binding protein expressed by glial cells. Some ... glial fibrillary acidic protein), cytokeratin, vimentin and fibronectin. S-100 protein and GFAP expression seem to be strongest ... The protein Annexin A1 (ANXA1), found in high quantities in the anterior pituitary gland, is located specifically in the ... Experiments have been carried out to assess the protein markers they express, in order to determine their cell-type and thus ...
The S100 proteins are a family of low molecular-weight proteins found in vertebrates characterized by two calcium-binding sites ... S100 proteins are markers for inflammatory diseases and can mediate inflammation and act as antimicrobials. S100 proteins have ... and knockdown of aryl hydrocarbon receptor downregulates the expression of S100 proteins in THP-1 cells. Most S100 proteins ... S100 proteins have been implicated in a variety of intracellular and extracellular functions, such as regulation of protein ...
... is highly conserved across vertebrate evolution (NCBI database). It is a smaller calcium-binding protein (11.7-kDa ... which resembles the EF-hand domain of calmodulin (32% sequence identity), alpha-parvalbumin (54%), S100-beta (34%), and ... Oncomodulin is a parvalbumin-family calcium-binding protein expressed and secreted by macrophages (that typically traffic to ... It is small, acidic, has a high calcium-binding activity, and consists of 108 amino acid residues. It is released by ...
MATERIAL AND METHODS:Immunohistochemistry (IHC) was used to detect expression of the S100A8 protein in 74 tissue samples of ... RESULTS:IHC showed high levels of expression of S100A8 protein in endometrial carcinoma tissues, and HEC-1A adenocarcinoma ... S100A8 mRNA and S100A8 protein levels were detected by quantitative reverse transcription-polymerase chain reaction (qRT-PCR) ... down-regulation of the S100A8 gene induced cell apoptosis via inhibition of the phosphorylated or active form of protein kinase ...
The calcium binding protein S100β marks hedgehog-responsive resident vascular stem cells within vascular lesions ... ORCID: 0000-0002-5385-6502 (2021) The calcium binding protein S100β marks hedgehog-responsive resident vascular stem cells ... Using transgenic eGFP mice and genetic lineage tracing of S100β vSCs in vivo, we identified S100β/ Sca1 cells derived from a ... Both S100β and PTCH1 cells were present in human vessels while S100β cells were enriched in arteriosclerotic lesions. ...
Monoclonal Antibody to S100 Calcium Binding Protein (S100). MAA012Hu22 * $33600 $336.00 Unit price/ per ... TPBG/5T4: the Oncofetal Protein, an Appealing Target for ADC or Vaccine Therapeutics in Tumors! ... TPBG/5T4: the Oncofetal Protein, an Appealing Target for ADC or Vaccine Therapeutics in Tumors! ...
Mouse S100A10(S100 Calcium Binding Protein A10) ELISA Kit. Mouse S100A10(S100 Calcium Binding Protein A10) ELISA Kit ... Description: A sandwich ELISA kit for detection of S100 Calcium Binding Protein A10 from Mouse in samples from blood, serum, ... This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse S100 Calcium Binding Protein A10 ( ... This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse S100 Calcium Binding Protein A10 ( ...
S100 Calcium Binding Protein A5 (S100A5) Monoclonal Antibody, Cat#CAU29400. Rating Required Select Rating. 1 star (worst). 2 ... Title: Mycoplasma promotes malignant transformation in vivo, and its DnaK, a bacterial chaperone protein, has broad oncogenic ... S100 Calcium Binding Protein A5 (S100A5) Monoclonal Antibody, Cat#CAU29400 Browse by Categories, Price, Brand and more... Show ...
... Shipped on dry ice. Store product at -20°C ... Recombinant Human S100 Calcium Binding Protein S100A8/S100A9 Heterodimer (C-His). Essential Extras. ...
The significance of serum S100 calcium-binding protein A4 in silicosis *Jing Zhang ...
Protein S100-A1, also known as S100 calcium-binding protein A1 is a protein which in humans is encoded by the S100A1 gene. ... "Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), ... Donato R (July 1999). "Functional roles of S100 proteins, calcium-binding proteins of the EF-hand type". Biochimica et ... "Entrez Gene: S100A1 S100 calcium binding protein A1". Morii K, Tanaka R, Takahashi Y, Minoshima S, Fukuyama R, Shimizu N, ...
S100 Calcium Binding Protein G / analysis * S100 Calcium Binding Protein G / immunology ... Results showed that all GABAergic-amacrines and displaced amacrines express the R2A-subunit protein. In addition, approximately ... both R2A and R2B receptor subunits are localized to cone outer segments suggests a possible alternative pathway for calcium ...
205863_at S100 calcium binding protein A12 0.002. 205603_s_at Diaphanous homolog 2 (Drosophila) 0.003 ... Protein-protein interactions are central to all cellular processes. Understanding of protein-protein interactions is therefore ... do not target the disease protein but a protein which is 2 or 3 steps away from the disease protein in the Protein-Protein ... The protein-protein interaction of these non-essential genes revealed. vital information regarding interacting proteins. Funct ...
S100 calcium-binding protein A10), immunoglobulin heavy constant Mu (IGHM) and CD4-1 [126]. The non-psychoactive component of ... by binding to equilibrative nucleoside transporter-1); inhibition ofG-protein coupled receptor 55 (GPR55); and the stimulation ... CBD belongs to the cannabinoid family and is a non-psychoactive compound that binds to specific G-protein-coupled receptors [77 ... Showalter, V.M.; Compton, D.R.; Martin, B.R.; Abood, M.E. Evaluation of binding in a transfected cell line expressing a ...
S100 calcium-binding protein B (S100B), and C-reactive protein (CRP). Results: Sixty-six randomized patients (n = 33 per group ...
Rat S100A9 (S100 Calcium Binding Protein A9) ELISA Kit , G-EC-05967 ... Rat IGFBP-3 (Insulin-Like Growth Factor Binding Protein 3) ELISA Kit , G-EC-06007 ... Rat FABP1 (Fatty Acid Binding Protein 1, Liver) ELISA Kit , G-EC-06023 ... Rabbit TGFβI (Transforming Growth Factor Beta Induced Protein) ELISA Kit , G-EC-06049 ...
Mouse S100A9 (S100 Calcium Binding Protein A9) CLIA Kit , G-EC-01707 Mouse S100A9 (S100 Calcium Binding Protein A9) CLIA Kit , ... Mouse S100A8 (S100 Calcium Binding Protein A8) CLIA Kit , G-EC-01706 Mouse S100A8 (S100 Calcium Binding Protein A8) CLIA Kit , ... Mouse S100A10 (S100 Calcium-binding Protein A10) CLIA Kit , G-EC-01708 Mouse S100A10 (S100 Calcium-binding Protein A10) CLIA ... Mouse S100A10 (S100 Calcium-binding Protein A10) CLIA Kit , G-EC-01708 ...
All astrocytes expressed functional markers including glial fibrillary acidic protein (GFAP), excitatory amino acid transporter ... κ for S100 calcium-binding protein B (S100B; 1:100; Sigma), rabbit polyclonal IgG antiserum for the excitatory amino acid ... Fixed cells were permeabilised by incubation in 0.1% (w/v) Triton X-100 in PBS for 5 min and blocking of nonspecific binding ... Revett TJ, Baker GB, Jhamandas J, Kar S . Glutamate system, amyloid β peptides and tau protein: functional interrelationships ...
The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 ... Upregulated genes include calcium-binding S100 proteins such as S100A9, S100A10, S100A6, and S100A13, and granzymes B and C. ... PURPOSE: Altered level of S100 calcium-binding proteins is involved in tumor development and progression. However, their role ... Annexin A2, a calcium phospholipid binding protein, has been shown to play an important role in ovarian cancer metastasis. This ...
S100 calcium binding protein B. ISO. protein:increased expression:cerebral cortex, hippocampus, astrocyte. RGD. PMID:20002528. ... TATA-box binding protein. ISO. associated with Sudden Infant Death; protein:altered expression:brainstem (human). RGD. PMID: ... surfactant protein B. ISO. protein:decreased expression:serum:. RGD. PMID:25953386. RGD:151667446. NCBI chrNW_004955424: ... protein:increased expression:plasma (rat). protein:decreased expression:serum. RGD. PMID:19342292 PMID:20040038. RGD:4142829 ...
Phagocyte-specific calcium-binding S100 proteins as clinical laboratory markers of inflammation. Clin Chim Acta. June 2004. 344 ... Patients with low protein levels in ascitic fluid (, 1 g/dL) have a 10-fold higher risk of developing spontaneous bacterial ... Phagocyte-specific S100A8/A9 protein levels during disease exacerbations and infections in systemic lupus erythematosus. J ... Correlation between faecal excretion of indium-111-labelled granulocytes and calprotectin, a granulocyte marker protein, in ...
S100 calcium-binding protein A4. ISO. CTD Direct Evidence: marker/mechanism. CTD. PMID:30818366. NCBI chr 2:176,090,951... ... Protein-Protein Interactions) PhenoMiner (Quatitative Phenotypes) Gene Annotator OLGA (Gene List Generator) AllianceMine ... homeodomain interacting protein kinase 2. ISO. CTD Direct Evidence: marker/mechanism. CTD. PMID:28318631. NCBI chr 4:67,439,327 ... protein:increased expression:nephron tubule, kidney interstitium (human). RGD. PMID:10580398 PMID:21346373. RGD:12879397, RGD: ...
S100 calcium-binding protein A2 NM_005978.2 0.281 calpain Calcium-activated neutral protease large subunit X04366.1 0.262 ... pRB-binding protein M96577.1 0.483 SKP1A S-phase kinase-associated protein 1A (p19A; SKP1A), transcript variant 1 NM_006930.2 ... pRB-binding protein M96577.1 0.483 SKP1A S-phase kinase-associated protein 1A (p19A; SKP1A), transcript variant 1 NM_006930.2 ... The protein p53 binding to the MGMT promoter element was examined. Lane 1, PCR amplification of MGMT and GAPDH sequences in ...
Schafer, B, Heizmann, C. The S100 family of EF-hand calcium-binding proteins: functions and pathology. Trends Biochem Sci 1996 ... The S100/calgranulins constitute a family of closely related calcium-binding polypeptides containing two EF-hand regions, ... We propose that RAGE-S100 interaction provides a novel costimulatory axis in which aggregates of S100 proteins bridge and ... Enhanced cellular oxidant stress by the interaction of AGEs with their receptors/binding proteins. J Biol Chem 1994. 269:9889- ...
S100 calcium-binding protein A6 (calcyclin) ENST00000292162 6277 May function in stimulation of Ca2+-dependent insulin release ... S100 calcium-binding protein A6 (calcyclin) ENST00000292162 6277 May function in stimulation of Ca2+-dependent insulin release ... Protein degradation 12q24.31 Yes B and C RPS13 f Ribosomal protein S13 NM_001017.2 6207 Encodes a ribosomal protein that is a ... Protein degradation 12q24.31 Yes B and C RPS13 f Ribosomal protein S13 NM_001017.2 6207 Encodes a ribosomal protein that is a ...
Implementation of the S100 Calcium-Binding Protein B Biomarker in a Clinical Setting: A Retrospective Study of Benefits, Safety ...
2021). S100 calcium-binding protein A9 from tumor-associated macrophage enhances cancer stem cell-like properties of ... Protein samples from tumors derived SORE6± cells were extracted using the mammalian protein extraction reagent M-Per (Promega, ... were used to detect individual protein expression. Western blot imaging system was used for testing individual protein ... Additionally, total protein lysates of tumors derived from SORE6± cells were extracted and processed for GFP positivity via ...
The calciumbinding, vertebrate‐specific S100 protein family consists of 20 paralogs in humans (referred as the S100ome), with ... The calcium-binding, vertebrate-specific S100 protein family consists of 20 paralogs in humans (referred as the S100ome), with ... is a vital globular transport protein with potential multiple ligand binding sites. Characterizing the binding affinity of ... High throughput competitive fluorescence polarization assay reveals functional redundancy in the S100 protein family ...
S100A7/Psoriasin fusion protein Ag3738 Full Name. S100 calcium binding protein A7. ... It is an EF-hand type calcium binding protein localized in epithelial cells, regulates cell proliferation and differentiation. ... S100A7 (psoriasin), a member of the S100 protein family, is a well-known antimicrobial peptide and a signaling molecule which ... Differentially expressed proteins identified by TMT proteomics analysis in children with verrucous epidermal naevi.. Authors - ...
Protein S100-A9; S100 A9; S100 calcium-binding protein A9; S100 calcium-binding protein A9 (calgranulin B) ... calcium ion binding protein binding microtubule binding zinc ion binding antioxidant activity Toll-like receptor 4 binding ... S100A9 (MRP-14) is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are ... S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in the ...
Recombinant Human S100A6 protein, His-SUMO-tagged can be used for research. ... Purified Recombinant Human S100A6 protein, His-SUMO-tagged from Creative Biomart. ... S100A6; S100 calcium binding protein A6; CACY, S100 calcium binding protein A6 (calcyclin) , S100 calcium binding protein A6 ( ... growth factor-inducible protein 2A9; prolactin receptor-associated protein; S100 calcium-binding protein A6 (calcyclin); 5B10; ...
  • The aim of this study was to investigate the expression and silencing of the S100A8 gene, which encodes the S100 calcium-binding protein A8 (S100A8), and apoptosis and phosphorylation of protein kinase B (Akt) in tissue samples of endometrial carcinoma and HEC-1A endometrial adenocarcinoma cells in vitro . (medscimonit.com)
  • Immunohistochemistry (IHC) was used to detect expression of the S100A8 protein in 74 tissue samples of endometrial cancer and 22 normal endometrial tissue samples. (medscimonit.com)
  • S100A8 mRNA and S100A8 protein levels were detected by quantitative reverse transcription-polymerase chain reaction (qRT-PCR) and Western blotting. (medscimonit.com)
  • Enzyme-linked immunosorbent assays (ELISAs) were used to determine the serum concentrations of the S100A8, S100A9, and IL-6 proteins. (scielo.br)
  • The proteins S100A8 and S100A9 form a heterodimer called calprotectin . (wn.com)
  • Further studies demonstrated that MitoTEMPO administration suppressed the mRNA and protein expressions of MDSC-associated proinflammatory mediators, such as monocyte chemoattractant protein-1 (MCP-1), S100 calcium-binding protein A8 (S100A8), and S100 calcium-binding protein A9 (S100A9). (hindawi.com)
  • Full length human recombinant protein of human S100A9 produced in SF9 cell. (thermofisher.com)
  • Results showed that all GABAergic-amacrines and displaced amacrines express the R2A-subunit protein. (nih.gov)
  • Another protein, calgranulin A (Cal A), is involved in the regulation of several cell processes, including the cell cycle and cell differentiation. (bvsalud.org)
  • Description: A sandwich ELISA kit for detection of S100 Calcium Binding Protein A10 from Mouse in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (novosides.eu)
  • This Human S100A1 ELISA Kit was designed for the quantitative measurement of Human S100A1 protein in serum, plasma, tissue homogenates. (cusabio.com)
  • The primary focus of Rajnarayanan's research team is to design and develop molecules that target functionally relevant protein interactions and molecular solutions to understand protein circuitry in the endocrine and the neuroendocrine system. (nyit.edu)
  • Lee, D.H., Asare, B.K. and Rajnarayanan, R.V. (2016) "Discovery at the Interface: Towards Novel Anti-Proliferative Agents Targeting Human Estrogen Receptor\S100 Interactions. (nyit.edu)
  • These changes allow interactions with specific target proteins and modulate their activity. (cusabio.com)
  • The knowledge of interactions between proteins in crowded mixtures, as they exist in the interior of living cells, is essential since they ultimately determine their stability, phase behavior, solution structure and dynamics. (lu.se)
  • As a first step on our way to establish a well-defined model cytosol with a complete experimental description of the effective interactions and the resulting solution structure and thermodynamic stability, we need to identify individual proteins that differ in size and charge and are suitable components for our generic cell cytosol. (lu.se)
  • We investigate the solution structure of calbindin D 9k using SAXS and quantify the protein-protein interactions through second virial coefficients as a function of the calcium binding state (holo and apo) and the screening conditions, both experimentally and via Monte Carlo computer simulations. (lu.se)
  • The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. (cancerindex.org)
  • In intestinal ENTEROCYTES it mediates intracellular calcium transport from apical to basolateral membranes via calcium binding at two EF-HAND MOTIFS. (bvsalud.org)
  • Moreover, real-time quantitative PCR, western blot, and immunohistochemistry were conducted to detect the mRNA and protein expressions in the liver tissues. (hindawi.com)
  • This is the first study describing the production and distribution of ETS-1 and ETS-2 mRNAs and proteins using in situ hybridization and immunohistochemistry in murine ocular tissue sections of normal control eyes and tumoral eyes from mice of the same age. (molvis.org)
  • Material and Methods: In this study, immunohistochemistry (IHC) was performed to identify the prognostic role of S100A2 protein expression in the tumour core of the tissue microarrays (TMAs) in colorectal cancer patients (n=787). (gla.ac.uk)
  • Astrocytes may be recognized as such by their expression of glial fibrillary acidic protein, glutamine synthetase, glutamate transporter 1 (GLT1), aquaporin-4, aldehyde dehydrogenase 1 family member L1, and other proteins. (jneurosci.org)
  • Through virtual models, his 2004 study centered on the potential for old drugs to target the coronavirus's main enzyme catalyzing the breakdown of proteins into smaller polypeptides or single amino acids, an essential process for the propagation of the coronaviral life cycle. (nyit.edu)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse S100 Calcium Binding Protein A10 (S100A10) in serum, plasma, tissue homogenates, cell lysates and other biological fluids. (novosides.eu)
  • In the blood vascular system, human serum albumin (HSA) is a vital globular transport protein with potential multiple ligand binding sites. (researchgate.net)
  • Objective -To measure serum calprotectin concentration in dogs with inflammatory bowel disease (IBD) before and after initiation of treatment and evaluate its correlation with a clinical scoring system (canine IBD activity index), serum canine C-reactive protein concentration, and severity of histopathologic changes. (avma.org)
  • Results -Mean serum calprotectin concentrations for dogs with IBD at baseline (431.1 μg/L) and 3 weeks after initiation of treatment (676.9 μg/L) were significantly higher, compared with that (219.4 μg/L) for control dogs, and were not significantly correlated with the canine IBD activity index, serum C-reactive protein concentration, or severity of histopathologic changes. (avma.org)
  • The objective of this proof of principle study was to evaluate a variety of patient variables, along with six brain-specific and inflammatory serum protein biomarkers, as predictors of long-term cognitive outcome following paediatric TBI. (biomedcentral.com)
  • Secondary outcomes evaluated stress and inflammatory indices using the Perceived Stress Scale (PSS), S100 calcium-binding protein B (S100B), and C-reactive protein (CRP). (nih.gov)
  • T he immune-inflammatory dysregulation theory in schizophrenia 1 , 2 posits an imbalance of pro- and anti-inflammatory cytokines and elevated levels of inflammatory proteins (eg, C-reactive protein, S100 calcium-binding protein B [S100B], and prostaglandin E2) in subgroups of patients with schizophrenia experiencing an exacerbation of symptoms. (psychiatrist.com)
  • and identifying EF hand protein S100 as a non-classical interactor of estrogen receptors. (nyit.edu)
  • This protein may function in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis. (thermofisher.com)
  • The differentiation-induced psoriasin expression was found to be mediated by the protein kinase C pathway. (medicaljournals.se)
  • The various markers that enable assessment of the progression of preneoplastic lesions to spindle cell carcinoma include the p16 protein, which halts the cell cycle and induces apoptosis by pRb-mediated phosphorylation of cyclin-dependent kinase 4 (CDK4). (bvsalud.org)
  • In vitro, S100β/Sca1 cells isolated from atheroprone regions of the mouse aorta expressed hedgehog signalling components, acquired the di-methylation of histone 3 lysine 4 (H3K4me2) stable SMC epigenetic mark at the Myh11 locus and underwent myogenic differentiation in response to recombinant sonic hedgehog (SHh). (dcu.ie)
  • Recombinant SHh promoted myogenic differentiation of human induced pluripotent stem cell-derived S100β neuroectoderm progenitors in vitro. (dcu.ie)
  • S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. (cancerindex.org)
  • Exhibiting high consistence in sequence and structure, S100 family members are interchangeable in function and they show a wide spectrum of biological processes, including proliferation, apoptosis, migration, inflammation and differentiation and the like. (cancerindex.org)
  • Estrogens are important regulators of growth and differentiation in (range, 0 -9 fmol/mg protein, median 0.7). (lu.se)
  • Cystatin A (Cys A), a cysteine protease inhibitor, is a precursor of proteins involves in keratinocyte keratinization, and is expressed during the late phase of differentiation of these cells. (bvsalud.org)
  • Intracellular psoriasin has been found to interact with various signalling proteins, including the nuclear factor (NF)-kB regulator Jab1, while secreted psoriasin functions as an antimicrobial peptide and has the ability to induce chemotaxis of neutrophils and T cells (6). (medicaljournals.se)
  • We have shown previously that extracellular psoriasin binds to the receptor for advanced glycation end products (RAGE), promoting endothelial cell proliferation (8). (medicaljournals.se)
  • In the liver of obesity, the resident immune cells such as macrophages (Kupffer cells) and dendritic cells produce proinflammatory chemokines and cytokines, including monocyte chemoattractant protein-1 (MCP-1), interleukin-1 β (IL-1 β ), and tumor necrosis factor- α (TNF- α ) in response to hepatocellular damage [ 10 - 12 ]. (hindawi.com)
  • S100 calcium-binding protein A5 ( S100A5 ) is a protein that in humans is encoded by the S100A5 gene . (wn.com)
  • ETS-1 and ETS-2 mRNA and protein levels were much higher in the ocular tissues of Tyrp-1-TAg mice than in control ocular tissues from wild-type mice. (molvis.org)
  • Using transgenic eGFP mice and genetic lineage tracing of S100β vSCs in vivo, we identified S100β/ Sca1 cells derived from a S100β non-SMC parent population within lesions that co-localise with smooth muscle α-actin (SMA) cells following iatrogenic flow restriction, an effect attenuated following hedgehog inhibition with the smoothened inhibitor, cyclopamine. (dcu.ie)
  • Prognostic values of S100 family members in ovarian cancer patients. (cancerindex.org)
  • While the prognostic value of each individual S100 in ovarian cancer is still elusive. (cancerindex.org)
  • In current study, we investigated the prognostic value of S100 family members in the ovarian cancer. (cancerindex.org)
  • S100 calcium-binding protein A2 (S100A2) has been purposed as a potential marker in many types of cancer, however, the prognostic value of S100A2 in CRC is rarely reported. (gla.ac.uk)
  • This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling. (abcam.com)
  • This protein may function in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. (microarraystation.com)
  • Although the function of these receptor subunits in rod and cone photoreceptors remains to be determined, the fact that both R2A and R2B receptor subunits are localized to cone outer segments suggests a possible alternative pathway for calcium entry into a region where this cation plays such a crucial role in the process of phototransduction. (nih.gov)
  • Binding of these ligands to RAGE does not accelerate clearance or degradation but rather begins a sustained period of cellular activation mediated by receptor-dependent signaling. (jci.org)
  • Immature calcium handling in immature myocardium raises intracellular calcium concentrations after ischemia and reperfusion. (medscape.com)
  • Characterizing the binding affinity of compounds to HSA is ess. (researchgate.net)
  • This protein has a Ca 2+ affinity 20- to 100-fold higher than the other S100 proteins studied under identical conditions. (wn.com)
  • Both S100β and PTCH1 cells were present in human vessels while S100β cells were enriched in arteriosclerotic lesions. (dcu.ie)
  • S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. (cancerindex.org)
  • Dogs with CE and protein-losing enteropathy had the greatest number of differentially expressed genes. (avma.org)
  • What does this gene/protein do? (cancerindex.org)
  • Using semi-quantitative reverse-transcription polymerase chain reaction (RT-PCR) and western blots experiments, we compared changes in ETS-1 and ETS-2 expression, their protein levels, and the regulation of some of their target gene expressions at different stages of the ocular tumoral progression in the transgenic mouse model, Tyrp-1-TAg, with those in normal eyes from control mice of the same age. (molvis.org)
  • 4. Kessel C, Holzinger D, Foell D. Phagocyte-derived S100 proteins in autoinflammation: putative role in pathogenesis and usefulness as biomarkers. (scielo.br)
  • Foell D, Roth J. Proinflammatory S100 proteins in arthritis and autoimmune disease. (scielo.br)
  • Finally, the activity of Na + /K + adenosine triphosphatase (ATPase) increases with maturation, and this affects the sodium-calcium exchange mechanism. (medscape.com)
  • Scope includes mutations and abnormal protein expression. (cancerindex.org)
  • By means of oligonucleotide microarray and RNA interference, we reveal that the sensitizing effect of IFN-β was possibly due to attenuation of MGMT expression via induction of the protein p53. (aacrjournals.org)
  • Subsequently, Ca 2+ that is bound to calbindin-D 28K is shuttled toward the basolateral Ca 2+ extrusion systems. (researchwithrutgers.com)
  • The amount of sarcoplasmic reticulum and its ability to sequester calcium similarly increase in early development. (medscape.com)
  • One potential candidate is calbindin D 9k, a monomeric calcium-binding protein of the S100 family of the calmodulin-related proteins, involved in Ca 2+ buffering and in trans-cellular transport of Ca 2+ ions. (lu.se)
  • The p63 protein, a homologue of p53, may be associated with tumor formation in the epithelial tissue, acting as an oncogene 11,12 . (bvsalud.org)
  • and amphoterin, a nuclear protein sometimes found in the ECM (Table 1 ). (jci.org)
  • However, these proteins may all be regulated both developmentally and functionally, restricting their utility. (jneurosci.org)
  • Rajnarayanan's team has developed human computer interface (HCI) devices using 3-D printed protein models to generate functionally relevant clusters of simulated structural interactomics data to accelerate compound discovery. (nyit.edu)
  • The DNA repair protein O 6 -methylguanine-DNA methyltransferase (MGMT) plays an important role in cellular resistance to alkylating agents. (aacrjournals.org)
  • A cellular DNA-repair protein, namely O 6 -methylguanine-DNA methyltransferase (MGMT) protein, reverses alkylation at the O 6 position of guanine, thereby inhibiting the lethal cross-linking and bringing about resistance to alkylating agents ( 2, 3 ). (aacrjournals.org)
  • In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers conformational changes. (cusabio.com)
  • As a consequence, the effects of hemodilution are markedly enhanced in neonates compared with adults, as evidenced by decreased levels of plasma protein, coagulation factors, and hemoglobin. (medscape.com)
  • Conclusion: p63, p16, MIB, Cal A, Cys A are markedly expressed and p16 is strongly suppressed in oral cavity tumors, which suggests that the latter protein may play a role in negative regulation of cell cycle progression. (bvsalud.org)
  • Small calcium binding protein that plays important roles in several biological processes such as Ca(2+) homeostasis, chondrocyte biology and cardiomyocyte regulation. (cusabio.com)
  • A subtype of S100 calcium binding protein G that plays a fundamental role in the VITAMIN D-mediated transport of calcium in reptiles, amphibians, birds and mammals. (bvsalud.org)
  • 1977. Metabolism of halogenated methanes and macromolecular binding. (cdc.gov)