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Platelet-derived growth factors (PDGFs) have been implicated in the control of cell proliferation, survival and migration. The PDGF family of growth factors consists of five different disulphide-linked dimers built up of four different polypeptide chains encoded by four different genes. Theses isoforms, PDGF-AA, PDGF-AB, PDGF-BB, PDGF-CC and PDGF-DD, act via two receptor tyrosine kinases, PDGF receptors α and β. Thus far, gene-targeting experiments have been attempted to create knockout mice deficient for PDGFR-α or PDGFR-β. Those mice, however, died either at the embryonic stage or several days after birth. Platelet-derived growth factor receptors, PDGFR-α and PDGFR-β, have five extracellular immunoglobulin-like domains and an intracellular tyrosine kinase domain. Upon binding a PDGF, the receptors form homo- and heterodimers. Dimerization of the receptors juxtaposes the intracellular part of the receptors, which allow phosphorylation in trans between the two receptors in the complex. These autophosphorylation provide docking sites for downstream signal transduction molecules. More than 10 different SH2–domain-containing molecules have been shown to bind to different autophosphorylation sites in the PDGF α- and β-receptors. There are signal transduction molecules with enzymatic activity, such as PI3-kinase, PLC-γ, Src, SHP-2, GAP, as well as adaptor molecules such as Grb2, Shc, Nck, Grb7 and Crk, and Stats. Each of the different partners recruited by the activated receptor initiates different signaling pathways, making possible a great variety of cellular response.

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Ataxia telangiectasia mutated (ATM) is a serine/threonine-specific protein kinase that is activated by DNA double-strand breaks. It phosphorylates several key proteins that initiate activation of the DNA damage checkpoint, leading to cell cycle arrest, DNA repair or apoptosis. Several of these targets are p53, CHK2, BRCA1, and H2AX.
ATM triggers the G1/S checkpoint; ATR (Ataxia telangiectasia and Rad3-related) prevents G1/S stasis. In this single point in the cell cycle, it would appear that ATM and ATR function in opposition to one another.
Ataxia telangiectasia (AT) is a rare neurodegenerative, autosomal recessive disorder characterized by chromosome instability, radiosensitivity, immunodeficiency and a predisposition for cancer.
The ATR (ATM and Rad3-related) kinase and its downstream effector kinase, Chk1, are central regulators of the replication checkpoint. Loss of these checkpoint proteins causes replication fork collapse and chromosomal rearrangements. ATR are thought to be master controllers of cell cycle checkpoint signaling pathways that are required for cell response to DNA damage and for genome stability.

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Fibronectin (FN) exists in two main forms: 1) as a soluble glycoprotein in blood plasma (plasma FN), and 2) as an insoluble glycoprotein in tissue extracellular matrices (cellular FN). Many different cell types synthesize fibronectin and secrete it as a disulfide-bonded dimer composed of 230–270 kDa subunits. FN is one of the largest multi-domain proteins that interact with a variety of macromolecules like heparin, collagen /gelatin, and fibrin. FN is involved in many cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/ adhesion and so can be used as a therapeutic agent for wound healing. In addition, its age-dependent increase in plasma and tissues may be accompanied in pathological states, especially in tumor growth, by its proteolytic breakdown.

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α-fetoprotein (AFP) is a glycoprotein of 590 amino acids containing 3.4% carbohydrate content with a molecular weight of 61,000 – 75,000 Da. AFP is normally produced in the developing embryo and fetus by the fetal yolk sac, the fetal gastrointestinal tract, and eventually by the fetal liver. In humans, AFP levels decrease gradually after birth, reaching adult levels by 8 to 12 months. Normal adult AFP levels are low and AFP has no known function in normal adults.
The biologic role of AFP has not been defined yet. Because of its biochemical similarity to albumin, it has been postulated that AFP could be a carrier protein. It may have an immunoregulatory function during pregnancy.
Increased serum levels are found in some tumors, such as hepatocellular
carcinoma (HCC), hepatoblastoma, and germ cell tumors. Although total AFP is a useful serological marker for diagnosis of HCC, the false-negative or positive rate with AFP level is very high. AFP-L3, an isoform of AFP which binds Lens culinaris agglutinin, can be particularly useful in early identification of aggressive tumors associated with HCC. AFP mRNA, the circulating genetic markers, also has been used in monitoring distal metastasis or postoperative recurrence of HCC.

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14-3-3, a family of acidic and soluble proteins, highly conserved in amino acid sequences from yeast to mammals, is expressed in all eukaryotic cells. Seven isoforms(β, γ, ε, η, ζ, σ and τ/θ) encoded by seven distinct genes are identified in mammals and forms homo- and hetero- dimeric cup-shaped structures. As 14-3-3 is interacted with more than 100 binding partners, it regulates key proteins involved in various biological processes such as signal trans-duction, cell cycle, transcriptional control, cell proliferation, apoptosis, and ion channel physiology. Most 14-3-3 requires phosphorylation of serine or threonine residues in the target sequence. This protein is abundantly expressed in the brain and has been detected in the cerebrospinal fluid of patients with different neurological disorders.

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Cyclin-dependent kinase-5 (CDK5) is a member of the cyclin-dependent kinase family of serine/threonine kinases. Its mRNA and protein are expressed in kidney, testes, and ovary. And Its activity is detected almost exclusively in brain extracts.
Similar to other Cdks, monomeric Cdk5 displays no enzymatic activity, but Cdk5 is not activated by cyclins. Instead, Cdk5 activity requires association with one of two brain-specific regulatory subunits called p35 and p39. The two activators regulate the spatial and temporal expression of active Cdk5 to restrict its activity primarily to post-mitotic neurons.

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The human Catecholamine-Sulfating Phenol Sulfotransferase (CSPS) is the only sulfotransferase that catalyses the sulfation of catecholamins, in particular the neurotransmitter dopamine, with high activity. CSPS is required for stimulation by Mn2+ of the sulfating activity and expressed in the human intestine, brain, platelet and other tissues. In the brain it may play a role in regulating the levels of dopamine. It also serves as a detoxifying function in the intestine, where it may detoxify potentially lethal dietary monoamines.

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The complement system is a part of the larger immune system and three biochemical pathways are present: the classical complement pathway, the alternative pathway, and the mannose-binding lectin pathway.
Human complement factor C6 is one of five components (C5b, C6, C7, C8, and C9) that interact to form the cytolytic membrane attack complex (MAC) which is the cytolytic end product of the complement cascade. MAC is typically formed on the surface of intruding pathogenic bacterial as a result of the activation of the complement system, and it is one of the ultimate weapons of the immune system.
The sixth component of complement, C6, is a 913 amino acid single polypeptide chain serum glycoprotein. Homology study suggests that C6 could contain two domains, an amino-terminal region that is related to complement C8 and C9, and a carboxyl-terminal region that has partial homology to the complement regulatory proteins factor H and factor I.
Genetic deficiencies of terminal complement components lead to markedly increased susceptibility to only one particular Gram-negative genus, the Neisseria. The susceptibility is attributable to the major role played by complement-mediated killing in host defense against the pathogen.

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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a catalytic enzyme commonly known to be involved in glycolysis. The enzyme exists as a tetramer of identical 37 kDa subunits. GAPDH catalyzes the reversible reduction of 1,3-bisphos-phoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Apart from playing a key role in glycolysis, this ubiquitously expressed enzyme also displays other activities unrelated to its glycolytic function. GAPDH is reported to be involved in the processes of DNA replication (1), DNA repair (2), nuclear RNA export (3-4), membrane fusion (5) and microtubule bundling. Other studies also provide evidence of GAPDH playing an essential part of the program of gene expression observed in apoptosis and as part of the cellular phenotype of age-related neurodegenerative diseases (6-7).

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There are ten mitogen-activated protein kinase (MAPK) phosphatases (MKPs) that act as negative regulators of MAPK activity in mammalian cells.
MKP2(DUSP4) is a dual threonine/tyrosine phosphatase that specifically dephosphorylates and inactivates MAPKs(ERK, JNK, p38). It contains one Rhodanese domain and one tyrosine-protein phosphatase domain.
MKP2 is expressed in a variety of tissues, and is localized in the nucleus.
Transcription factor E2F-1 acts as a transcriptional regulator of MKP2. E2F-1/MKP2 pathway mediates apoptosis under oxidative stress and that MKP2 suppresses tumor formation.
MKP2 is a novel transcription target of p53 in mediating apoptosis by 10-bp palindrome motif (CTGGCGCCAG) in the MKP2 promoter.

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The inter-α-trypsin inhibitor (ITI, IαI) family, a typical and classical example for protein-glycosaminoglycan-protein (PGP) complexes, occurs constitutively in plasma at relatively high concentrations and is a result of alternate combinations of three kinds of heavy chains with a common light chain, the bikunin proteoglycan. Bikunin has two proteinase inhibitor domains and belongs to the Kunitz-type protease inhibitor family; it displays an inhibitory activity against trypsin, leukocyte elastase and plasmin. The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid and this binding promotes the stability of the extra-cellular matrix. The ITI protein family is suspected of playing a key role in the extra-cellular matrix biology.

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NF-κB (Nuclear Factor kappa B) is a nuclear transcription factor found in all cell types and is involved in cellular responses to stimuli such as stress, cytokines, free radicals, ultraviolet irradiation, and bacterial or viral antigens. NF-κB plays a key role in regulating the immune response to infection. Consistent with this role, incorrect regulation of NF-κB has been linked to cancer, inflammatory and autoimmune diseases, septic shock, viral infection and improper immune development. There are five members in the NF-κB family: NF-κB1, NF-κB2, RelA (also named p65), RelB, and c-Rel. The RelB protein is present in the cytosol, bound to p50 or p52 and an inhibitory IκB protein, forming an inactive trimeric complex. Following cell signalling events leading to IκB degradation, Rel/NFκ-B proteins are translocated to the nucleus where they regulate gene expression. The genes controlled by Rel/NF-κB family members are predominantly genes involved in the host response to infection, stress and injury. RelB mediates the regulation of genes involved in immune and inflammatory processes.

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Catalase is a homotetrameric heme-containing enzyme present within the matrix of all peroxisomes. It carries out a dismutation reaction in which hydrogen peroxide is converted to water and oxygen. Human catalase has the last four amino acids (-KANL) at the extreme C-terminus for peroxisome targeting. The monomer of human catalase is 61.3 kD in molecular size. Catalase has been implicated as an important factor in inflammation, mutagenesis, prevention of apoptosis, and stimulation of a wide spectrum of tumors. Loss of catalase leads to the human genetic disease, acatalasemia, or Takahara’s disease (1).

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The complement system is a part of the larger immune system and three biochemical pathways are present: the classical complement pathway, the alternative pathway, and the mannose-binding lectin pathway.
Complement component C4 is an essential component of humoral immune response. In its activated form, C4b becomes a subunit of the C3 convertase, which is an enzymatic complex that activates C3 of the classical and lectin complement activation pathways. The classical pathway is initiated by the activation of the C1-complex (C1q, C1r and C1s) by C1q's binding to antibody-antigen. The C1-complex now binds to and splits C2 and C4 producing C2a and C4b. C4b and C2a bind to form C3-convertase. Production of C3-convertase leads to cleavage of C3 into C3a and C3b and C3b joins with the C3 convertase to make C5 convertase.
Human C4 is the most polymorphic protein of the complement system. Complement C4 exists as two isotypes, C4A (acidic) and C4B (basic). Although the sequence identity is very high, they have different hemolytic activities, covalent affinities to antigens and immune complexes, and serological reactivities. Each C4 contains β chain, α chain, C4a anaphyltoxin, C4b, and γ chain.
C4-deficient mice shows incomplete clearance of microbial attack and C4-deficiency in human shows increased autoimmune diseases.

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Anti-Peroxiredoxin 5 Rabbit Polyclonal Antibody

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Dual specificity phosphatase 13(Also known as BEDP; MDSP; TMDP; SKRP4; DUSP13A; DUSP13B) is an enzyme that in humans is encoded by the DUSP13 gene.[1]
Members of the protein tyrosine phosphatase superfamily cooperate with protein kinases to regulate cell proliferation and differentiation. This superfamily is separated into two families based on the substrate that is dephosphorylated. One family, the dual specificity phosphatases (DSPs) acts on both phosphotyrosine and phosphoserine/threonine residues. This gene encodes different but related DSP proteins through the use of non-overlapping open reading frames, alternate splicing, and presumed different transcription promoters. Expression of the distinct proteins from this gene has been found to be tissue specific and the proteins may be involved in postnatal development of specific tissues. A protein encoded by the upstream ORF was found in skeletal muscle, whereas the encoded protein from the downstream ORF was found only in testis. In mouse, a similar pattern of expression was found. Multiple alternatively spliced transcript variants were described, but the full-length sequence of only some were determined.[1]

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PTEN acts as a phosphatase to dephosphorylate phosphatidylinositol (3,4,5)-trisphosphate (PtdIns (3,4,5)P3). The product of this enzymatic reaction is PtdIns(4,5)P2. This dephosphorylation is important because it results in inhibition of the AKT signaling pathway.
PTEN is a 403 amino acid protein, and a member of the large PTP (protein tyrosine phosphatase) family. PTEN crystal structure revealed that the N-terminal phosphatase domain is followed by a tightly associated C-terminal C2 domain. These two domains together form a minimal catalytic unit. The phosphatase domain contains the active site which carries out the enzymatic function of the protein, whilst the C2 domain allows PTEN to bind to the phospholipid membrane.
PTEN is one of the most commonly lost tumour suppressors in human cancer, and its deregulation is also implicated in several other diseases. Hereditary mutation of PTEN causes tumor-susceptibility diseases such as Cowden disease.

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Anti-PTPRM Mouse Monoclonal Antibody [clone: T5-AF1A8]

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Mammalian target of rapamycin (mTOR), a serine/threonine kinase involved in diverse cellular processes, including protein translation, mRNA turnover, and protein stability, mediates, at least in part, some of the biological actions of Akt. As a Kinase subunit of both mTORC1(complex1) and mTORC2(complex2), mTOR regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation.

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Anti-ACTB Rabbit Polyclonal Antibody

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Platelet-derived growth factors (PDGFs) have been implicated in the control of cell proliferation, survival and migration. The PDGF family of growth factors consists of five different disulphide-linked dimers built up of four different polypeptide chains encoded by four different genes. Theses isoforms, PDGF-AA, PDGF-AB, PDGF-BB, PDGF-CC and PDGF-DD, act via two receptor tyrosine kinases, PDGF receptors α and β. Thus far, gene-targeting experiments have been attempted to create knockout mice deficient for PDGFR-α or PDGFR-β. Those mice, however, died either at the embryonic stage or several days after birth. Platelet-derived growth factor receptors, PDGFR-α and PDGFR-β, have five extracellular immunoglobulin-like domains and an intracellular tyrosine kinase domain. Upon binding a PDGF, the receptors form homo- and heterodimers. Dimerization of the receptors juxtaposes the intracellular part of the receptors, which allow phosphorylation in trans between the two receptors in the complex. These autophosphorylation provide docking sites for downstream signal transduction molecules. More than 10 different SH2–domain-containing molecules have been shown to bind to different autophosphorylation sites in the PDGF α- and β-receptors. There are signal transduction molecules with enzymatic activity, such as PI3-kinase, PLC-γ, Src, SHP-2, GAP, as well as adaptor molecules such as Grb2, Shc, Nck, Grb7 and Crk, and Stats. Each of the different partners recruited by the activated receptor initiates different signaling pathways, making possible a great variety of cellular response.

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Insulin receptor substrate (IRS) proteins play a central role in maintaining basic cellular functions such as growth and metabolism through insulin/insulin like growth factor (IGF) signaling. Four members (IRS-1, IRS-2, IRS-3, IRS-4) of this family have been identified which differ in their subcellular distribution and interaction with SH2 domain proteins. After phosphorylation by activated receptors, these intracellular signaling molecules recruit various downstream effector pathways including phosphatidylinositol 3-kinase, tyrosine protein phosphatase SHPTP-2, and several smaller adapter molecules such as the growth factor receptor-binding protein Grb-2.
IRS-1, the best characterized IRS protein, has eighteen potential tyrosine phosphorylation sites which directly bind to SH2 domains in downstrem proteins. IRS-1 consists of amino terminal containing pleckstrin homology (PH) domain followed by a phosphotyrosine-binding (PTB) domain which binds to IR and IGFR, and carboxy terminal containing multiple tyrosine and serine residues which become docking sites for proteins that have PTB domain such as SH2 domain.
IRS-4 is the last identified member of the IRS family. Cloning of human IRS-4 revealed a predicted protein of similar length to both IRS-1 and IRS-2and showed only 27% and 29% identity with IRS-1 and IRS-2, respectively. In contrast, IRS-4 exhibits higher degree of homology in the PH domain (43 to 50 %) and the PTB domain (43 to 66%) with the corresponding domains in IRS-1, IRS-2 and IRS-3.
IRSs are also thought to be able to induce malignant transformation. IRS-1 has been shown to be constitutively active in breast cancer.

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Attractin is a serum glycoprotein of 175 kDa and found in both membrane-bound and secreted forms as a result of alternative splicing. Both the secreted and membrane-bound forms of attractin may be involved in the development and maintenance of the central nervous system. Membrane-bound attractin is a co-receptor for Agouti, antagonist of melanocortin-1 receptor. Secreted attractin, expressed by activated T lymphocytes and modulates interactions between T cells and monocytes/macrophages, was examined as a potential marker of immune activity. Attractin may be a component of a pathway for regulated protein turnover that also involves mahogunin, a wide-expressed E3 ubiquitin ligase found at particularly high levels in the brain. Attractin was considered as an extracellular target amenable for the development of obesity-regulating drugs, also.

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Signal transducer and activator of transcription (STAT), named after their dual role, generally mediate cytokine, growth factor and hormone receptor signal transduction. In mammals, seven STAT proteins have been identified. STAT5 has been implicated in cellular functions of proliferation, differentiation and apoptosis with relevance to processes of hematopoiesis and immunoregulation, reproduction, and lipid metabolism. Two highly homologous STAT5 isoforms, 96kDa STAT5a and 94kDa STAT5b, are encoded by two tandemly linked genes. Although both STAT5 isoforms are roughly 95% homologous at the level of cDNA, they exhibit both redundant and non-redundant functions in vivo, probably due to differences in their transactivation domain. Aberrant regulation of STAT5 has been observed in solid tumors as well as in patients with either chronic or acute myeloid leukemia. Kinase inhibitors are currently being developed to negatively regulate STAT5 activity for clinical purposes.

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Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis.
Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol (1).

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Enolase (2-phosphogly-cerate hydrolyase or phosphopyruvate hydrates) is a glycolytic enzyme that catalyzes the dehydration and conversion of 2-phosphoglycerate to phosphoenolpyruvate. It comprises three distinct subunits, alpha, beta and gamma. Non Neuronal Enolase(ENO1) is an isoform of mammalian enolase and is composed of 2 alpha subunits. The gene for ENO1 also encodes a shorter monomeric structural lens protein, tau-crystallin.
Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.
Used as a diagnostic marker for many tumors and, in the heterodimeric form, alpha/gamma, as a marker for hypoxic brain injury after cardiac arrest. Also marker for endometriosis. Antibodies against alpha-enolase are present in sera from patients with cancer-associated retinopathy syndrome (CAR), a progressive blinding disease which occurs in the presence of systemic tumor growth, primarily small-cell carcinoma of the lung and other malignancies. Is identified as an autoantigen in Hashimoto encephalopathy (HE) a rare autoimmune disease associated with Hashimoto thyroiditis (HT). HT is a disorder in which destructive processes overcome the potential capacity of thyroid replacement leading to hypothyroidism

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The mammalian Phospholipase C(PLC) family has two closely related proteins, PLC1 and PLC2. The PLC isozymes have the core structure domains and a unique array of domains containing an additional PH domain, two SH2 domains and one SH3 domain. In response to extracellular stimuli, such as hormones and growth factors, receptor tyrosine kinases (RTKs) phosphorylate and activate PLC. Activated PLC catalyzes hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) to produce the metabolic second messenger molecules inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG).

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Kininogens are precursors for kinin, and the two main types of them are high-molecular weight kininogen (HMWK) and low-molecular weight kininogen (LMWK). HMWK also known as the Williams-Fitzgerald-Flaujeac factor is a protein from the blood coagulation system as well as the kinin-kallikrein system. It acts mainly as a cofactor on coagulation and inflammation, and has no intrinsic catalytic activity. LMWK is produced locally by numerous tissues, and secreted together with tissue kallikrein.
Kininogens are synthesized in the liver and circulate in the plasma and other body fluids.
The kinins are pharmacologically active polypeptides released in the tissues and body fluids as a result of the enzymatic action of kallikreins on kininogens. The kinin family includes bradykinin (BK) (Arg-Pro-Pro-gly-Phe-Ser-Pro-Phe-Arg), kallidin (Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) and methionyl-lysyl-BK (Met-Lys-Arg-Pro-Pro-Gly-Phe-Arg). Kallidin and methionyl-lysyl-BK are converted into BK by aminopeptidases present in plasma and urine. Active tissue kallikrein acts on LMWK to release kallidin. The plasma kallikrein is found in circulation in an inactive form, which is known as prekallikrein or Fletcher factor.
BK and kallidin act through activation of G-protein-coupled constitutive B(2) or inducible kinin B(1) receptors linked to signaling pathways involving increased intracellular Ca concentrations and/or release of mediators including arachidonic acid metabolites, NO and EDHF (Endothelium-derived hyperpolarizing factor). In the cardiovascular system, the kallikrein-kinin system exerts a fine control of vascular smooth muscle tone and arterial blood pressure, and plays a significant cardioprotective effect.

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Methionine sulfoxide reductase (MsrA) reduces methionine sulfoxide (MetO) residues in proteins and free MetO to Methionine (Met). The catalytic activity of MsrA is dependent of bound metal and cofactors but it requires reducing equivalents from either DTT or a thioredoxin-regenerating system. MsrA plays an essential role in protecting cells against oxidative damage. The substrates of MsrA include calmodulin, HIV protease and 1-proteinase-inhibitor (1-3). Recent studies indicate that there is a connection between MsrA and Alzheimer’s disease in mammals (4).

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Reversible phosphorylation of tyrosine residues is a key regulatory mechanism for numerous cellular events such as proliferation, differentiation, gene expression and migration. Abnormalities in tyrosine phosphorylation play a role in the pathogenesis of numerous inherited or acquired human diseases from cancer to immune deficiencies.
There are at least 107 genes coding for PTPs (protein tyrosine phosphatases) in the human genome.
All known PTPs contain a highly conserved 12 amino acid catalytic
domain and are further distinguished on the basis of additional structural motifs. The receptor-like PTPs exhibit an extracellular domain, a single transmembrane and one or two intracellular phosphatase domains. The nonreceptor cytoplasmic PTPs contain a single phosphatase domain and additional amino acid sequences that are homologous to motifs found in other classes of proteins.
Protein tyrosine phosphatases PTPN5 (STEP), PTPRR and PTPN7 comprise a family of phosphatases that specifically inactivate MAPKs (mitogen-activated protein kinases).
There are multiple forms of STEP in the adult rat brain which show differential enrichment in brain regions implicated in aspects of cognitive,
affective, and motor behaviors. Some of the STEP isoforms are generated through alternative splicing of a single STEP gene and each has unique intracellular targets and functions.