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α2-Macroglobulin (α2M), is a 720-kDa homotetrameric glycoprotein composed of four identical 180 kDa subunit. α2M shares with other α-macroglobulins, like the complement components C3 and C4 and the pregnancy zone protein PZP, an extraordinary binding capacity for a variety of ligands. This allows the α-macroglobulins to serve as humoral defense barriers against foreign peptides in the plasma. α2M interacts and captures virtually any proteinase, often referred to as a panprotease inhibitor. In the brain of Alzheimer's disease (AD) patients, α2M also has been localized to diffuse amyloid plaques, supporting an important role for α2M in AD etiopathology.

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α2-Macroglobulin (α2M), is a 720-kDa homotetrameric glycoprotein composed of four identical 180 kDa subunit. α2M shares with other α-macroglobulins, like the complement components C3 and C4 and the pregnancy zone protein PZP, an extraordinary binding capacity for a variety of ligands. This allows the α-macroglobulins to serve as humoral defense barriers against foreign peptides in the plasma. α2M interacts and captures virtually any proteinase, often referred to as a panprotease inhibitor. In the brain of Alzheimer's disease (AD) patients, α2M also has been localized to diffuse amyloid plaques, supporting an important role for α2M in AD etiopathology.

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Immunoglobulin M (IgM) forms polymers where multiple immunoglobulins are covalently linked together with disulfide bonds, normally as a pentamer and the J chain is attached to most pentamers. It has a large molecular mass of approximately 900 kD. Due to its polymeric nature, IgM possesses high avidity, and is particularly effective at complement activation. It is sometimes called a "natural antibody", but it is likely that the antibodies arise due to sensitization in the very young to antigens that are naturally occurring in nature. IgM is the first immunoglobulin expressed by mature B cells. IgM antibodies appear early in the course of an infection and usually do not reappear after further exposure. IgM antibodies do not pass across the human placenta. These two biological properties of IgM make it useful in the diagnosis of infectious diseases. Demonstrating IgM antibodies in patients serum indicates recent or in serum from a neonate intrauterine infection such as congenital rubella.

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Retinol binding protein (RBP), a 21kDa single-chain glycoprotein, is the primary plasma transport protein for retinol (vitamin A1). RBP solubilizes the water-insoluble retinol and works as a vehicle for transport to the target organs, and it may also protect the bound retinol from oxidative damage in the plasma. The circulating RBP binds to another protein called transthyretin (TTR), a 55-kDa plasma thyroxine binding protein. Such protein-protein complex formation is thought to prevent glomerular filtration of low molecular mass RBP. Serum levels of RBP are useful in the detection of liver disease, protein-calorie malnutrition, and vitamin A deficiencies. In addition, the determination of RBP serum levels has been shown to be important in the mediation of antitumor effects.

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Plasminogen, a 92kDa glycoprotein, is produced by the liver and is present in plasma and extracellular fluids. Plasminogen is the inactive precursor of plasmin, a potent serine protease involved in the dissolution of fibrin blood clots. Plasminogen can be converted into the active plasmin by plasminogen activators urokinase (uPA), tissue plasminogen activator (tPA), factor XII-dependent components. The plasmin system has been implicated in a variety of physiological and pathological processes such as fibrinolysis, tissue remodeling, cell migration, inflammation, and tumor invasion and metastasis. Hereditary defects of plasminogen is a predisposing risk factor for thromboemboric disease.

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The c-Jun N-terminal protein kinases (JNKs) are a family of serine/threonine protein kinases of the mitogen-activated protein kinase (MAPK) group. JNKs, which are essential regulators of physiological and pathological processes, are involved in several diseases including diabetes, atherosclerosis, stroke, and Parkinson's and Alzheimer's diseases. The JNK family consists of three isoforms; JNK1 and JNK2, which are ubiquitous, and JNK3, which is present primarily in the heart, brain and testis. Differential splicing and exon use yield 10 isoforms of JNK. JNK1 is an important mediator of insulin resistance associated with obesity, but it is also indispensable for the intact cytoarchitecture of the brain.

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Protein Phosphatase 2A (PP2A) is one of the major Ser/Thr phosphatases implicated in the regulation of many cellular processes including regulation of different signal transduction pathways, cell cycle progression, DNA replication, gene transcription and protein translation. The core structure comprises a 36 kDa catalytic subunit (PP2AC) and a 65 kDa regulatory subunit (PR65 or A subunit). Each PP2A subunit has at least two isoforms and the catalytic subunit, present in the α and β isoforms, share 97% homology. The differential association of all these subunits gives rise to an extensive subset of oligomeric holoenzymes. It is widely thought that PP2A exercises regulatory flexibility and differential substrate specificity through the specific association of the core dimer (PP2AD) with one of the three regulatory B subunits. Moreover, PP2A interacts with a still growing number of cellular and viral proteins and is regulated by posttranslational modifications.

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ERK1 and ERK2 are widely expressed and are involved in the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virus infection, ligands for heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors and transforming agents, activate the ERK1 and ERK2 pathways.
When growth factors bind to the receptor tyrosine kinase, Ras interacts with Raf, the serine/threonine protein kinase and activates it as well. Once actived, Raf phosphorylates serine residue in 2 further kinases, MEK1/2, which in turn phosphorylates tyrosine/threonine in extracellular-signal regulated kinase(ERK) 1/2. Upon activation, the ERKs either phosphorylate a number of cytoplasmic targets or migrate to the nucleus, where they phosphorylate and activate a number of transcription factors such as c-Fos and Elk-1.

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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-bisphosphoglycerate 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, DNA repair, nuclear RNA export, membrane fusion 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. On recent study, GAPDH has identified of the most oxidant sensitive cell proteins.

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Ferredoxin reductase is a ubiquitous flavoenzyme, containing noncovalently bound FAD as a prosthetic group (1). It plays a role in delivering NADPH or low potential one-electron donors such as ferredoxin and flavodoxin to redox-based metabolisms in plastids, mitochondria and bacteria (2). In mammals, ferredoxin reductase is loosely associated with the inner mitochondrial membrane and receives electrons from NADPH. These electrons are transferred to ferredoxin which shuttles electrons to cytochrome P450 in the adrenal cortex mitochondrial steroid hydroxylation systems (3).

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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, α, β and γ. The γγ and αγ dimeric forms of enolase, referred to as neuron-specific enolase(NSE), are localized mainly in neurons and neuroectodermal tissue. NSE has a high stability in biological fluids and can easily diffuse to the extracellular medium and cerebrospinal fluid(CSF) when neuronal membranes are injured. NSE is used clinically as a sensitive and useful marker of neuronal damage in several neurological disorders including stroke, hypoxic brain damage, status epilepticus, Creutzfeldt-Jakob disease, and herpetic encephalitis.

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Transthyretin(TTR), generally called prealbumin, is a plasma protein that plays an important role in physiology such as a transporter of hormone thyroxine and retinal-binding protein. After produced primarily in the liver, TTR is excreted into the plasma. TTR represents a disproportionate fraction (25%) of CSF protein, prompting the suggestion that it is either selectively transported across the blood-CSF barrier or synthesized de novo within the central nervous system.
Transthyretin is a constituent found to the neuritic plaques, neurofibrillary tangles, and microangiopathic lesions of senile cerebral amyloid. It has been reported that more than 40 different mutations in the TTR gene associated with amyloid deposition.

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Synaptotagmins(Syts) are a large gene family of synaptic vesicle integral membrane proteins. Syt functions as regulators of both exocytosis /endocytosis and is involved in neurotransmitter secretion from small secretory vesicles. 13 isoforms of Syt have been identified(SytI-XIII).
SynaptotagminVI is localized to the endoplasmic reticulum and/or Golgi-like perinuclear compartment. It may be important for trafficking and calcium signaling as it is specially expressed in non-neuronal tissues. Also SytVI is present in the acrosomal region of mammalian spermatozoa. The cytosolic domain of SytVI can abrogate exocytosis by competing with the endogenous protein for essential interactions with the fusion machinery involved in a acrosomal exocytosis.

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Transglutaminase(TGase) catalyses the crosslink of proteins by forming -(-glutamyl) lysine isopeptide bonds and requires the binding of Ca2+ for its activity. In mammals, eight distinct TGase isoenzymes have been identified. Tissue transglutaminase (tTGase), also known as TGase 2, has four distinct domains: N-terminal -sandwich, catalytic core and two C-terminal -barrel domains. tTGase may have a role in cell death, cell proliferation, cell differentiation, and receptor-mediated endocytosis. In the Alzheimer’s disease brain, the elevated tTGase activity is manifested by polymerization of a number of proteins, including A peptide, -amyloid precursor protein and the tau protein, with formation of neurofibrillary tangles.

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Glutaredoxin (Grx), also known as thiol transferase, is a small heat-stable oxidoreductase. Grxs form part of the glutaredoxin system, comprising NADPH, GSH and glutathione reductase, which transfers electrons from NADPH to glutaredoxins via GSH (1). First recovered in E.coli as GSH-dependent hydrogen donors for ribonucleotide reductase, Grx catalyzes GSH-disulfide oxido-reductase via two redox-active cysteine residues (2). The active sequence (Cys-Pro-Tyr-Cys) is conserved in a variety of species. The 12 kDa dithiol protein has a role in reduction of mixed disulfides in cells exposed to oxidative stress (3).

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Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic /mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract (1). Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation (2). Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine (3). All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site (4-5).

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Glutaredoxin (Grx), also known as thiol transferase, is a small heat-stable oxidoreductase. Grxs form part of the glutaredoxin system, comprising NADPH, GSH and glutathione reductase, which transfers electrons from NADPH to glutaredoxins via GSH (1). First recovered in E.coli as GSH-dependent hydrogen donors for ribonucleotide reductase, Grx catalyzes GSH-disulfide oxido-reductase via two redox-active cysteine residues (2). The active sequence (Cys-Pro-Tyr-Cys) is conserved in a variety of species. The 12 kDa dithiol protein has a role in reduction of mixed disulfides in cells exposed to oxidative stress (3).

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The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 – 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1).

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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 thioredoxindependent 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.

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Glutathione peroxidases (Gpxs) are ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic/mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPxfamily to be discovered. GPx2, also known as gastrointestinal GPx(GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract (1). Extracellular plasma GPx(pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation (2). Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxylipids in low density lipoprotein orthymine (3). All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site (4-5).

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Protein Phosphatase 2A (PP2A) is a ubiquitous and conserved Serine/Threonine phosphatase and accounts for a large fraction of phosphatase activity in eukaryotic cells. PP2A plays an important role in cell cycle regulation, cell growth control, development, regulation of various signal transduction pathways, and cell mobility.
PP2A comprises A and B subunits which are regulatory and a catalytic C subunit. When the PP2A catalytic C subunit (36 kDa) associates with the regulatory A (65 kDa, PR65) and B subunits (PR55, PR56, PR72, PR93 etc), wide variety of heterotrimeric holoenzymes are produced with distinct functions and characteristics. The different association of the subunits give PP2A large regulatory flexibility and differential substrate specificity. The A subunit exists as two isoforms ( α and β ) as does the C subunit, whereas the B subunits fall into three families designated B, B' (also called B56), and B''. The A subunit is the scaffold required for the formation of the heterotrimeric complex and the binding of A subunit alters the enzymatic activity of the catalytic subunit, even if the B subunit is absent.

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Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak, Bid and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). The mitochondrial release of cytochrome c through anion channel is regulated by Bcl-2 and Bcl-xL. The Bcl-2 family of proteins are key regulators of many signals leading to caspase, which when activated cause cellular destruction by cleaving a range of vital cellular substrates.
The members of the Bcl-2 family share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4).
The Bcl-2 gene has been implicated in a number of cancers, including melanoma, breast, prostate, and lung carcinomas, as well as schizophrenia and autoimmunity. It is also thought to be involved in resistance to conventional cancer treatment.
Apoptosis is an important component of the sequence of events during which anticancer drugs induce an antitumor response. The molecular mechanism for drug-induced apoptosis is associated with a mitochondrial dysfunction that is characterized by an increase in MOMP and a release of cytochrome c from mitochondria, indicating that Bcl-2 plays a critical role in anticancer drug-induced apoptosis.

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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.

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Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/ dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds (1). Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations (2). Specific protein disulfide targets for reduction by Trx include protein disulfide–isomerase (PDI) (3) and a number of transcription factors such as p53 (4), NF-kB (5) and AP-1 (T1-151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins (6-7).

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Transglutaminase(TGase) catalyses the crosslink of proteins by forming ε-(γ-glutamyl) lysine isopeptide bonds and requires the binding of Ca2+ for its activity. In mammals, eight distinct TGase isoenzymes have been identified. Tissue transglutaminase (tTGase), also known as TGase 2, has four distinct domains: N-terminal β-sandwich, catalytic core and two C-terminal β-barrel domains. tTGase may have a role in cell death, cell proliferation, cell differentiation, and receptor-mediated endocytosis. In the Alzheimer’s disease brain, the elevated tTGase activity is manifested by polymerization of a number of proteins, including Aβ peptide, β-amyloid precursor protein and the tau protein, with formation of neurofibrillary tangles.

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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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Cyclin D3, ~34kDa, is a member of cyclin D family that promotes cell cycle progression to the DNA systhesis (S) phase. Cyclins complexed with cyclin-dependent kinases(CDKs) mediate phosphorylation of other proteins relevant to cell proliferation. D-type cyclins and their complexing CDKs phosphorylate the retinoblastoma gene product with influences transcription of growth-controlling genes. Cyclin D3 regulates cell proliferation during hematopoiesis, carcinogenesis, and may have function in the terminally differentiated cells. In recent studies, there is reports that cyclin D3 involves in multiple myeloma and malignant precursor T cells.

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Haptoglobin (abbreviated as Hp) is a protein in the blood plasma that binds free hemoglobin released from erythrocytes with high affinity and thereby inhibits its oxidative activity. Hp in its simplest form consists of two α- and two β-chains, connected by disulfide bridges. The chains originate from a common precursor protein which is proteolytically cleaved during protein synthesis. Hp exists in two allelic forms in the human population, so called Hp1 and Hp2; the latter one having arisen due to the partial duplication of Hp1 gene. Three phenotypes of Hp are found in humans: Hp1-1, Hp2-1, and Hp2-2. Hp phenotypes are associated with pathogenesis of a number of human disorders, such as diabetes, cardiovascular disease, etc. Hp plays a role in the host defence responses to infection and inflammation, acting as a natural antagonist for receptor-ligand activation of the immune system, also.

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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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NCK1 is one of the adaptor proteins which mediate specific protein-protein interactions in signaling processes. Adaptor proteins usually contain several domains like SH2 (Src homology 2) and SH3 which allow specific interactions with other specific proteins.
NCK1 and NCK2 showing high sequence identity (68%) have three SH3 domains and a C-terminal SH2 domain. Both of them bind receptor tyrosine kinases such as PDGFR and other tyrosine phosphorylated
proteins via their SH2 domains. Various molecules which interact with SH domains of Nck and regulate signaling process of actin cytoskeleton reorganization have been identified. Ncks are thought to have important functions in the development of mesodermal structures during embryogenesis, linked to a role in cell movement and cytoskeletal reorganization.
Nck also have a function in modulating mRNA translation at the level of initiation by interacting eukayotic initiation factor 2 (eIF2). Under the stressed conditions, protein synthesis is reduced by inhibiting the activity of eIF2 through the phosphorylation, transiently inhibiting recycling of eIF2
into its active form.