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p38 MAPK cascade regulates a variety of cellular responses to stress, inflammation and other signals. p38 MAPK is relatively inactive in the non-phosphorylated form and becomes rapidly activated by dual phosphorylation of a Thr-Gly-Tyr motifs. There are four isoforms of p38 MAPK, , ,  and , which differ in their tissue expression and affinity for upstream activators and downstream effectors.
When cells are exposed to tumor necrosis factor-, interleukin-1, heat shock, or other activating stimuli, activation of MAPK kinase-3 and –6 occurs by phosphorylation. Activated MAPK kinase-3/6 phosphorylate each residue of Thr180 and Tyr182 in p38 MAPK. Phospho-p38 MAPK activates ATF-2, CHOP-1, MEF-2 and other transcription factors through phosphorylation.

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Noggin is a 32 kDa glycoprotein that binds to bone morphogenetic protein (BMP) and antagonizes the action of them. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo. BMPs also regulate cell proliferation, differentiation, lineage determination, motility, and death. BMP antagonists include noggin, chordin, follistatin, ventroptin, twisted gastrulation, Dan, and gremlin etc. They play a crucial role in bone development, by regulating the BMP functions.
Noggin plays a key role in neurulation by inhibiting BMP4, along with other morphogens such as chordin and follistatin and in the formation of the neural plate. Noggin inhibits BMP signaling by blocking the molecular interfaces of the binding epitopes for both type I and type II receptors. It antagonizes the action of BMPs, and induces neural tissue and dorsalizes ventral mesoderm.

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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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Glutamine Synthetase(GS) catalyzes the conversion of ammonia and glutamate to glutamine. This reaction consumes a molecule of ATP:
Glutamate + NH4+ + ATP
 Glutamine + ADP + Pi
GS is found in astrocytes as an octamer of identical 45kDa subunits. Most well known function of GS is the detoxification of brain ammonia. It also has an important role in controlling metabolic regulations of neurotransmitter glutamate. Because of the multiple functions and importance of GS in cellular metabolism, both catalytic activities and synthesis are highly regulated. The activity of GS is controlled by adenylylation. Its activity is decreased in the cerebral cortex of brains affected by Alzheimer’s disease, particularly in the vicinity of senile plaques. It is also decreased under conditions of glucose deprivation. On the other hands, the level of expression of GS is increased during ischemia in vivo or hypoxia in culture.

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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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Glutathione reductase (GR) is a member of pyridine nucleotide-disulfide oxidoreductases, which includes the closely related enzymes thioredoxin reductase, lipoamide dehydrogenase, trypanothione reductase and mercuric ion reductase. GR is a cytoplasmic flavoenzyme widely distributed in aerobic organisms. The dimeric protein is composed of two identical subunits, each containing 1 FAD and 1 redox-active disulfide/dithiol as components of the catalytic apparatus. It plays a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG) (1):
GSSG + NADPH + H+  2GSH + NADP+
In most eukaryotic cells, GR maintains the ratio of [GSH]/[GSSG] elevated, and participates in several vital functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis (2).

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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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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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Btk (Bruton's tyrosine kinase) is a member of the Tec family of protein tyrosine kinases (PTKs) and plays a modulatory role in many cellular processes, such as proliferation, development, differentiation, survival, and apoptosis. The Tec kinases are the second largest family of non-receptor tyrosine kinases and include Tec, Btk, Bmx, Itk, and TXK/Rlk. Mutations of Btk gene cause a primary immunodeficiency disease in humans, X-linked aγglobulinemia (XLA) which is characterized by a lack of circulating B lymphocytes and an absence of immunoglobulins as a result of defects in B cell maturation and function. Btk is found in all hematopoietic cells, with the exception of T lymphocytes and plasma cells. Btk contains amino-terminal PH (pleckstrin homology) domain which binds phosphatidylinositol (3,4,5)-trisphosphate (PIP3) helping membrane translocation upon PI3 kinase activation. The Tec kinases have similar structure of N-terminal PH domains followed by Tec homology (TH), Src homology 3 (SH3), Src homology 2 (SH2), and kinase domains. Autophosphorylation of Tyr223 in SH3 domain is necessary for full activation of Btk. Various binding proteins have been reported to interact with different domains of Btk.

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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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PRAK is a 471 amino acid protein with 20-30% sequence identity to the known MAP kinase-regulated protein kinases RSK1/2/3, MNK1/2 and MAPKAPK2/3.
The p38 mitogen-activated protein kinase (MAPK) pathway plays an important role in cellular responses to inflammatory stimuli and environmental stress. There are at least six protein kinases that can be regulated by p38α and/or p38β. These downstream kinases of p38s include MAPK-activated protein kinase 2 (MAPKAPK2 or MK2), MAPKAPK3, MAPK-interacting kinase 1 (MNK1), MNK2, p38-activated/regulated protein kinase (PRAK or MAPKAPK5), and mitogen- and stress-activated protein kinase (MSK). PRAK can be activated in response to cellular stress and proinflammatory cytokines. T182 within the activation loop of PRAK has been determined to be the regulatory phosphorylation site. PRAK has been reoprted to be essential for ras-induced senescence and tumor suppression. PRAK mediates senescence upon activation by p38 in response to oncogenic ras.

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The members of the Src-family kinases are Src, Lyn, Fyn, Yes, Hck, Lck, Fgr, Blk, and Yrk. Each of these have a common structure consisting of an unique domain at the N-terminal, followed by SH3, SH2 and tyrosine kinase domains.
In immume cells, the Src-family kinases play roles as critical regulators of a large number of intracellular signaling pathways, including integrin signaling pathway. Integrins are major cellular receptor that mediate cell to cell and cell to substratum interactions.
Src is expressed ubiquitously, however the expression level is higher in brain, osteoclasts, and platelets. Src plays a role in cell adhesion, cell morphology and motility, and bone resorption.
Src contains a 14-carbon myristoyl group attached to an SH4 domain, a unique domain, an SH3 domain, an SH2 domain, an SH2-kinase linker, a protein–tyrosine kinase domain (the SH1 domain), and a C-terminal regulatory segment.
One of the two most important regulatory phosphorylation sites in Src is Tyr527. Under basal conditions in vivo, 90–95% of Src is phosphorylated at Tyr527, and phosphotyrosine 527 binds intramolecularly with the Src SH2 domain. Tyrosine 416 is present in the activation loop and its phosphorylation promotes kinase activity.

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ζ-chain associated protein kinase, ZAP70, is a 70 kDa member of the Syk family kinase predominantly involved in T cell receptor (TCR) signaling. It is structurally homologous to Syk, a PTK that is involved in proximal BCR signaling. ZAP-70 is a key signaling molecule in T cell activation and also plays a role in apoptosis and cell migration.
SYK family tyrosine kinases contain a C-terminal kinase domain and tandem N-terminal SH2 domains that bind phosphorylated ITAMs (immunoreceptor tyrosine-based activation motif). Linker region that contains multiple tyrosines separates the SH2 domains from the kinase domain. Phosphorylated tyrosines act as docking sites for phospholipase Cγ1 (PLCγ1).
ZAP-70 and Syk are functionally homologous in antigen receptor signaling. Expression of ZAP-70 in Syk− B cells reconstitutes SCR function. Reconstitution requires the presence of functional Src homology 2 (SH2) and catalytic domains of ZAP-70.
Expression of ZAP-70 is an important negative prognostic factor in chronic lymphocytic leukemia (CLL) with more rapid disease progression and shorter survival.

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Creatine kinase (CK), also known as phosphocreatine kinase or creatine phosphokinase (CPK) is an enzyme expressed by various tissue types. It catalyzes the reversible transfer of the N-phosphoryl group from phosphocreatine (PCr) to ADP to regenerate ATP. Creatine kinase plays a key role in the energy homeostasis of cells with intermittently high, fluctuating energy requirements, such as skeletal and cardiac muscle cells, neurons, photoreceptors, spermatozoa and electrocytes.
Creatine kinase consists of two subunits, which can be either B (brain type) or M (muscle type). Therefore, three different cytosolic isoenzymes exist: CK-MM, CK-BB and CK-MB. Cytosolic CK isoenzymes are always co-expressed in a tissue-specific fashion together with a mitochondrial isoform. Skeletal muscle expresses CK-MM (98%) and low levels of CK-MB (1%). The heart muscle expresses CK-MM at 70% and CK-MB at 25-30%. CK-BB is expressed in all tissues at low levels.
Cytosolic CKs, in close conjunction with Ca2+-pumps, play a crucial role for the energetics of Ca2+-homeostasis. Octameric mitochondrial Mi-CK binds and crosslinks mitochondrial membranes. The CK system is
regulated by AMP-activated protein kinase via PCr/Cr and ATP/AMP ratios.
The cardiac-specific isoenzyme of creatine kinase, CK-MB, is a biomarker for myocardial infarction along with other markers such as cardiac Troponin I and myoglobin. The introduction of immunologic mass determination of CK-MB was a major breakthrough that replaced the traditional enzymatic assay.

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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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p38 MAPK cascade regulates a variety of cellular responses to stress, inflammation and other signals. p38 MAPK is relatively inactive in the non-phosphorylated form and becomes rapidly activated by dual phosphorylation of a Thr-Gly-Tyr motifs. There are four isoforms of p38 MAPK, , ,  and , which differ in their tissue expression and affinity for upstream activators and downstream effectors.
When cells are exposed to tumor necrosis factor-, interleukin-1, heat shock, or other activating stimuli, activation of MAPK kinase-3 and –6 occurs by phosphorylation. Activated MAPK kinase-3/6 phosphorylate each residue of Thr180 and Tyr182 in p38 MAPK. Phospho-p38 MAPK activates ATF-2, CHOP-1, MEF-2 and other transcription factors through phosphorylation.

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Ubiquitin(Ub) is a small protein that is composed of 76 amino acids. Ub is found only in eukaryotic organisms and is highly conserved. Ub can exist either in free form or as part of a complex with other proteins. In the latter case, Ub is attached(conjugated) to proteins through a covalent bond between the glycine at the C-terminal end of Ub and the side chains of lysine on the proteins; Ubiquitination.  Ub functions to regulate protein turnover in a cell by closely regulating the degradation of specific proteins. Ubiquitin has been immunohistochemically localized to a number of pathological inclusions, including ; Lewy bodies of Parkinson’s disease,neurofibrillary of Alzheimer’s disease, Pick bodies of Pick’s disease.

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IκB kinase α (IKKα) is a component of a multiprotein kinase complex that regulates the activity of the transcription factor NF-κB. Activation of the IKK complex via upstream stimuli leads to phosphorylation and degradation of NF-κB bound IκB(Inhibitor of κB). Subsequently, free NF-κB dimers enter the nucleus and regulate the transcription of a variety of target genes involved in cell proliferation and differentiation, apoptosis, and inflammation, etc. The IKK complex consists of 2 highly homologous kinase subunits, IKKα and IKKβ, and a nonenzymatic regulatory component, IKKγ/NEMO. The relative contributions of IKKα and IKKβ to the signalling complex vary according to the requirements of the cell. IKKβ plays a predominant role in immune responses, while IKKα alone appears to be sufficient for at least some developmental systems. Recently, IKK/NF-κB signaling pathway was studied as therapeutic targets in cancer.

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CAD (caspase-activated DNase), a 40kDa nuclear protein, is primarily responsible for cell-autonomous DNA degradation during apoptosis. CAD is present in healthy cells where it is held in an inactive state through the association with its inhibitor ICAD. The ICAD protein is inactivated in apoptotic cells via caspase-3 cleavage thereby releasing CAD, which subsequently cleaves chromosomal DNA. CAD is a magnesium-dependent endonuclease specific for double stranded DNA that generates double strand breaks with 3'-hydroxyl ends. The nuclease preferentially attacks chromatin in the internucleosomal linker DNA. However, the nuclease hypersensitive sites can be detected and CAD is potentially involved in large-scale DNA fragmentation as well. CAD-mediated DNA fragmentation triggers chromatin condensation that is another hallmark of apoptosis.

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The mitochondrial protein Smac/DIABLO(second mitochondria-derived activator) performs a critical function in apoptosis by eliminating the inhibitory effect of IAPs (inhibitor of apoptosis proteins) on caspases. The newly synthesized Smac protein contains 239 amino acids. Its N-terminal 55 residues encode the mitochondrial-targeting sequence and are proteolytically removed in the mature Smac protein. In the intrinsic cell death pathway, the key event leading to the activation of caspases is the release of several pro-apoptotic proteins such as Smac/DIABLO from the intermembrane space of mitochondria into the cytosol. During apoptosis, Smac is released from mitochondria and re-activates the processed initiator and effector caspases by relieving IAP-mediated inhibition. Furthermore, Smac/DIABLO plays an important regulatory role in the sensitization of cancer cells to both immune-and drug-induced apoptosis.

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Fibronectin is a high molecular weight glycoprotein containing about 5% carbohydrate that binds to receptor proteins that span the cells membrane, called integrins. In addition to integrins, they also bind extracellular matrix components such as collagen, fibrin and heparin. Fibronectin can be found in the blood plasma in its soluble form which is composed of two 250 kDa subunits joined together by disulfide bonds. Plasma fibronectin is made in the liver by hepatocytes. The insoluble form that serves as a linker in the extracellular matrix is a large complex of cross-linked subunits. Fibronectin is involved in many cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/ adhesion, so it can be used as a therapeutic agent for wound healing. It is also one of the few proteins for which production increases with age without any associated pathology.

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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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Lactoferrin(Lf), one of transferrin family, is found in external fluids, including milk and mucosal secretions, and prominent components of the secondary granules of neutrophils. Lf consists of a single polypeptide chain (approximately 80 kDa) folded into two structurally homologous lobes, each of which can reversibly bind one ferric ion (Fe3+). Lf plays a central role in iron metabolism and host defense system against microbial infection.

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Prothrombin precursor is synthesized in liver as a precursor of prothrombin containing a signal sequence and a propeptide domain at the N-terminus. Before its secretion into plasma, this precursor undergoes several posttranslational modifications, including removal of signal sequence and propeptide domains, glycosylation, and γ-glutamyl-carboxylation reaction. Prothrombin, cleaved by the prothrombinase enzyme complex that consists of serine protease factor Xa, cofactor Va, phospholipids and calcium, is converted to thrombin which converts fibrinogen into fibrin which in turn strengthens a protective clot. Activation of prothrombin is crucial in physiological and pathological coagulation. Various rare diseases involving prothrombin(e.g. hypoprothrombinemia) have been described.

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Vimentin is a member of the intermediate filament family of proteins found in various non-epithelial cells, especially mesenchymal cells. Vimentin is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. Vimentin plays a significant role in supporting and anchoring the position of the organelles in the cytosol. Although most intermediate filaments are stable structures, vimentin also has a dynamic nature which is important when offering flexibility to the cell.
Two monomers which have central α-helical domains, capped on each end by non-helical domains twist around each other to form a coiled-coil dimer. Two dimers then form a tetramer, which, in turn, form a sheet by interacting with other tetramers.
There are some reports related to the biochemical function of intermediate filament network. The intracellular movement of LDL-derived cholesterol from the lysosome to the site of esterification is a vimentin-dependent process. A role for vimentin in mechanotransduction of shear stress has also been suggested. The mechanical stress of fluid shear on endothelial cells seems to trigger MAPK signaling pathways and stimulates proliferation.

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The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxidoreductases. 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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Anti-G-CSF Rabbit Polyclonal Antibody

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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 6 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 1, 2, and 6 in cytosol, Prx 3 in mitochondria, Prx 4 in ER and secretion, Prx 5 showing complicated distribution including peroxisome, mitochondria and cytosol (1).

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Integrin-linked kinase (ILK) is an adaptor and signaling protein that couples integrins to the actin cytoskeleton and coordinates signal transduction from extracellular matrix and growth factors.
By interacting with the focal adhesion proteins PINCH, paxillin, and parvin, ILK regulates integrin- mediated cell adhesion and cytoskeletal dynamics within focal adhesions to regulate cell adhesion, spreading, and migration.
ILK is involved in the suppression of apoptosis and promotion of cell survival through the phosphorylation of AKT(Ser473), GSK-3(Ser9), myosin light chain(Ser18/19), and affixin.
ILK activity is stimulated by PI3 kinase and negatively regulated by the tumor suppressor PTEN.

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Cathepsin D(CatD) is a ubiquitously expressed lysosomal aspartyl
protease involved in the normal degradation of proteins apoptosis and
autophagy. Human CatD is synthesized on the endoplasmic reticulum as
a pre-pro-enzyme. Preprocathepsin D(412aa) is cleaved and glycosylated
to form an inactive procathepsin D (392aa) and then further cleaved to
generate an active intermediate (348aa) single-chain molecule. The active
intermediate is further processed into mature two chain form of cathepsin
D, this processing step is carried out by cathepsin B or L. The two-chain
form consists of an amino terminal light chain (14 kDa) and a
carboxyl-terminal heavy chain (34 kDa). Additionally, several more amino
acids are removed from the carboxyl terminus of the 34 kDa heavy chain.
Procathepsin D (pCD), secreted from cancer cells, acts as a mitogen on
both cancer and stromal cells and stimulates their proinvasive and
pro-metastatic properties.