background pdi 57 - Insights into the role of ERp57 angin bawa kabar kasana 79 in cancer PMC National Center for Background Evidence for association between asthma and the unfolded protein response is emerging Endoplasmic reticulum resident protein 57 ERp57 is an endoplasmic reticulumlocalized redox chaperone involved in folding and secretion of glycoproteins We have previously demonstrated that ERp57 is upregulated in allergenchallenged human and protein 57 ERp57PDIA3 is an important family member because it is the closest homologue to protein disulphide isomerase PDIA1 known as PDI the prototype of the PDI family and together PDI and ERp57 mediate disulphide bond formation of most proteins C E Jessop et al 2009 ERp57 is distinct from PDI because it displays dierences Functional Role of the Disulfide Isomerase ERp57 in Axonal Regeneration Protein disulfide isomerase PDI is the prototypic member of the PDI family of enzymes best known in forming disulfide bonds in endoplasmic reticulum proteins 1 Several members of this family have a role in platelet function and thrombosis including PDI ERp5 and ERp57 212 Plateletderived PDI mediates platelet aggregation secretion 35 and adhesion 46 However plateletderived PDI ERp57 is of similar size and domain structure to PDI with 33 identity in its amino acid sequences 14 ERp57 has 505 amino acids while PDI has 508 with the catalytic a and a domains sharing 50 amino acid identity 14 Like PDI it contains 2 CGHC activesite sequences and catalyzes the reversible oxidation of thiols to disulfides and the isomerization of disulfide bonds Endoplasmic reticulum protein 57 ERp57PDIA3 is an important family member because it is the closest homologue to protein disulphide isomerase PDIA1 known as PDI the prototype of the PDI family and together PDI and ERp57 mediate disulphide bond formation of most proteins C E Jessop et al 2009 Thiol Isomerases in Thrombus Formation Circulation Research ERp57 is a major PDI family member expressed in the nervous system and has deposit 888 slot 3 been identified as one of the main proteins upregulated in tissue derived from ALS and CreutzfeldtJacob patients 15 16 18 19 22 A few knockout mouse models for PDIs have been described to date including ERp57 ERp29 ERdj5 PDIA1 and AGR2 31 5257 Protein Disulfide Isomerase Endoplasmic Reticulum Protein 57 ERp57 is PDF Protein Disulfide Isomerase Endoplasmic Reticulum Protein 57 Springer Plateletderived ERp57 mediates platelet incorporation into a growing PDI the prototype of these thiol isomerases has a molecular weight of 57 000 and includes 508 amino acids Encoded by the P4HB gene it is composed of 4 thioredoxinlike domains abba where a and a are catalytically active units with the CGHC motif in the active site and preceeded by a signal sequence Protein disulfide isomerases PDIs are an important cellular oxidoreductase enzyme family including several structurally related components The members of this family are characterized by thioredoxinlike domains containing one or more active sites with the canonical CysXXCys sequencePhylogenetic analysis of the human PDI family and subfamilies revealed a high correlation among Protein disulfide isomeraseendoplasmic reticulum resident protein 57 P2X7 receptor signaling contributes to tissue factordependent ERp57PDIA3 new insight Cellular Molecular Biology Letters PDI is an oxidoreductase localized mainly in the endoplasmic reticulum ER but on the cell surface PDI is crucial for protein Snitrosylation and nitric oxide uptake 18 19 PDI may influence TF procoagulant function through thiol and nitric oxidedependent mechanisms since TF is susceptible to Snitrosylation and glutathionation 7 Structure The PDI family includes more than 20 members that catalyze cysteinebased redox reactions and play critical roles in productive protein folding 14 15ERp57 is a highly conserved protein consisting of four thioredoxinlike site domainstermed a b b and aand an acidic Cterminal tail Figure Figure1 1Domains a and a contain the redox active site whereas domains b and The disulfide isomerase ERp57 kakaktogel 45 mediates platelet aggregation hemostasis
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