Disulfide isomerase

The formation of disulfide bonds in the endoplasmic reti-culum requires protein disulfide isomerase (PDI) and endoplasmic reticulum oxidoreductin 1 (ERO1) that reoxi-dizes PDI. We report here that the expression of the rat, mouse andhumanhomologues ofERO1-Likeproteinabut not of the isoform ERO1-Lbare stimulated by hypoxia in rats vivo and in rat, mouse and human cell cultures.

8p fptmusic 16-04-2013 63 4   Download

Protein disulfide oxidoreductases are ubiquitous redox enzymes that catalyse dithiol–disulfide exchange reactions with a CXXC sequence motif at their active site. Adisulfide oxidoreductase, a highly thermostable protein, was isolated from Pyrococcus furiosus(PfPDO), which is characterized by two redox sites (CXXC) and an unusual molecularmass. Its 3D structure at high resolution suggests that it may be related to the multidomain protein disulfide-isomerase (PDI), which is currently known only in eukaryotes....

12p dell39 03-04-2013 37 3   Download

Protein disulfide isomerase family proteins are known to play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase family genes from soybean leaf (Glycine maxL. Merrill cv. Jack) mRNA by RT-PCR using forward and reverse primers designed from the expressed sequence tag clone sequences.

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Protein disulfide isomerase family proteins play important roles in the fold-ing of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disul-fide isomerase family genes from soybean leaf (Glycine maxL. Merrill. cv Jack). The cDNAs encode proteins of 525 and 551 amino acids, named GmPDIL-1 and GmPDIL-2, respectively.

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Adhesive properties of endothelial cells are influenced by the thioldisulfide balance. However, the molecular mechanism of this effect is unclear, although recent observations indicate that integrin receptors may be direct targets for redox modulation. The purpose of this study was to examine whether protein disulfide isomerase (PDI) is directly involved in this pro-cess.

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The protein disulfide isomerase is known to play important roles in the folding of nascent polypeptides and in the formation of disulfide bonds in the endoplasmic reticulum (ER). In this study, we cloned a gene of a novel protein disulfide isomerase family from soybean leaf (Glycine maxL. Mer-rill. cv Jack) mRNA.

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Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein, although disulfide bond formation can also play a regulatory role.

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The oxidative folding of disulfide-rich conotoxins is essential for their biological functions.In vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase. To elucidate the physiologic roles of pro-tein disulfide isomerase in the folding of conotoxins, we have cloned a novel full-length protein disulfide isomerase from Conus marmoreus.

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Protein disulfide isomerase is the most abundant and best studied of the disulfide isomerases that catalyze disulfide bond formation in the endoplas-mic reticulum, yet the specifics of how it binds substrate have been elusive. Protein disulfide isomerase is composed of four thioredoxin-like domains (abb¢a¢).

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Protein disulfide isomerase (PDI) and other PDI family proteins are mem-bers of the thioredoxin superfamily and are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum (ER). The exact functions of PDI family proteins in plants remain unknown.

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5¢-Deoxy-5¢-methylthioadenosine phosphorylase II fromSulfolobus solfatari-cus (SsMTAPII) and purine nucleoside phosphorylase from Pyrococcus furiosus (PfPNP) are hyperthermophilic purine nucleoside phosphorylases stabilized by intrasubunit disulfide bonds. In their C-terminus, both enzymes harbour a CXC motif analogous to the CXXC motif present at the active site of eukaryotic protein disulfide isomerase.

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Protein disulfide isomerases (PDIs) are enzymes that mediate oxidative pro-tein folding in the endoplasmic reticulum. Understanding of PDIs has historically been hampered by lack of structural information. Over the last several years, partial and full-length PDI structures have been solved at an increasing rate.

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To successfully dissect molecular pathwaysin vivo, there is often a need to use specific inhibitors. Bacitracin is very widely used as an inhibitor of pro-tein disulfide isomerase (PDI) in vivo. However, the specificity of action of an inhibitor for a protein-folding catalyst cannot be determined in vivo. Furthermore,in vitro evidence for the specificity of bacitracin for PDI is scarce, and the mechanism of inhibition is unknown.

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The peptide antibiotic bacitracin is widely used as an inhibitor of protein disulfide isomerase (PDI) to demonstrate the role of the protein-folding catalyst in a variety of molecular pathways. Commercial bacitracin is a mixture of at least 22 structurally related peptides.

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Transglutaminase 2 (TG2; EC 2.3.2.13) is the most abundantly expressed member of the transglutaminase family and exerts opposing effects on cell growth, differentiation and apoptosis via multiple activities, including transamidase, GTPase, cell adhesion, protein disulfide isomerase, kinase and scaffold activities.

12p cosis54 08-12-2012 38 2   Download

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Critical Care giúp cho các bạn có thêm kiến thức về ngành y học đề tài: Downregulation of protein disulfide isomerase in sepsis and its role in tumor necrosis factor-alpha release...

8p coxanh_3 27-10-2011 52 4   Download