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.
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...
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.
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.
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.
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....
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
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
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.
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.
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.
Transglutaminase 2 (TG2; EC 18.104.22.168) 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.
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
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.
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.
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.