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one additional protein, namely P58(IPK), specifically precipitated with Akita proinsulin and approximately ten fold more PDIA6, but not other PDI family members, was bound to Akita proinsulin. The latter suggests that PDIA6 may act as a key reductase
these findings demonstrated that ER Ca2+, PDIA6, IRE1alpha, and miR-322 function in a dynamic feedback loop modulating the UPR under conditions of disrupted ER Ca2+ homeostasis.
mitochondrial P5 may upregulate tricarboxylic acid cycle and possibly, other intramitochondrial metabolism.
By facilitating disulfide bond formation, and enhanced ER protein folding, PDIA6 may contribute to the protective effects of ATF6 in the ischemic mouse heart.
The cell surface trafficking of PDIA1, PDIA3, and PDIA6 is dependent on KDELR1, which travels in a dynamic manner to the cell surface. This transport is assumed to result in PDI cell surface association, which differs from PDI inducible secretion into the extracellular space.
ERp5 triggers fibrinogen dissociation from aIIbb3 integrin.
Study reported for the first time that one of the proteins that binds to P5 in U251 glioblastoma cells is vimentin, and the present findings indicated that P5 may be an attractive target for novel molecular targeted therapy of glioblastoma.
Results indicate that protein disulfide isomerase family 6 (PDIA6) overexpression promoted the proliferation of HeLa cells by suppressing the phosphorylation of beta-catenin, thereby inhibiting the degradation of beta-catenin through the ubiquitin-proteasome pathway.
the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD against PDI-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 inhibition.
Downregulation of PDIA6 inhibited BC cell proliferation and invasion in vitro as well as tumor growth and metastasis in vivo. In addition, PDIA6 downregulation suppressed the Wnt/beta-catenin signaling pathway.
Results indicate that re-expression of miR-127-3p and miR-376a-3p induces a strong tumor suppressor effect in GCTSC, which is partially mediated via COA1 and PDIA6.
ACE and PDIA6 were identified as potential HSPA2-interacting proteins; this assemblage resides in membrane raft microdomains located in the peri-acrosomal region of the sperm head.
Restoration of miR-127-3p and miR-376a-3p counteracts the neoplastic phenotype of giant cell tumor of bone derived stromal cells by targeting COA1, GLE1 and PDIA6.
PDIA3 and PDIA6 gene expression is a neoplasm aggressiveness marker in primary ductal breast cancer.
CDDP-resistant non-small lung cancer cells undergo profound remodeling of their endoplasmic reticulum (ER) proteome (>80 proteins identified by proteomics) and exhibit a dramatic overexpression of two protein disulfide isomerases, PDIA4 and PDIA6.
Txnip is located in the endoplasmic reticulum and interacts with endogenous PDIA6. Txnip increases PDI activity.
levels of expression of ERp5 and GRP78 correlated with the level of expression of membrane-bound MICA in chronic lymphocytic leukemia patients.
Data show that the lymph node (LN) stroma displayed in situ high levels of transcription and expression of the disulfide-isomerase ERp5 and of the disintegrin-metalloproteinase ADAM10, able to shed the ligands for NKG2D (NKG2D-L) from the cell membrane.
P5 forms a non-covalent complex with immunoglobulin heavy chain binding protein (BiP) and shows specificity towards BiP client proteins.
observed to have peptide-binding ability, and chaperone activity was confirmed with rhodanese and citrate synthase as substrates, but not with D-glyceraldehyde-3-phosphate dehydrogenase, showing substrate specificity with respect to chaperone activity
ERP5 regulates the binding of fibrinogen, cell-surface exposure of P-selectin, and coassociation of beta 3 integrin in stimulated platelets.
Pharmacological inhibition of thioreductase activity and ERp5 gene silencing revealed that cell-surface ERp5 function is required for MICA shedding
Protein disulfide isomerases (EC 18.104.22.168), such as PDIA6, are endoplasmic reticulum (ER) resident proteins that catalyze formation, reduction, and isomerization of disulfide bonds in proteins and are thought to play a role in folding of disulfide-bonded proteins (Hayano and Kikuchi, 1995
protein disulfide isomerase-related protein
, protein disulfide-isomerase A6
, thioredoxin domain containing 7
, thioredoxin domain-containing protein 7
, ER protein 5
, endoplasmic reticulum protein 5
, protein disulfide isomerase P5
, protein disulfide isomerase-associated 6
, thioredoxin domain containing 7 (protein disulfide isomerase)
, calcium-binding protein 1
, protein disulfide isomerase A6
, protein disulfide isomerase associated 6