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PDIA2  -  protein disulfide isomerase family A,...

Homo sapiens

Synonyms: PDA2, PDI, PDIP, PDIR, PDIp, ...
 
 
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Disease relevance of PDIA2

  • Previously, we found that protein-disulfide isomerase (PDI) is specifically up-regulated in response to hypoxia/brain ischemia in astrocytes [1].
  • Human protein-disulfide isomerase (hPDI)-related protein (hPDIR), which we previously cloned from a human placental cDNA library (Hayano, T., and Kikuchi, M. (1995) FEBS Lett. 372, 210-214), and its mutants were expressed in the Escherichia coli pET system and purified by sequential nickel affinity resin chromatography [2].
  • Screening for hPDIR-binding proteins using a T7 phage display system revealed that alpha1-antitrypsin binds to hPDIR [2].
  • Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology [3].
  • Furthermore, we demonstrate that human cytomegalovirus US3 protein inhibits CD8(+) T cell recognition by mediating PDI degradation, verifying the functional relevance of PDI-catalyzed peptide editing in controlling intracellular pathogens [4].
 

Psychiatry related information on PDIA2

  • METHOD: Eighty-one patients diagnosed with a mental disorder with psychotic features (schizophrenia, schizoaffective disorder, bipolar disorder, major depression) and 210 putatively healthy individuals were invited to complete the PDI and the brief version of the General Health Questionnaire (GHQ-12) [5].
  • Here we show, in brains manifesting sporadic Parkinson's or Alzheimer's disease, that PDI is S-nitrosylated, a reaction transferring a nitric oxide (NO) group to a critical cysteine thiol to affect protein function [6].
  • The Personality Disorder Institute/Borderline Personality Disorder Research Foundation randomized control trial (PDI/BPDRF RCT) is a randomized control trial comparing three treatments for borderline personality disorder (BPD) [7].
  • PURPOSE:: This prospective longitudinal study was designed to evaluate whether the four-month Movement Assessment of Infants (MAI), predicted two-year cognitive and motor developmental status measured by the Mental (MDI) and Psychomotor (PDI) Scales of the Bayley Scales of Infant Development (BSID) [8].
 

High impact information on PDIA2

  • In the endoplasmic reticulum of eukaryotes, disulfide formation is catalyzed by protein disulfide isomerase (PDI); by contrast, prokaryotes produce a family of disulfide bond (Dsb) proteins, which together achieve an equivalent outcome in the bacterial periplasm [9].
  • To determine whether this is the case, we investigated the ability of PDI to bind to a folding polypeptide chain within a functionally intact endoplasmic reticulum and to be dissociated from the alpha-subunit of P4H in vitro in the presence of reducing or oxidizing agents [10].
  • We also demonstrate that the dissociation of PDI from substrates observed in the presence of glutathione disulfide can be explained by competition for the peptide-binding site on PDI [10].
  • We further show that PDI suppresses TF coagulant activity in a nitric oxide-dependent pathway, linking the regulation of TF thrombogenicity to oxidative stress in the vasculature [11].
  • To determine the functional significance of PDI in cell migration, we tested the effect of a PDI inhibitor, bacitracin, and a PDI monoclonal antibody on glioma cell migration and invasion in vitro [12].
 

Chemical compound and disease context of PDIA2

  • In conclusion, using a global proteomics approach, PDI was identified to play an important role in glioma cell invasion, and its action was effectively inhibited by bacitracin [12].
  • However, the cell-surface thiol-reactive reagent 5, 5'-dithiobis(2-nitrobenzoic acid) (DTNB) had a much stronger inhibitory effect in our system, suggesting that cell-surface thiol-containing molecules other than PDI, acting alone or in concert, have a greater effect than PDI on HIV-1 Env-mediated fusion [13].
  • Fermentation process for tetrameric human collagen prolyl 4-hydroxylase in Escherichia coli: Improvement by gene optimisation of the PDI/beta subunit and repeated addition of the inducer anhydrotetracycline [14].
  • The aim of this study was to evaluate the therapeutic activity of Deprenyl in patients with Parkinson disease already being treated with L-Dopa + PDI [15].
 

Biological context of PDIA2

  • This article reviews our current knowledge of the PDI family members and identifies four novel PDIs in the human genome [16].
  • It is known that the b' domain of PDI provides the principal peptide binding site of PDI and that this domain is critical for catalysis of isomerization but not oxidation reactions in protein substrates [17].
  • These observations suggested that ubiquilin together with PDI have critical functions as regulatory proteins for CHOP-mediated cell death, and therefore up-regulation of these proteins may result in acquisition of tolerance against ischemic stress in glial cells [1].
  • Thus, the substrate specificity of hPDIR differed from that associated with isomerase activity, and the contribution of the CSMC motif to the oxidative refolding of alpha1-antitrypsin was the most definite of the three (CSMC, CGHC, CPHC) [2].
  • Protein disulfide isomerase (PDI) catalyzes protein folding and thiol-disulfide interchange reactions [18].
 

Anatomical context of PDIA2

  • Interestingly, ubiquilin is also up-regulated in response to hypoxia in glial cells with a time course similar to that of PDI induction [1].
  • Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas [18].
  • Northern analysis of normal human tissues and various human tumor cell lines revealed PDIp mRNA (2.0 kb) expression only in the normal pancreas [18].
  • In pancreatic islets, Ero1beta expression is high, but is inversely correlated with PDI and PDIp levels, demonstrating that cell-specific differences exist in the regulation of oxidative protein folding in vivo [19].
  • Sp1 also appears to participate in the regulation of PDI gene expression, since overexpression of Sp1 stimulated PDI promoter activity in HeLa cells and mutations introduced into each of these Sp1-binding sites separately reduced the promoter strength, although even the largest decrease was only about 50% [20].
 

Associations of PDIA2 with chemical compounds

  • It has been suggested that this binding is regulated by the redox state of PDI, with association requiring the presence of glutathione, and dissociation the presence of glutathione disulfide [10].
  • The effectiveness of PDI as a catalyst of native disulfide bond formation in folding polypeptides depends on the ability to catalyze disulfide-dithiol exchange, to bind non-native proteins, and to trigger conformational changes in the bound substrate, allowing access to buried cysteine residues [17].
  • Thus, DTT appears to alter the conformation of PDI, as suggested by the DTT-induced change in DNA association, but not its NM association [21].
  • In a number of other cell types, a 55-kDa thyroid hormone-binding protein has been identified and shown to be a subunit of the enzyme protein disulfide isomerase (PDI) [22].
  • The hydrodynamic properties of glial-p55, determined by molecular sieve chromatography and sucrose density centrifugation, showed that this protein has a native molecular mass of 115 kDa, which is in close agreement with that reported for PDI [22].
 

Physical interactions of PDIA2

  • Immobilized PDI was not found to interact neither with soluble tetrameric GAPDH, nor with soluble denatured GAPDH [23].
 

Other interactions of PDIA2

 

Analytical, diagnostic and therapeutic context of PDIA2

References

  1. Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death. Ko, H.S., Uehara, T., Nomura, Y. J. Biol. Chem. (2002) [Pubmed]
  2. Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding. Horibe, T., Gomi, M., Iguchi, D., Ito, H., Kitamura, Y., Masuoka, T., Tsujimoto, I., Kimura, T., Kikuchi, M. J. Biol. Chem. (2004) [Pubmed]
  3. Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology. Conn, K.J., Gao, W., McKee, A., Lan, M.S., Ullman, M.D., Eisenhauer, P.B., Fine, R.E., Wells, J.M. Brain Res. (2004) [Pubmed]
  4. Redox Regulation Facilitates Optimal Peptide Selection by MHC Class I during Antigen Processing. Park, B., Lee, S., Kim, E., Cho, K., Riddell, S.R., Cho, S., Ahn, K. Cell (2006) [Pubmed]
  5. The psychometric discriminative properties of the Peters et al Delusions Inventory: a receiver operating characteristic curve analysis. Preti, A., Rocchi, M.B., Sisti, D., Mura, T., Manca, S., Siddi, S., Petretto, D.R., Masala, C. Comprehensive psychiatry (2007) [Pubmed]
  6. S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Uehara, T., Nakamura, T., Yao, D., Shi, Z.Q., Gu, Z., Ma, Y., Masliah, E., Nomura, Y., Lipton, S.A. Nature (2006) [Pubmed]
  7. The Personality Disorders Institute/Borderline Personality Disorder Research Foundation Randomized Control Trial for Borderline Personality Disorder: Reliability of Axis I and II Diagnoses. Critchfield, K.L., Levy, K.N., Clarkin, J.F. The Psychiatric quarterly (2007) [Pubmed]
  8. The Movement Assessment of Infants (MAI) as a Predictor of Two-Year Neurodevelopmental Outcome for Infants Born at Term Who Are at Social Risk. Rose-Jacobs, R., Cabral, H., Beeghly, M., Brown, E.R., Frank, D.A. Pediatric physical therapy : the official publication of the Section on Pediatrics of the American Physical Therapy Association. (2004) [Pubmed]
  9. Protein disulfide isomerase: the structure of oxidative folding. Gruber, C.W., Cemazar, M., Heras, B., Martin, J.L., Craik, D.J. Trends Biochem. Sci. (2006) [Pubmed]
  10. Is protein disulfide isomerase a redox-dependent molecular chaperone? Lumb, R.A., Bulleid, N.J. EMBO J. (2002) [Pubmed]
  11. Disulfide isomerization switches tissue factor from coagulation to cell signaling. Ahamed, J., Versteeg, H.H., Kerver, M., Chen, V.M., Mueller, B.M., Hogg, P.J., Ruf, W. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  12. Protein disulfide isomerase expression is related to the invasive properties of malignant glioma. Goplen, D., Wang, J., Enger, P.?.?., Tysnes, B.B., Terzis, A.J., Laerum, O.D., Bjerkvig, R. Cancer Res. (2006) [Pubmed]
  13. Role of protein disulfide isomerase and other thiol-reactive proteins in HIV-1 envelope protein-mediated fusion. Ou, W., Silver, J. Virology (2006) [Pubmed]
  14. Fermentation process for tetrameric human collagen prolyl 4-hydroxylase in Escherichia coli: Improvement by gene optimisation of the PDI/beta subunit and repeated addition of the inducer anhydrotetracycline. Neubauer, A., Soini, J., Bollok, M., Zenker, M., Sandqvist, J., Myllyharju, J., Neubauer, P. J. Biotechnol. (2007) [Pubmed]
  15. Deprenyl in Parkinson disease: personal experience. Giovannini, P., Grassi, M.P., Scigliano, G., Piccolo, I., Soliveri, P., Caraceni, T. Italian journal of neurological sciences. (1985) [Pubmed]
  16. The thioredoxin-like fold: hidden domains in protein disulfide isomerases and other chaperone proteins. Clissold, P.M., Bicknell, R. Bioessays (2003) [Pubmed]
  17. Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase. Pirneskoski, A., Klappa, P., Lobell, M., Williamson, R.A., Byrne, L., Alanen, H.I., Salo, K.E., Kivirikko, K.I., Freedman, R.B., Ruddock, L.W. J. Biol. Chem. (2004) [Pubmed]
  18. Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas. Desilva, M.G., Lu, J., Donadel, G., Modi, W.S., Xie, H., Notkins, A.L., Lan, M.S. DNA Cell Biol. (1996) [Pubmed]
  19. Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta. Dias-Gunasekara, S., Gubbens, J., van Lith, M., Dunne, C., Williams, J.A., Kataky, R., Scoones, D., Lapthorn, A., Bulleid, N.J., Benham, A.M. J. Biol. Chem. (2005) [Pubmed]
  20. Interaction of transcription factor Sp1 with the promoter of the gene for the multifunctional protein disulphide isomerase polypeptide. Tasanen, K., Oikarinen, J., Kivirikko, K.I., Pihlajaniemi, T. Biochem. J. (1993) [Pubmed]
  21. Evidence that protein disulfide isomerase (PDI) is involved in DNA-nuclear matrix anchoring. VanderWaal, R.P., Spitz, D.R., Griffith, C.L., Higashikubo, R., Roti Roti, J.L. J. Cell. Biochem. (2002) [Pubmed]
  22. Characterization of a N-bromoacetyl-L-thyroxine affinity-labeled 55-kilodalton protein as protein disulfide isomerase in cultured glial cells. Safran, M., Leonard, J.L. Endocrinology (1991) [Pubmed]
  23. Study on the interactions between protein disulfide isomerase and target proteins, using immobilization on solid support. Muronetz, V.I., Zhang, N.X., Bulatnikov, I.G., Wang, C.C. FEBS Lett. (1998) [Pubmed]
  24. Thermodynamics of the folding of D-glyceraldehyde-3-phosphate dehydrogenase assisted by protein disulfide isomerase studied by microcalorimetry. Liang, Y., Li, J., Chen, J., Wang, C.C. Eur. J. Biochem. (2001) [Pubmed]
  25. Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp. Ruddock, L.W., Freedman, R.B., Klappa, P. Protein Sci. (2000) [Pubmed]
  26. Screening for novel pancreatic genes from in vitro-induced pancreas in Xenopus. Sogame, A., Hayata, T., Asashima, M. Dev. Growth Differ. (2003) [Pubmed]
  27. Identification of protein disulfide isomerase as an endothelial hypoxic stress protein. Graven, K.K., Molvar, C., Roncarati, J.S., Klahn, B.D., Lowrey, S., Farber, H.W. Am. J. Physiol. Lung Cell Mol. Physiol. (2002) [Pubmed]
  28. Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR). Hayano, T., Kikuchi, M. FEBS Lett. (1995) [Pubmed]
 
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