Characterization and Chromosomal Localization of a New Protein Disulfide Isomerase, PDIp, Highly Expressed in Human Pancreas

Desilva, Mark G.; Lu, Jinping; Donadel, Giulia; Modi, William S.; Xie, Hong; Notkins, Abner Louis; Lan, Michael S.

doi:10.1089/dna.1996.15.9

Cited by 74 publications

(79 citation statements)

References 39 publications

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“…The same appears to be true for metazoan organisms, in which expression of PDIs also appears to be constitutive, although the actual levels may be higher during fetal development, when large amounts of proteins are being synthesized (42). A pancreas-specific PDI family member appears to be the sole example of a tissue-specific form in adults (43). Thus, the finding of two developmentally regulated PDIs in T. brucei contrasts with the consensus view in the literature that PDIs are constitutively expressed in eukaryotic organisms because of their essential role in protein folding.…”

Section: Discussionmentioning

confidence: 82%

Characterization of Two Protein Disulfide Isomerases from the Endocytic Pathway of Bloodstream Forms of Trypanosoma brucei

Rubotham¹,

Woods

García‐Salcedo³

et al. 2005

Journal of Biological Chemistry

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Proteins from the endocytic pathway in bloodstream forms of Trypanosome brucei are modified by the addition of linear poly-N-acetyllactosamine side chains, which permits their isolation by tomato lectin affinity chromatography. Antibodies against this tomato lectin binding fraction were employed to screen a cDNA expression library from bloodstream forms of T. brucei. Two cDNAs were prominent among those selected. These cDNAs coded for two putative protein disulfide isomerases (PDIs) that respectively contained one and two double-cysteine redox-active sites and corresponded to a single domain PDI and a class 1 PDI. Assays of the purified recombinant proteins demonstrated that both proteins possess isomerase activity, but only the single domain PDI had a reducing activity. These PDIs possess a number of unusual features that distinguish them from previously characterized PDIs. The expression of both is developmentally regulated, they both co-localize with markers of the endocytic pathway, and both are modified by N-glycosylation. The larger PDI possesses N-glycans containing poly-N-acetyllactosamine, a modification that is indicative of processing in the Golgi and suggests the presence of a novel trafficking pathway for PDIs in trypanosomes. Although generally PDIs are considered essential, neither activity appeared to be essential for the growth of trypanosomes, at least in vitro.

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Section: Discussionmentioning

confidence: 82%

Characterization of Two Protein Disulfide Isomerases from the Endocytic Pathway of Bloodstream Forms of Trypanosoma brucei

Rubotham¹,

Woods

García‐Salcedo³

et al. 2005

Journal of Biological Chemistry

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“…The PDI family member PDIp is exclusively expressed in the pancreas (19) and PDILT, in testis (20). As a lymphocytespecific protein, pERp1 likely is under control of a transcription factor specific for lymphocyte lineages.…”

Section: Discussionmentioning

confidence: 99%

Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1

Anken¹,

Pena²,

Hafkemeijer³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Plasma cells daily secrete their own mass in antibodies, which fold and assemble in the endoplasmic reticulum (ER). To reach these levels, cells require pERp1, a novel lymphocyte-specific small ER-resident protein, which attains expression levels as high as BiP when B cells differentiate into plasma cells. Although pERp1 has no homology with known ER proteins, it does contain a CXXC motif typical for oxidoreductases. In steady state, the CXXC cysteines are locked by two parallel disulfide bonds with a downstream C(X)6C motif, and pERp1 displays only modest oxidoreductase activity. pERp1 emerged as a dedicated folding factor for IgM, associating with both heavy and light chains and promoting assembly and secretion of mature IgM.

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“…Although little is known about islet expression of PDI, a pancreatic isoform of this protein has been identified (71). Recent studies have shown that NO can react with PDI to inhibit platelet aggregation (72) and that PDI is involved in the entry of NO into cells (73).…”

Section: Discussionmentioning

confidence: 99%

Cytokine- or chemically derived nitric oxide alters the expression of proteins detected by two-dimensional gel electrophoresis in neonatal rat islets of Langerhans.

et al. 2000

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Interleukin-1␤ (IL-1␤) treatment of neonatal rat islets19 of a total of 1,600 detectable proteins in GSNOtreated islets (P < 0.01). We conclude 1) that the expression of up to 42 proteins is altered by cytokineinduced or chemically generated NO in the precise experimental conditions chosen and 2) that the majority of proteins altered by prior treatment with IL-1␤ may be the result of NO-independent IL-1␤-mediated regulation of gene expression. This study demonstrates that the combination of 2D gel electrophoresis and mass spectrometry is a powerful tool in the identification of ␤-cell proteins involved in the response to toxic mediators.

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Characterization and Chromosomal Localization of a New Protein Disulfide Isomerase, PDIp, Highly Expressed in Human Pancreas

Cited by 74 publications

References 39 publications

Characterization of Two Protein Disulfide Isomerases from the Endocytic Pathway of Bloodstream Forms of Trypanosoma brucei

Characterization of Two Protein Disulfide Isomerases from the Endocytic Pathway of Bloodstream Forms of Trypanosoma brucei

Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1

Cytokine- or chemically derived nitric oxide alters the expression of proteins detected by two-dimensional gel electrophoresis in neonatal rat islets of Langerhans.

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