The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex.
Open accessAbstract
A bovine liver protein which catalyzes the transfer of triglyceride between membranes has previously been isolated from the lumen of the microsomal fraction. When further purified about 100-fold, two polypeptides of molecular mass 58,000 and 88,000 were identified (Wetterau, J. R., and Zilversmit, D. B. (1985) Chem. Phys. Lipids 38, 205-222). We demonstrate here that the two polypeptides (referred to as 58-kDa and 88-kDa, respectively) are associated in a protein-protein complex, and that the triglyceride transfer activity is associated with this complex. Antibodies specific for either polypeptide immunoprecipitated both the 58-kDa and 88-kDa polypeptides as well as the lipid transfer activity. The 58-kDa subunit of the microsomal transfer protein complex was identified as protein disulfide-isomerase (PDI) (EC 5.3.4.1) by 1) a comparison of the amino-terminal sequence of PDI and the 58-kDa subunit of the transfer protein, 2) a comparison of the reverse phase high performance liquid chromatography peptide maps of CNBr digests of PDI and the lipid transfer protein, 3) immunoprecipitation competition experiments in which PDI was found to compete with the lipid transfer protein for immunoprecipitation by the anti-58-kDa polyclonal antibodies, 4) immunological cross-reactivity of the microsomal triglyceride transfer protein complex with polyclonal antibodies raised against PDI, and 5) the appearance of protein disulfide isomerase activity following the dissociation of purified microsomal transfer protein complex with guanidine HCl. In conclusion, the microsomal triglyceride transfer protein has a multi-subunit structure which is unique compared to other intracellular lipid transfer proteins which have been described to be single polypeptides. The unexpected finding that PDI is a component of the microsomal triglyceride transfer protein complex suggests a new previously undescribed role for protein disulfide isomerase.
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Kivirikko, K. I., Myllylä, R., & Pihlajaniemi, T. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.5.2537773 · Cited by 320
Cited by
Microsomal triglyceride transfer protein and its role in apoB-lipoprotein assembly
Hussain, M. M., Shi, J., & Dreizen, P. (2003) · Journal of Lipid Research · doi:10.1194/jlr.r200014-jlr200 · Cited by 591
Protein folding: local structures, domains, subunits, and assemblies
Jaenicke, R. (1991) · Biochemistry · doi:10.1021/bi00227a001 · Cited by 438
Lyles, M. M., & Gilbert, H. F. (1991) · Biochemistry · doi:10.1021/bi00217a004 · Cited by 419
Sharp, D., Blinderman, L., Combs, K. A., Kienzle, B., Ricci, B., Wager-Smith, K., Gil, C. M., Turck, C. W., Boumas, M.-E., Rader, D. J., et al. (1993) · Nature · doi:10.1038/365065a0 · Cited by 393
Self-citationNoiva, R., & Lennarz, W. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50556-7 · Cited by 318
Metadata
- Authors
- Wetterau, J. R., Combs, K. A., Spinner, S. N., & Joiner, B. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-06
- Volume
- 265
- Issue
- 17
- Pages
- 9800-9807
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1591366077
- Cited by
- 365
- References
- 1
- FWCI
- 16.15
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Wetterau, J. R., Combs, K. A., Spinner, S. N., & Joiner, B. J. (1990). Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)38742-3
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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