DOI: 10.1016/0014-5793(94)01386-f. Two resident ER‐proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase

Two resident ER‐proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase

10.1016/0014-5793(94)01386-f

Crossref journal-article

Wiley

FEBS Letters (311)

Abstract

Protein disulfide‐isomerase (PDI) is the best known representative of a growing family of enzymes with thioredoxin domains. Two such proteins with thioredoxin (Trx) domains, CaBP1 and CaBP2 (ERp72), have previously been isolated from rat liver microsomes. Here we report that they, like PDI are substrates for thioredoxin reductase and will catalyze NADPH‐dependent insulin disulfide reduction. The activity of CaBP1 and CaBP2 in this assay was higher than that of PDI but lower than that of E. coli Trx. Furthermore, as isolated the thioredoxin domains of CaBP1 and CaBP2 were in disulfide form as judged by stoichiometric oxidation of 2 and 3 mol of NADPH in CaBP1 and CaBP2, respectively. The redox potential of the active site disulfide/dithiol was estimated from the equilibrium with a mutant E. coli Trx, P34H Trx, with a known redox potential (−235 mV). This showed that CaBP1 and CaBP2, like PDI, have a much higher redox potential than wild type thioredoxin (−270 mV) in agreement with a role in formation of protein disulfide bonds. In conclusion, in vitro CaBP1 and CaBP2 share catalytic properties in thiol disulfide‐interchange reactions with PDI. Thus, the well known activity of PDI is not unique in the endoplasmic reticulum and CaBP1 and CaBP2 may be regarded as functional equivalents.

Bibliography

LundstrÃ¶m-Ljung, J., Birnbach, U., Rupp, K., SÃ¶ling, H.-D., & Holmgren, A. (1995). Two resident ERâproteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase. FEBS Letters, 357(3), 305â308. Portico.

Authors 5

Johanna Lundström-Ljung (first)
Ulrike Birnbach (additional)
Katrin Rupp (additional)
Hans-Dieter Söling (additional)
Arne Holmgren (additional)

References 28 Referenced 68

10.1016/S0021-9258(18)96749-9
10.1016/0092-8674(89)90043-3
10.1038/317267a0
10.1146/annurev.bi.54.070185.001321
10.1016/S0021-9258(18)71625-6
10.1002/prot.340110103
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10.1021/bi00077a018
{'key': 'e_1_2_1_13_1', 'first-page': '785', 'volume': '213', 'author': 'Nguyen Van P.', 'year': '1993', 'journal-title': 'Eur. J. Biochem.'} / Eur. J. Biochem. by Nguyen Van P. (1993)
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Dates

Type	When
Created	23 years, 1 month ago (July 25, 2002, 9:35 p.m.)
Deposited	1 year, 11 months ago (Sept. 16, 2023, 12:19 p.m.)
Indexed	1 year ago (Aug. 12, 2024, 7:50 a.m.)
Issued	30 years, 7 months ago (Jan. 9, 1995)
Published	30 years, 7 months ago (Jan. 9, 1995)
Published Online	22 years, 1 month ago (Aug. 5, 2003)
Published Print	30 years, 7 months ago (Jan. 9, 1995)

Funders 0

None

BibTeX

@article{Lundstr_m_Ljung_1995, title={Two resident ER‐proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase}, volume={357}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(94)01386-f}, DOI={10.1016/0014-5793(94)01386-f}, number={3}, journal={FEBS Letters}, publisher={Wiley}, author={Lundström-Ljung, Johanna and Birnbach, Ulrike and Rupp, Katrin and Söling, Hans-Dieter and Holmgren, Arne}, year={1995}, month=jan, pages={305–308} }

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