The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action.
Open accessAbstract
with insulin disulfides was estimated from fluorescence measurements and the enzymatic rates to be around 1 X 10’ M-’ s-l. This is around 10,000 times higher than the second order rate constant for the reaction between insulin and dithiothreitol, demonstrating the high affinity of insulin for thioredoxin-(SH)z. Nondisulfide oxidants such as Cu2+ ions, diamide, and vitamin KI, which are known to mimic the effects of insulin on cellular hexose transport, were rapidly reduced by the thioredoxin system. The exceptional reactivity of insulin and thioredoxin-(SH)2, in vitro, is consistent with a physiological function for mammalian thioredoxin in the degradation of insulin. Functions for thioredoxin in the “thiol oxidation-reduction model” of insulin action are discussed.
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Cites
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Cuatrecasas, P. (1974) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.43.070174.001125 · Cited by 639
Diamide, a new reagent for the intracellular oxidation of glutathione to the disulfide
Kosower, N. S., Kosower, E. M., Wertheim, B., & Correa, W. S. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90850-x · Cited by 525
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution.
Holmgren, A., Söderberg, B. O., Eklund, H., & Brändén, C. I. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.6.2305 · Cited by 438
Self-citationBinding and degradation of 125I-insulin by rat hepatocytes.
Terris, S., & Steiner, D. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40770-9 · Cited by 421
Insulin Interactions with Liver Plasma Membranes
Freychet, P., Kahn, R., Roth, J., & Neville, D. M. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45126-0 · Cited by 397
Thioredoxin and glutathione regulate photosynthesis in chloroplasts
WOLOSIUK, R. A., & BUCHANAN, B. B. (1977) · Nature · doi:10.1038/266565a0 · Cited by 344
Enzymatic Synthesis of Deoxyribonucleotides
Moore, E. C., Reichard, P., & Thelander, L. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97743-4 · Cited by 340
Fractionation of oxidized insulin
Sanger, F. (1949) · Biochemical Journal · doi:10.1042/bj0440126 · Cited by 318
Atomic Positions in Rhombohedral 2-Zinc Insulin Crystals
BLUNDELL, T. L., CUTFIELD, J. F., CUTFIELD, S. M., DODSON, E. J., DODSON, G. G., HODGKIN, D. C., MERCOLA, D. A., & VIJAYAN, M. (1971) · Nature · doi:10.1038/231506a0 · Cited by 312
Cited by
Molecular and Cellular Aspects of Thiol–Disulfide Exchange
Gilbert, H. F. (1990) · Advances in Enzymology - and Related Areas of Molecular Biology · doi:10.1002/9780470123096.ch2 · Cited by 758
Nishiyama, A., Matsui, M., Iwata, S., Hirota, K., Masutani, H., Nakamura, H., Takagi, Y., Sono, H., Gon, Y., & Yodoi, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21645 · Cited by 730
Thioredoxin and Related Molecules–From Biology to Health and Disease
Lillig, C. H., & Holmgren, A. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724
Self-citationAntioxidant Function of Thioredoxin and Glutaredoxin Systems
Holmgren, A. (2000) · Antioxidants & Redox Signaling · doi:10.1089/ars.2000.2.4-811 · Cited by 502
Self-citationNagy, P. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4973 · Cited by 477
Metadata
- Authors
- Holmgren, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1979-09
- Volume
- 254
- Issue
- 18
- Pages
- 9113-9119
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2152614869
- Cited by
- 323
- References
- 26
- FWCI
- 4.43
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Holmgren, A. (1979). Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)86818-7
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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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