The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase
Abstract
High levels of reactive species of nitrogen and oxygen in diabetes may cause modifications of proteins. Recently, an increase in protein tyrosine nitration was found in several diabetic tissues. To understand whether protein tyrosine nitration is the cause or the result of the associated diabetic complications, it is essential to identify specific proteins vulnerable to nitration with in vivo models of diabetes. In the present study, we have demonstrated that succinyl-CoA:3-oxoacid CoA-transferase (SCOT; EC 2.8.3.5 ) is susceptible to tyrosine nitration in hearts from streptozotocin-treated rats. After 4 and 8 wk of streptozotocin administration and diabetes progression, SCOT from rat hearts had a 24% and 39% decrease in catalytic activity, respectively. The decrease in SCOT catalytic activity is accompanied by an accumulation of nitrotyrosine in SCOT protein. SCOT is a mitochondrial matrix protein responsible for ketone body utilization. Ketone bodies provide an alternative source of energy during periods of glucose deficiency. Because diabetes results in profound derangements in myocardial substrate utilization, we suggest that SCOT tyrosine nitration is a contributing factor to this impairment in the diabetic heart.
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Citations
Cites
Role of oxidative stress in diabetic complications: a new perspective on an old paradigm.
Baynes, J. W., & Thorpe, S. R. (1999) · Diabetes · doi:10.2337/diabetes.48.1.1 · Cited by 2,441
Nitric oxide and mitochondrial respiration
Brown, G. C. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00025-0 · Cited by 702
Nitric oxide synthase activity in mitochondria
Ghafourifar, P., & Richter, C. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01397-5 · Cited by 567
Regulation of energy substrate metabolism in the diabetic heart
Stanley, W. (1997) · Cardiovascular Research · doi:10.1016/s0008-6363(97)00047-3 · Cited by 480
Cited by
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Peroxynitrite: biochemistry, pathophysiology and development of therapeutics
Szabó, C., Ischiropoulos, H., & Radi, R. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2222 · Cited by 2,134
Multi-dimensional Roles of Ketone Bodies in Fuel Metabolism, Signaling, and Therapeutics
Puchalska, P., & Crawford, P. A. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.12.022 · Cited by 1,610
Ketone bodies as signaling metabolites
Newman, J. C., & Verdin, E. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.09.002 · Cited by 966
Oxidative stress in the placenta
Myatt, L., & Cui, X. (2004) · Histochemistry and Cell Biology · doi:10.1007/s00418-004-0677-x · Cited by 800
Metadata
- Authors
- Turko, I. V., Marcondes, S., & Murad, F.
- Venue
- American Journal of Physiology-Heart and Circulatory Physiology
- Publisher
- American Physiological Society
- Published
- 2001-12-01
- Volume
- 281
- Issue
- 6
- Pages
- H2289-H2294
- ISSN
- 0363-6135 (ISSN-L)
- 1522-1539
- OpenAlex
- W2154715233
- Cited by
- 181
- References
- 4
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- closed
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- Turko, I. V., Marcondes, S., & Murad, F. (2001). Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase. American Journal of Physiology-Heart and Circulatory Physiology. https://doi.org/10.1152/ajpheart.2001.281.6.h2289
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