Postconditioning leads to an increase in protein S-nitrosylation
| العنوان: | Postconditioning leads to an increase in protein S-nitrosylation |
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| المؤلفون: | Junhui Sun, Mark J. Kohr, Angel Aponte, Guang Tong, Charles Steenbergen, Elizabeth Murphy |
| المصدر: | American Journal of Physiology-Heart and Circulatory Physiology. 306:H825-H832 |
| بيانات النشر: | American Physiological Society, 2014. |
| سنة النشر: | 2014 |
| مصطلحات موضوعية: | Male, Physiology, Carbazoles, Nitric Oxide, Protein S, Nitric oxide, Mice, chemistry.chemical_compound, Protein S-nitrosylation, Physiology (medical), NG-Nitroarginine Methyl Ester, medicine, Animals, Ischemic Postconditioning, biology, medicine.disease, Mice, Inbred C57BL, chemistry, Biochemistry, Reperfusion Injury, Models, Animal, biology.protein, Signaling and Stress Response, Signal transduction, Cardiology and Cardiovascular Medicine, Reperfusion injury, Signal Transduction |
| الوصف: | Previous studies have shown a role for nitric oxide and S-nitrosylation (SNO) in postconditioning (PostC), but specific SNO proteins and sites have not been identified in the myocardium after PostC. In this study, we examined SNO signaling in PostC using a Langendorff-perfused mouse heart model. After 20 min of equilibrium perfusion and 25 min of global ischemia, PostC was applied at the beginning of reperfusion with six cycles of 10 s of reperfusion and 10 s of ischemia. The total period of reperfusion was 90 min. Compared with the ischemia-reperfusion (I/R) control, PostC significantly reduced postischemic contractile dysfunction and infarct size. PostC-induced protection was blocked by treatment with NG-nitro-l-arginine methyl ester (l-NAME) (10 μmol/l; a constitutive NO synthase inhibitor), but not by either ODQ (10 μmol/l, a highly selective soluble guanylyl cyclase inhibitor) or KT5823 (1 μmol/l, a specific protein kinase G inhibitor). Two biotin switch based methods, two dimensional CyDye-maleimide difference gel electrophoresis (2D CyDye-maleimide DIGE) and SNO-resin-assisted capture (SNO-RAC), were utilized to identify SNO-modified proteins and sites. Using 2D CyDye-maleimide DIGE analysis, PostC was found to cause a 25% or greater increase in SNO of a number of proteins, which was blocked by treatment with l-NAME in parallel with the loss of protection. Using SNO-RAC, we identified 77 unique proteins with SNO sites after PostC. These results suggest that NO-mediated SNO signaling is involved in PostC-induced cardioprotection and these data provide the first set of candidate SNO proteins in PostC hearts. |
| تدمد: | 1522-1539 0363-6135 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5961d0620e23e1980083bb6868da7606Test https://doi.org/10.1152/ajpheart.00660.2013Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....5961d0620e23e1980083bb6868da7606 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15221539 03636135 |
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