Regulation of sGCviahsp90, Cellular Heme, sGC Agonists, and NO: New Pathways and Clinical Perspectives
| العنوان: | Regulation of sGCviahsp90, Cellular Heme, sGC Agonists, and NO: New Pathways and Clinical Perspectives |
|---|---|
| المؤلفون: | Arnab Ghosh, Dennis J. Stuehr |
| المصدر: | Antioxidants & Redox Signaling. 26:182-190 |
| بيانات النشر: | Mary Ann Liebert Inc, 2017. |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | Models, Molecular, inorganic chemicals, 0301 basic medicine, Protein Conformation, Physiology, Protein subunit, Clinical Biochemistry, Heme, Nitric Oxide, Bioinformatics, Models, Biological, Biochemistry, 03 medical and health sciences, Cytosol, Soluble Guanylyl Cyclase, 0302 clinical medicine, Heat shock protein, Humans, Medicine, heterocyclic compounds, HSP90 Heat-Shock Proteins, Molecular Biology, General Environmental Science, biology, business.industry, Nitrosylation, Eukaryota, Cell Biology, Hsp90, Cell biology, Nitric oxide synthase, 030104 developmental biology, 030220 oncology & carcinogenesis, Chaperone (protein), cardiovascular system, biology.protein, General Earth and Planetary Sciences, Disease Susceptibility, Nitric Oxide Synthase, Protein Multimerization, Signal transduction, Forum Review Article, business, Soluble guanylyl cyclase, Biomarkers, Protein Binding, Signal Transduction |
| الوصف: | Significance: Soluble guanylate cyclase (sGC) is an intracellular enzyme that plays a primary role in sensing nitric oxide (NO) and transducing its multiple signaling effects in mammals. Recent Advances: The chaperone heat shock protein 90 (hsp90) associates with signaling proteins in cells, including sGC, where it helps to drive heme insertion into the sGC-β1 subunit. This allows sGC-β1 to associate with a partner sGC-α1 subunit and mature into an NO-responsive active form. Critical Issues: In this article, we review evidence to date regarding the mechanisms that modulate sGC activity by a pathway where binding of hsp90 or sGC agonist to heme-free sGC dictates the assembly and fate of an active sGC heterodimer, both by NO and heme-dependent or heme-independent pathways. Future Directions: We discuss some therapeutic implications of the NO-sGC-hsp90 nexus and its potential as a marker of inflammatory disease. Antioxid. Redox Signal. 26, 182–190. |
| تدمد: | 1557-7716 1523-0864 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32367711c17d052d2cbe43a2e035426bTest https://doi.org/10.1089/ars.2016.6690Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....32367711c17d052d2cbe43a2e035426b |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15577716 15230864 |
|---|