Cysteine S-Nitrosylation Protects Protein-tyrosine Phosphatase 1B against Oxidation-induced Permanent Inactivation
نویسندگان
چکیده
منابع مشابه
Protein tyrosine phosphatase 1B deficiency in podocytes protects against hyperglycemia-induced renal injury
Diabetic nephropathy is one of the most devastating complications of diabetes, and growing evidence implicates podocyte dysfunction in disease pathogenesis. Protein tyrosine phosphatase 1B (PTP1B; encoded by PTPN1) is an established metabolic regulator in vivo but its metabolic functions in podocytes remains unexplored. To that end, we generated podocyte-specific PTP1B knockout (pod-PTP1B KO) m...
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OBJECTIVE Cardiovascular dysfunction is a major cause of mortality in patients with sepsis. Recently, we showed that gene deletion or pharmacological inhibition of protein tyrosine phosphatase 1B (PTP1B) improves endothelial dysfunction and reduces the severity of experimental heart failure. However, the cardiovascular effect of PTP1B invalidation in sepsis is unknown. Thus, we explored the ben...
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Singlet oxygen ((1)O(2)), an electronically excited form of molecular oxygen, is a mediator of biological effects of ultraviolet A radiation, stimulating signaling cascades in human cells. We demonstrate here that (1)O(2) generated by photosensitization or by thermodecomposition of 3,3'-(1,4-naphthylidene)dipropionate-1,4-endoperoxide inactivates isolated protein tyrosine phosphatases (PTPases)...
متن کاملOxidative inactivation of protein tyrosine phosphatase 1B by organic hydroperoxides.
Protein tyrosine phosphatases (PTPs) are cysteine-dependent enzymes that play a central role in cell signaling. Organic hydroperoxides cause thiol-reversible, oxidative inactivation of PTP1B in a manner that mirrors the endogenous signaling agent hydrogen peroxide.
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As most intracellular signaling takes place via cascades of phosphorylation and dephosphorylation of tyrosines, protein tyrosine phosphatases have emerged as new and promising targets. Among them, protein tyrosine phosphatase 1B (PTP1B) negatively regulates insulin signaling by dephosphorylation of key tyrosine residues within the regulatory domain of the β-subunit of the insulin receptor, ther...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2008
ISSN: 0021-9258
DOI: 10.1074/jbc.m805287200