منابع مشابه
S-Nitrosylation of mitochondrial caspases
Caspase-3 is a cysteine protease located in both the cytoplasm and mitochondrial intermembrane space that is a central effector of many apoptotic pathways. In resting cells, a subset of caspase-3 zymogens is S-nitrosylated at the active site cysteine, inhibiting enzyme activity. During Fas-induced apoptosis, caspases are denitrosylated, allowing the catalytic site to function. In the current st...
متن کاملS-nitrosylation regulates mitochondrial quality control via activation of parkin
Parkin, a ubiquitin E3 ligase of the ring between ring fingers family, has been implicated in mitochondrial quality control. A series of recent reports have suggested that the recruitment of parkin is regulated by phosphorylation. However, the molecular mechanism that activates parkin to induce mitochondrial degradation is not well understood. Here, and in contrast to previous reports that S-ni...
متن کاملActin S-Nitrosylation Inhibits Neutrophil
The focus of this work was to elucidate the mechanism for inhibition of neutrophil 2 integrin adhesion molecules by hyperoxia. Results demonstrate that exposure to high oxygen partial pressures increases synthesis of reactive species derived from type 2 nitric-oxide synthase andmyeloperoxidase, leading to excessive S-nitrosylation of -actin and possibly profilin. Hyperoxia causes S-nitrosylatio...
متن کاملS-nitrosylation in cardiovascular signaling.
Well over 2 decades have passed since the endothelium-derived relaxation factor was reported to be the gaseous molecule nitric oxide (NO). Although soluble guanylyl cyclase (which generates cyclic guanosine monophosphate, cGMP) was the first identified receptor for NO, it has become increasingly clear that NO exerts a ubiquitous influence in a cGMP-independent manner. In particular, many, if no...
متن کاملProtein S-nitrosylation and cardioprotection.
Nitric oxide (NO) plays an important role in the regulation of cardiovascular function. In addition to the classic NO activation of the cGMP-dependent pathway, NO can also regulate cell function through protein S-nitrosylation, a redox dependent, thiol-based, reversible posttranslational protein modification that involves attachment of an NO moiety to a nucleophilic protein sulfhydryl group. Th...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2001
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.200104008