Interactions between cell surface protein disulphide isomerase and S-nitrosoglutathione during nitric oxide delivery
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چکیده
منابع مشابه
Platelet cell-surface protein disulphide-isomerase mediated S-nitrosoglutathione consumption.
S-nitrosothiols (RSNOs) regulate several aspects of platelet physiology including inhibition of activation, adhesion and aggregation. PDI (protein disulphide-isomerase) has recently been found to be localized to the cell surface, where it exhibits both disulphide-exchange and denitrosation activities. The disulphide-exchange activity of PDI has been linked to aspects of platelet aggregation. Th...
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What is it? Protein disulphide isomerase is an enzyme with two interrelated activities: as an oxidoreductase, it can catalyse the formation, reduction and isomerisation of disulphide bonds; and as a polypeptide binding protein, it can function as a molecular chaperone which assists the folding of polypeptides. Transient association of PDI with nascent polypeptides during their folding prevents ...
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Since thiols can undergo nitrosation and the cell membrane is rich in thiol-containing proteins, we considered the possibility that membrane surface thiols may regulate cellular entry of NO. Recently, protein disulfide isomerase (PDI), a protein that catalyzes thio-disulfide exchange reactions, has been found on the cell-surface membrane. We hypothesized that cell-surface PDI reacts with NO, ca...
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Disulphide bonds are found in practically every class of extracellular protein, and the formation of disulphide bonds must be regarded as a key post-translational modification of secretory proteins. Despite this, and despite the fact that the existence of disulphide bonds has been known for many years, the mechanism of disulphide bond formation during protein biosynthesis and secretion is not w...
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Protein disulphide-isomerase can be partially purified from the high-speed-supernatant fraction of extensively disrupted chick-embryo tendon tissue. The catalytic properties of the preparation resemble those of the enzyme from mammalian liver. Gel electrophoresis and isoelectric focusing show the enzyme to be very acidic, with pI 4.4 +/- 0.3. Gel filtration indicates an Mr for the active enzyme...
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ژورنال
عنوان ژورنال: Nitric Oxide
سال: 2007
ISSN: 1089-8603
DOI: 10.1016/j.niox.2006.08.001