Title : Effects of S-glutathionylation and S-nitrosylation on calmodulin binding to triads and FKBP12 binding to type 1 calcium release channels.

Pub. Date : 2005 Jul-Aug

PMID : 15998242






3 Functional Relationships(s)
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1 In addition, we show that 35S-labeled 12-kDa FK506-binding protein ([35S]FKBP12) bound with a Kd of 13.1 nM to RyR1 present in triads or heavy sarcoplasmic reticulum vesicles; RyR1 S-nitrosylation by NOR-3 or GSNO, but not S-glutathionylation, specifically increased by four- to fivefold this Kd value. FK 409 ryanodine receptor 1 Homo sapiens
2 RyR1 S-glutathionylation (induced by GSH plus H2O2) or RyR1 S-nitrosylation (produced by NOR-3) increased by approximately six- or twofold, respectively, the Kd of apocalmodulin (apoCaM) or Ca2+-calmodulin (CaCaM) binding to triads. FK 409 ryanodine receptor 1 Homo sapiens
3 RyR1 S-glutathionylation (induced by GSH plus H2O2) or RyR1 S-nitrosylation (produced by NOR-3) increased by approximately six- or twofold, respectively, the Kd of apocalmodulin (apoCaM) or Ca2+-calmodulin (CaCaM) binding to triads. FK 409 ryanodine receptor 1 Homo sapiens