Abstract
Background Soluble guanylate cyclase (sGC) is the main receptor of nitric oxide (NO). NO binds to the ferrous heme moiety of sGC thus activating the enzyme and increasing cyclic GMP (cGMP) levels. sGC is inhibited by various oxidants which either convert ferrous heme to ferric suppressing NO binding or modify essential thiol groups of sGC. Certain heat shock proteins (Hsp) can protect the enzymes from this inactivation. Hence, we suggested that Hsp can block oxidant-induced inhibition of sGC.
Highlights
Soluble guanylate cyclase is the main receptor of nitric oxide (NO)
NO binds to the ferrous heme moiety of Soluble guanylate cyclase (sGC) activating the enzyme and increasing cyclic GMP levels. sGC is inhibited by various oxidants which either convert ferrous heme to ferric suppressing NO binding or modify essential thiol groups of sGC
The interaction of Hsp90 with sGC can be important for maintenance of NO-dependent cellular cyclic GMP (cGMP) synthesis in damaged tissues
Summary
Address: 1Department of Bioorganic Chemistry, School of Biology, Lomonosov Moscow State University, Moscow, Russia and 2Department of Integrative Biology and Pharmacology, University of Texas at Houston Medical School, Houston, Texas, USA. 2nd International Conference of cGMP Generators, Effectors and Therapeutic Implications Meeting abstracts
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