Journal
FEBS LETTERS
Volume 582, Issue 2, Pages 327-331Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.12.025
Keywords
soluble guanylate cyclase; cGMP; hsp90; proteasome; nitric oxide
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Endothelium-derived nitric oxide (NO) activates the heterodimeric heme protein soluble guanylate cyclase (sGC) to form cGMP. In different disease states, sGC levels and activity are diminished possibly involving the sGC binding chaperone, heat shock protein 90 (hsp90). Here we show that prolonged hsp90 inhibition in different cell types reduces protein levels of both sGC subunits by about half, an effect that was prevented by the proteasome inhibitor MG132. Conversely, acute hsp90 inhibition affected neither basal nor NO-stimulated sGC activity. Thus, hsp90 is a molecular stabilizer for sGC tonically preventing proteasomal degradation rather than having a role in short-term activity regulation. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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