Abstract
Address: 1G.P. Livanos and M. Simou Laboratories, Evangelismos Hospital, Department of Critical Care and Pulmonary Services, University of Athens School of Medicine, Greece, 2Vascular Biology Center, Medical College of Georgia, Augusta, Georgia, USA, 3Department of Pharmacology and Program in Vascular Cell Signaling and Therapeutics, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut, USA and 4Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras, Greece
Highlights
Zongmin Zhou*1, Christina Gerassimou1, Richard C Venema2, Charis Roussos1, William C Sessa3, John Catravas2 and Andreas Papapetropoulos1,4
We show that hsp90 binds to both subunits of the most common Soluble guanylyl cyclase (sGC) form, α1β1
The physiological importance of the hsp90/sGC interaction was investigated by treating rat smooth muscle cells (RASMC) with the hsp90 inhibitors radicicol (RAD) and geldanamycin (GA) and determining both sGC activity and protein levels
Summary
Zongmin Zhou*1, Christina Gerassimou1, Richard C Venema2, Charis Roussos1, William C Sessa3, John Catravas2 and Andreas Papapetropoulos1,4. Interaction between hsp90 and soluble guanylyl cyclase: physiological significance and mapping of the domains mediating binding Email: Zongmin Zhou* - apapapet@upatras.gr * Corresponding author from 2nd International Conference of cGMP Generators, Effectors and Therapeutic Implications Potsdam, Germany, 10–12 June, 2005
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