| Title | Interaction between hsp90 and soluble guanylate cyclase: physiological significance and mapping of the domains mediating binding | |
| Author | C. Gerasimou1, Z. Zhou1, C. Roussos1 and A. Papapetropoulos1,2
1G.P. Livanos and M. Simou Laboratories, Evangelismos Hospital, Critical Care Department, University of Athens School of Medicine and 2Department of Molecular Pharmacology, School of Pharmacy, University of Patras, Patra, Greece |
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| Citation | Gerasimou, C., Zhou, Z., Roussos, C. and Papapetropoulos, A.: Interaction between hsp90 and soluble guanylate cyclase: physiological significance and mapping of the domains mediating binding, Epitheorese Klin. Farmakol. Farmakokinet. 18(1): 112-114 (2004) | |
| Publication Date | Accepted for publication: 2004 | |
| Full Text Language | English | |
| Order – Buy | Ηλεκτρονική Μορφή: pdf (10 €) – Digital Type: pdf (10 €) pharmakonpress[at]pharmakonpress[.]gr | |
| Keywords | Hsp90, Soluble Guanylate Cyclase, sGC, protein levels | |
| Other Terms | review article | |
| Summary | Heat shock protein 90 (hsp90) regulates stability and function of many client proteins including members of the NO-cGMP signaling pathway. Soluble guanylate cyclase (sGC), which is the main intracellular receptor of NO, was recently reported to be an hsp90 interacting partner; however, the interaction between the two proteins remains to be characterized and functionally evaluated, in the present study, we show that hsp90 binds to both subunits of the most commonly found sGC isoform, α1β1. Characterization of the region of hsp90 required to bind each subunit in immuno-precipitation experiments, revealed that residues 310-456 of hsp90 interact with both a1 and β1. The region of 01 responsible for binding to hsp90 was mapped in in vitro binding assays and was found to lie between residues 200-408. The importance of the hsp90- sGC interaction was investigated by treating rat smooth muscle cells (RASMC) with the hsp90 inhibitors radicicoi (RAD) and geldanamycin (GA) for 1, 24 and 48hours and determining both sGC activity and protein levels. Long-term (24 or 48 hr) inhibition of hsp90 resulted in a strong decrease of both α1 and β1 protein levels, as well as sGC activity. | |
| References | 1. Pratt W.B., Toft D.O.: Exp. Biol. Med. 228: 111-133 (2003)
2. Hobbs A.J.: Trends Pharmacol. Sci. 1&. 484-491 (1997) 3. Nedvetsky P.I., Sessa W.C., Schmidt H.H.: PNAS 99:16510-16512 (2002) 4. Venema R.C., et al.: Am. J. Physiol. Heart Circ. Physiol. 285: H669-678 (2003) |
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| Relative Papers |
Online ISSN 1011-6575
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Articles published in this Journal are Indexed or Abstracted in: • Chemical Abstracts • Elsevier’s Bibliographic Databases: Scopus, EMBASE, EMBiology, Elsevier BIOBASE SCImago Journal and Country Rank Factor
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