TAILIEUCHUNG - Báo cáo khoa học: Homologous desensitization of guanylyl cyclase A, the receptor for atrial natriuretic peptide, is associated with a complex phosphorylation pattern

Atrial natriuretic peptide (ANP), via its guanylyl cyclase A (GC-A) recep-tor and intracellular guanosine 3¢,5¢-cyclic monophosphate production, is critically involved in the regulation of blood pressure. In patients with chronic heart failure, the plasma levels of ANP are increased, but the car-diovascular actions are severely blunted, indicating a receptor or postrecep-tor defect. | Homologous desensitization of guanylyl cyclase A the receptor for atrial natriuretic peptide is associated with a complex phosphorylation pattern Juliane Schroter1 Rene P. Zahedi2 Michael Hartmann1 Birgit GaBner1 Alexandra Gazinski1 Jens Waschke3 Albert Sickmann2 4 and Michaela Kuhn1 1 Institute of Physiology University of Wurzburg Germany 2 Institute for AnalyticalSciences Dortmund Germany 3 Institute of Anatomy University of Wurzburg Germany 4 Medizinisches Proteom-Center Ruhr-University Bochum Germany Keywords atrialnatriuretic peptide cyclic GMP guanylylcyclase A mass spectrometry phosphorylation Correspondence M. Kuhn Institute of Physiology University of Wurzburg Rontgenring 9 97070 Wurzburg Germany Fax 49 931 31 82741 Tel 49 931 31 82721 E-mail . Re-use of this article is permitted in accordance with the Terms and Conditions set out at http . com authorresources Received 25 January 2010 revised 13 March 2010 accepted 17 March 2010 doi Atrial natriuretic peptide ANP via its guanylyl cyclase A GC-A receptor and intracellular guanosine 3 5 -cyclic monophosphate production is critically involved in the regulation of blood pressure. In patients with chronic heart failure the plasma levels of ANP are increased but the cardiovascular actions are severely blunted indicating a receptor or postreceptor defect. Studies on metabolically labelled GC-A-overexpressing cells have indicated that GC-A is extensively phosphorylated and that ANP-induced homologous desensitization of GC-A correlates with receptor dephosphorylation a mechanism which might contribute to a loss of function in vivo. In this study tandem MS analysis of the GC-A receptor expressed in the human embryonic kidney cell line HEK293 revealed unambiguously that the intracellular domain of the receptor is phosphorylated at multiple residues Ser487 Ser497 Thr500 Ser502 Ser506 Ser510 and Thr513. MS .

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