TAILIEUCHUNG - Báo cáo khoa học: Cardiac troponin C-L29Q, related to hypertrophic cardiomyopathy, hinders the transduction of the protein kinase A dependent phosphorylation signal from cardiac troponin I to C

We investigated structural and functional aspects of the first mutation in TNNC1, coding for the calcium-binding subunit (cTnC) of cardiac tropo-nin, which was detected in a patient with hypertrophic cardiomyopathy [Hoffmann B, Schmidt-Traub H, Perrot A, Osterziel KJ & Gessner R (2001) Hum Mut17, 524]. This mutation leads to a leucine–glutamine exchange at position 29 in the nonfunctional calcium-binding site of cTnC. | ềFEBS Journal Cardiac troponin C-L29Q related to hypertrophic cardiomyopathy hinders the transduction of the protein kinase A dependent phosphorylation signal from cardiac troponin I to C Anja Schmidtmann1 Christopher Lindow1 Sylvie Villard2 Arnd Heuser3 Andreas Mugge1 Reinhard GeBner3 Claude Granier2 and Kornelia Jaquet1 1 Herz- und Kreislaufzentrum der Ruhr-Universitat Bochum Bergmannsheil Forschungslabor Molekulare Kardiologie Bochum Germany 2 Centre de Pharmacologie et Biotechnologie pour la sante Faculte de Pharmacie Montpellier France 3 Charite Campus Virchow-Klinikum Institut fur Laboratoriumsmedizin und Pathobiochemie Berlin Germany Keywords cTnC-L29Q hypertrophic cardiomyopathy human cardiac troponin I phosphorylation peptide arrays Correspondence K. Jaquet Herz- und Kreislaufzentrum der Ruhr-Universitat Bochum Bergmannsheil Forschungslabor Molekulare Kardiologie St Josef-Hospital Gudrunstr. 56 44791 Bochum Germany Fax 49 234 509 2363 Tel 49 234 509 2722 E-mail Received 24 June 2005 revised 21 September 2005 accepted 3 October 2005 doi We investigated structural and functional aspects of the first mutation in TNNC1 coding for the calcium-binding subunit cTnC of cardiac troponin which was detected in a patient with hypertrophic cardiomyopathy Hoffmann B Schmidt-Traub H Perrot A Osterziel KJ Gessner R 2001 Hum Mut 17 524 . This mutation leads to a leucine-glutamine exchange at position 29 in the nonfunctional calcium-binding site of cTnC. Interestingly the mutation is located in a putative interaction site for the nonphosphorylated N-terminal arm of cardiac troponin I cTnl Finley NL Abbott MB Abusamhadneh E Gaponenko V Dong W Seabrook G Howarth JW Rana M Solaro RJ Cheung HC et al. 1999 FEBS Lett 453 107-112 . According to peptide array experiments the nonphosphorylated cTnI arm interacts with cTnC around L29. This interaction is almost abolished by L29Q as observed upon protein kinase .

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