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386 results on '"Vassort, G."'

12. Abstracts of the XVIII European Conference on Muscle and Motility: De Blije Werelt, Lunteren, The Netherlands September 12–16, 1989

Author

Nesterov, V. P., Peiper, U., Hiller, J., Krienke, B., Schüttler, K., Szymanski, C., Bottinelli, R., Cappelli, V., Minelli, R., Reggiani, C., Schiaffino, S., Carlhoff, D., D'Haese, J., Dabrowska, R., Nowak, E., Borovikov, Y. S., Cummins, P., Russell, G., McLoughlin, D., Cummins, B., Bonet, A., Harricane, M. C., Audemard, E., Mornet, D., Ropert, S., Cavaillé, F., Redwood, C. S., Bryan, J., Cross, R. A., Kendrick-Jones, J., Marston, S. B., Taggart, M., Marston, S., Makuch, R., Stokarska, G., Dabrowska, R., Cecchi, G., Colomo, F., Poggesi, C., Tesi, C., Puceat, M., Clement, O., Lechene, P., Pelosin, J. -M., Ventura-Clapter, R., Vassort, G., Fischer, W., Pfitzer, G., Ankrett, R. J., Rowe, A. J., Bagshaw, C. R., Perry, S. V., Hebisch, S., Levine, B., Moir, A. J. G., Leszyk, J., Derancourt, J., Patcheil, V., Cavadore, C., Collins, J. H., Swiderek, K., Jaquet, K., Mittmann, K., Meyer, H. E., Heilmeyer, Jr, L. M. J., Travers, F., Barman, T., Duvert, M., Grandier-Vazeille, X., Verna, A., Dan-Goor, M., Mühlrad, A., Muhlrad, A., Polzar, B., Kießling, P., Mannherz, H. G., Lehmann-Klose, S., Gröschel-Stewart, U., Bettache, N., Bertrand, R., Kassab, R., Roulet, A., Cardinaud, R., Harford, J. J., Squire, J. M., Maeda, Y., Chew, M. W. K., Huber, Pia, Schaub, Marcus C., Pierobon-Bormioli, S., Betto, R., Ceoldo, S., Salviati, G., Martinez, I., Ofstad, R., Olsen, R. L., Trinick, J., Barlow, D., Gautel, M., Gibson, T., Labeit, S., Leonard, K., Wardale, J., Whiting, A., Draeger, A., Barth, M., Herzog, M., Gimona, M., Small, J. V., Stelzer, E., Amos, B., Ikebe, M., Bernengo, J. C., Rinne, Bettina, Wray, John S., Poole, K. J. V., Goody, R. S., Thomas, Daniel, Rowe, Arthur, Schröder, R. R., Hofmann, W., Müller, U. C., Menetret, J. -F., Wray, J. S., Lakey, A., Tichelaar, W., Ferguson, C., Bullard, B., Kabsch, W., Pai, E. F., Suck, D., Holmes, K. C., Jarosch, Robert, van Mastrigt, R., Pollack, Gerald H., Horowitz, Arie, Anderl, R., Kuhn, H. J., Burton, K., Jung, D. W. G., Blangé, T., Treijtel, B. W., Bagni, M. A., Garzella, P., Huxley, A. F., Beckers-Bleukx, G., Maréchal, G., Bershitsky, S. Y., Tsaturyan, A. K., Woodward, S. K. A., Eccleston, J. F., Geeves, M. A., Knight, Peter, Fortune, Neil, Geeves, Mike, Arner, A., Arheden, H., Lombardi, V., Piazzesi, G., Stienen, G. J. M., Elzinga, G., de Beer, E. L., van Buuren, K. J. H., ten Kate, Y. J., Grundeman, R. L. F., Schiereck, P., Trombitas, K., Versteeg, P. G. A., Rowe, Arthur J., Bolger, Paul, van der Laarse, W. J., Diegenbach, P. C., Flitney, F. W., Jones, D. A., Hatfaludy, S., Shansky, J., Smiley, B., Vandenburgh, H. H., de Haan, A., Lodder, M. A. N., Berquin, A., Lebacq, J., Curtin, N. A., Woledge, R. C., Hellstrand, P., Lönnbro, P., Wadsö, I., Lammertse, T. S., Zaremba, R., Daut, J., Woledge, R. C., Kushmerick, M. J., McFarland, E., Lyons, G. E., Sassoon, D., Ontell, M., and Buckingham, M. E.

Published
1990
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15. Cardiac alpha1-adrenoceptors mediate positive inotropy via myofibrillar sensitization

Author

Puceat, M., Terzic, A., Clement, O., Scamps, F., Vogel, S.M., and Vassort, G.

Subjects
Sympathomimetic agents -- Research, Cardiotonic agents -- Research, Adrenergic mechanisms, Calcium channels, Biological sciences, Chemistry, Pharmaceuticals and cosmetics industries
Abstract

Alpha1-adrenoceptor agonists have advantages over standard cardiac inotropic agents because these sensitize myofibrils via a receptor-mediated mechanism. Alpha1-adrenoceptor stimulation enhances myocardial contraction without producing adverse rhythmic effects and calcium overload by increasing sensitiviity to calcium influx. This may be due to alkalinization of the intracellular pH and consequent increase in alkaline phosphatase-sensitive phosphorylation. The focus of cardiac pharmacology now centers on the phosphoinositol and adrenergic pathways in muscular contraction.

Published
1992

16. Impaired modulation of the cardiac L-type Ca2+ channel activity by ahnak-1 after myocardial infarction

Author

Alvarez Gonzalez, J., Haase, H., Vassort, G., and Morano, I.

Subjects
lcsh:Internal medicine, lcsh:Diseases of the circulatory (Cardiovascular) system, Cardiovascular and Metabolic Diseases, lcsh:RC666-701, ahnak-1, calcium channels, patch-clamp, heart, cardiomyocytes, myocardial infarction, lcsh:RC31-1245
Abstract

Introduction: The L-type cardiac Ca2+ channel (Cav 1.2) is an important determinant of cardiac repolarization and the main source of activator Ca2+ during excitation-contraction coupling in cardiac cells. Its defective regulation is a major cause of arrhythmias and contractile dysfunction. We have recently shown that the cytoskeletal protein ahnak-1 modulates Ca2+ current through Cav 1.2 channels (ICaL) by interacting with the regulatory beta-subunit of the Cav 1.2 channel and that the genetic variant of ahnak-1 I5483T (previously Ile5236Thr), interferes with the beta-adrenergic stimulation of ICaL. Objective: To extend our study of the I5483T variant to ventricular cardiomyocytes dissociated from remodelled infarcted rat hearts (PMI). Methods: The patch-clamp technique was used to record ICaL from enzymatically dissociated ventricular cardiomyocytes from young (2-month-old) and six-month-old sham-operated and PMI rats. Results: Basal ICaL was increased from 11 ± 0.5 A/F in young cardiomyocytes to 14.6 ± 1.1 A/F and 15.7 ± 1 A/F in sham and PMI cardiomyocytes respectively, while isoprenaline (ISO, 1 µmol/L) further increased ICaL by 101 ± 6%, 109 ± 10% and 104 ± 12% respectively. When cells were intracellularly perfused with a peptide containing the mutated ahnak-1 sequence (10 µmol/L) basal ICaL was increased to 20 ± 1 A/F, 22 ± 2 A/F and 21 ± 2 A/F in young, sham and PMI cardiomyocytes respectively. In these cells ISO increased ICaL by 11 ± 4%, 33 ± 6% and 79 ± 12% respectively. Conclusion: Modulation of ICaL by ahnak-1is impaired by myocardial ischemia and remodelling. Since ahnak-1 and Cav 1.2 channels co-localize in the transverse T-tubule system, remodelling of T-tubules could affect the interaction of ahnak-1 with the regulatory beta subunit of these channels.

Published
2012

24. Ahnak1 modulates L-type Ca(2+) channel inactivation of rodent cardiomyocytes

Author

Alvarez, J.L., Petzhold, D., Pankonien, I., Behlke, J., Kouno, M., Vassort, G., Morano, I., and Haase, H.

Subjects
Cardiovascular and Metabolic Diseases
Abstract

Ahnak1, a giant 700 kDa protein, has been implicated in Ca(2+) signalling in various cells. Previous work suggested that the interaction between ahnak1 and Cavbeta(2) subunit plays a role in L-type Ca(2+) current (I (CaL)) regulation. Here, we performed structure-function studies with the most C-terminal domain of ahnak1 (188 amino acids) containing a PxxP consensus motif (designated as 188-PSTP) using ventricular cardiomyocytes isolated from rats, wild-type (WT) mice and ahnak1-deficient mice. In vitro binding studies revealed that 188-PSTP conferred high-affinity binding to Cavbeta(2) (K (d) approximately 60 nM). Replacement of proline residues by alanines (188-ASTA) decreased Cavbeta(2) affinity about 20-fold. Both 188-PSTP and 188-ASTA were functional in ahnak1-expressing rat and mouse cardiomyocytes during whole-cell patch clamp. Upon intracellular application, they increased the net Ca(2+) influx by enhancing I (CaL) density and/or increasing I (CaL) inactivation time course without altering voltage dependency. Specifically, 188-ASTA, which failed to affect I (CaL) density, markedly slowed I (CaL) inactivation resulting in a 50-70% increase in transported Ca(2+) during a 0 mV depolarising pulse. Both ahnak1 fragments also slowed current inactivation with Ba(2+) as charge carrier. By contrast, neither 188-PSTP nor 188-ASTA affected any I (CaL) characteristics in ahnak1-deficient mouse cardiomyocytes. Our results indicate that the presence of endogenous ahnak1 is required for tuning the voltage-dependent component of I (CaL) inactivation by ahnak1 fragments. We suggest that ahnak1 modulates the accessibility of molecular determinants in Cavbeta(2) and/or scaffolds selectively different beta-subunit isoforms in the heart.

Published
2010

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