%0 Journal Article %1 Louk_1998_251 %A Loukianov, E. %A Ji, Y. %A Baker, D. L. %A Reed, T. %A Babu, J. %A Loukianova, T. %A Greene, A. %A Shull, G. %A Periasamy, M. %D 1998 %J Ann. N. Y. Acad. Sci. %K 10603953 ATPase, Animals, Chains, Contraction, Heart, Heavy Humans, Isoenzymes, Mice, Muscle, Myocardia, Myocardium, Myosin Reticulum, Sarcoplasmic Skeletal, Transgenic, l {C}a$^{2+}$-Transporting %P 251--259 %T Sarco(endo)plasmic reticulum Ca$^2+$ ATPase isoforms and their role in muscle physiology and pathology. %U http://www.annalsnyas.org/cgi/content/full/853/1/251 %V 853 %X Recent studies suggest that SR Ca$^2+$ transport function is altered in hypertrophied and failing myocardium. To understand whether alterations in SR Ca$^2+$ ATPase levels affect myocardial contractility, we generated transgenic mice that specifically overexpress SERCA2a or SERCA1 pump in the mouse heart, using the cardiac alpha-MHC promoter. Analysis of SERCA2a transgenic mice show both an increase in mRNA and protein levels (120-150\% of the wild type). Isolated work performing heart preparations revealed that SERCA2a mice have improved myocardial performance. On the other hand, SERCA1 overexpression in the heart resulted in isoform replacement without any change in total SERCA protein. Interestingly, SERCA1 transgenic hearts exhibited super contractility with a significant increase in rates of muscle contraction (+dp/dt) and relaxation (-dp/dT). The time to peak pressure and half-time to relaxation were significantly shorter.

@article{Louk_1998_251, abstract = {Recent studies suggest that SR {C}a$^{2+}$ transport function is altered in hypertrophied and failing myocardium. To understand whether alterations in SR {C}a$^{2+}$ ATPase levels affect myocardial contractility, we generated transgenic mice that specifically overexpress SERCA2a or SERCA1 pump in the mouse heart, using the cardiac alpha-{MHC} promoter. Analysis of SERCA2a transgenic mice show both an increase in m{RNA} and protein levels (120-150\% of the wild type). Isolated work performing heart preparations revealed that SERCA2a mice have improved myocardial performance. On the other hand, SERCA1 overexpression in the heart resulted in isoform replacement without any change in total SERCA protein. Interestingly, SERCA1 transgenic hearts exhibited super contractility with a significant increase in rates of muscle contraction (+dp/dt) and relaxation (-dp/dT). The time to peak pressure and half-time to relaxation were significantly shorter.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Loukianov, E. and Ji, Y. and Baker, D. L. and Reed, T. and Babu, J. and Loukianova, T. and Greene, A. and Shull, G. and Periasamy, M.}, biburl = {https://www.bibsonomy.org/bibtex/25dd79179c0745dfa276db0324a7929a2/hake}, description = {The whole bibliography file I use.}, file = {Louk_1998_251.pdf:Louk_1998_251.pdf:PDF}, interhash = {b5f5df6c774d4a2d3e1a2355ae87083a}, intrahash = {5dd79179c0745dfa276db0324a7929a2}, journal = {Ann. N. Y. Acad. Sci.}, key = 118, keywords = {10603953 ATPase, Animals, Chains, Contraction, Heart, Heavy Humans, Isoenzymes, Mice, Muscle, Myocardia, Myocardium, Myosin Reticulum, Sarcoplasmic Skeletal, Transgenic, l {C}a$^{2+}$-Transporting}, month = Sep, pages = {251--259}, pmid = {10603953}, timestamp = {2009-06-03T11:21:21.000+0200}, title = {Sarco(endo)plasmic reticulum {C}a$^{2+}$ ATPase isoforms and their role in muscle physiology and pathology.}, url = {http://www.annalsnyas.org/cgi/content/full/853/1/251}, volume = 853, year = 1998 }