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Sarco(endo)plasmic Reticulum Ca 2+ ATPase Isoforms and Their Role in Muscle Physiology and Pathology
Author(s) -
LOUKIANOV EVGENY,
JI YONG,
BAKER DEBRA L.,
REED THOMAS,
BABU JEGADEESH,
LOUKIANOVA TANYA,
GREENE ADAM,
SHULL GARY,
PERIASAMY MUTHU
Publication year - 1998
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1998.tb08273.x
Subject(s) - contractility , serca , gene isoform , medicine , genetically modified mouse , endocrinology , contraction (grammar) , phospholamban , transgene , heart failure , atpase , muscle contraction , chemistry , cardiac muscle , biology , biochemistry , enzyme , gene
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 α‐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.