Tropomyosin 3 expression leads to hypercontractility and attenuates myofilament length-dependent Ca activation
نویسندگان
چکیده
KATHY PIEPLES,1 GRACE ARTEAGA,5 R. JOHN SOLARO,5 INGRID GRUPP,2 JOHN N. LORENZ,3 GREG P. BOIVIN,4 GANAPATHY JAGATHEESAN,1 ERIN LABITZKE,1 PIETER P. DETOMBE,5 JOHN P. KONHILAS,5 THOMAS C. IRVING,6 AND DAVID F. WIECZOREK1 1Department of Molecular Genetics, Biochemistry, and Microbiology, 2Department of Pharmacology and Cell Biophysics, 3Department of Molecular and Cellular Physiology, 4Department of Pathology and Laboratory Medicine, College of Medicine, University of Cincinnati, Cincinnati, Ohio 45267-0529; 5Department of Physiology and Biophysics, College of Medicine, University of Illinois, Chicago, 60612; and 6Center for Synchrotron Radiation Research and Instrumentation and Department of Biological, Chemical, and Physical Sciences, Illinois Institute of Technology, Chicago, Illinois 60616
منابع مشابه
Tropomyosin 3 expression leads to hypercontractility and attenuates myofilament length-dependent Ca(2+) activation.
Tropomyosin (TM), an integral component of the thin filament, is encoded by three striated muscle isoforms: alpha-TM, beta-TM, and TPM 3. Although the alpha-TM and beta-TM isoforms are well characterized, less is known about the function of the TPM 3 isoform, which is predominantly found in the slow-twitch musculature of mammals. To determine its functional significance, we ectopically expresse...
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