Characterization of the Phosphoprotein Profile in Spontaneously Beating Cultured Rat Heart Cells
- 1 May 1982
- journal article
- research article
- Published by Frontiers Media SA in Experimental Biology and Medicine
- Vol. 170 (1) , 19-24
- https://doi.org/10.3181/00379727-170-41389
Abstract
Culture of neonatal rat hearts yields a fairly homogeneous population of synchronous and spontaneously beating myocardial cells. Incubation of the culture with 32Pi followed by polyacrylamide gel electrophoresis and autoradiography yields a reproducible profile of both high and low MW phosphoproteins. This phosphoprotein profile is clearly distinct from that observed with mesenchymal cells, the major contaminant of the heart cell cultures. By comparison with purified standard proteins and by copurification with neonatal rat myosin, one of these phosphoproteins was identified as the 20,000-dalton myosin L chain. The demonstration of phosphoproteins in intact contracting myocardial cells provides a system to study the complex interaction of the phosphoproteins involved in the control of cardiac contractility.This publication has 6 references indexed in Scilit:
- Heterogeneity of rat cardiac cells of defined origin in single cell cultureJournal of Molecular and Cellular Cardiology, 1980
- The Regulation of Contractile Activity in MuscleBiochemical Society Transactions, 1979
- A high molecular weight phosphoprotein in cultured fibroblasts that associates with polymerized tubulinExperimental Cell Research, 1978
- Characterization and regulation of heart adenosine 3':5'-monophosphate-dependent protein kinase isozymes.Journal of Biological Chemistry, 1977
- Studies on the phosphorylation of the inhibitory subunit of troponin during modification of contraction in perfused rat heartBiochemical Journal, 1976
- Myosin light-chain phosphataseBiochemical Journal, 1976