The phosphorylation of cardiac contractile proteins
作者： P. J. England , D. Mills , S. A. Jeacocke , H. T. Pask
DOI: 10.1007/978-3-642-85326-5_20
关键词:
摘要: Two contractile proteins, troponin-I and C-protein, are rapidly phosphorylated in perfused heart response to stimulation by catecholamines. Both only increases intracellular cyclic AMP, good substrates for AMP-dependent protein kinase vitro. The phosphorylation of decreases the affinity troponin complex Ca2+ increasing off-rate dissociation. This is probably part mechanism whereby catecholamines increase rate relaxation heart. C-protein vivo vitro on 4–5 sites, but function both its unknown. Myosin P-light chain (phosphorylated a Ca2+-dependent kinase) approximately 50 % control perfusions, this unchanged during acute inotropic interventions. However, perfusions with 32Pi indicate an active kinase/phosphatase couple, which may be fully under conditions.
springer.com
sci-hub.st 参考文章(27)
R Starr, G Offer, The interaction of C-protein with heavy meromyosin and subfragment-2. Biochemical Journal. ,vol. 171, pp. 813- 816 ,(1978) , 10.1042/BJ1710813
S A Jeacocke, P J England, Phosphorylation of myosin light chains in perfused rat heart. Effect of adrenaline and increased cytoplasmic calcium ions Biochemical Journal. ,vol. 188, pp. 763- 768 ,(1980) , 10.1042/BJ1880763
A J G Moir, R J Solaro, S V Perry, The site of phosphorylation of troponin I in the perfused rabbit heart. The effect of adrenaline. Biochemical Journal. ,vol. 185, pp. 505- 513 ,(1980) , 10.1042/BJ1850505
H.C. Hartzell, L. Titus, Effects of cholinergic and adrenergic agonists on phosphorylation of a 165,000-dalton myofibrillar protein in intact cardiac muscle. Journal of Biological Chemistry. ,vol. 257, pp. 2111- 2120 ,(1982) , 10.1016/S0021-9258(19)68153-6
S.P. Robertson, J.D. Johnson, M.J. Holroyde, E.G. Kranias, J.D. Potter, R.J. Solaro, The effect of troponin I phosphorylation on the Ca2+-binding properties of the Ca2+-regulatory site of bovine cardiac troponin. Journal of Biological Chemistry. ,vol. 257, pp. 260- 263 ,(1982) , 10.1016/S0021-9258(19)68355-9
Michael J. Holroyde, David A.P. Small, Elizabeth Howe, R.John Solaro, Isolation of cardiac myofibrils and myosin light chains with in vivo levels of light chain phosphorylation. Biochimica et Biophysica Acta. ,vol. 587, pp. 628- 637 ,(1979) , 10.1016/0304-4165(79)90014-X
E. Pires, S.V. Perry, M.A.W. Thomas, Myosin light-chain kinase, a new enzyme from striated muscle. FEBS Letters. ,vol. 41, pp. 292- 296 ,(1974) , 10.1016/0014-5793(74)81232-9
R. J. SOLARO, A. J. G. MOIR, S. V. PERRY, Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart Nature. ,vol. 262, pp. 615- 617 ,(1976) , 10.1038/262615A0
Kathleen Franks, James T. Stull, Roger Cooke, Myosin phosphorylation regulates the ATPase activity of permeable skeletal muscle fibers FEBS Letters. ,vol. 144, pp. 33- 37 ,(1982) , 10.1016/0014-5793(82)80563-2
The Location of C-Protein in Rabbit Skeletal Muscle Proceedings of The Royal Society B: Biological Sciences. ,vol. 192, pp. 451- 461 ,(1976) , 10.1098/RSPB.1976.0023