The effects of caldesmon on smooth muscle heavy actomeromyosin ATPase activity and binding of heavy meromyosin to actin.
作者： J A Lash , J R Sellers , D R Hathaway
DOI: 10.1016/S0021-9258(18)66691-8
关键词: Biochemistry 、 Caldesmon 、 ATPase 、 Calmodulin 、 Actin 、 Meromyosin 、 Heavy meromyosin 、 Biology 、 Binding protein 、 Phosphorylation
摘要: Caldesmon was purified to homogeneity from both chicken gizzard and bovine aortic smooth muscles. aorta slightly larger than caldesmon gizzards (Mr = 140,000) when the two were compared electrophoretically. bound tightly actin saturating at a molar ratio of 1 monomer per 6.6 monomers. Ca2+-calmodulin appeared reduce affinity for actin. also potent inhibitor heavy actomeromyosin ATPase activity producing maximal effect 7-10 This antagonized by Ca2+-calmodulin. While inhibited activity, it greatly enhanced binding unphosphorylated phosphorylated meromyosin in presence MgATP, reducing Kd factor 40 each form meromyosin. Although we did identify Ca2+-calmodulin-stimulated "caldesmon kinase" preparations under nondenaturing conditions, observed no phosphorylation (2 mol PO4/mol caldesmon) on capacity inhibit activity. Our results suggest that could serve some role muscle function enhancing cross-bridge while inhibiting actomyosin
sci-hub.st 参考文章(34)
W. T. Perrie, S. V. Perry, An electrophoretic study of the low-molecular-weight components of myosin Biochemical Journal. ,vol. 119, pp. 31- 38 ,(1970) , 10.1042/BJ1190031
J M Chalovich, E Eisenberg, Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin. Journal of Biological Chemistry. ,vol. 257, pp. 2432- 2437 ,(1982) , 10.1016/S0021-9258(18)34942-1
P K Ngai, C A Carruthers, M P Walsh, Isolation of the native form of chicken gizzard myosin light-chain kinase. Biochemical Journal. ,vol. 218, pp. 863- 870 ,(1984) , 10.1042/BJ2180863
P J Silver, J T Stull, Regulation of myosin light chain and phosphorylase phosphorylation in tracheal smooth muscle. Journal of Biological Chemistry. ,vol. 257, pp. 6145- 6150 ,(1982) , 10.1016/S0021-9258(20)65118-3
J R Haeberle, D R Hathaway, A A DePaoli-Roach, Dephosphorylation of myosin by the catalytic subunit of a type-2 phosphatase produces relaxation of chemically skinned uterine smooth muscle. Journal of Biological Chemistry. ,vol. 260, pp. 9965- 9968 ,(1985) , 10.1016/S0021-9258(17)39195-0
D Wallach, P J Davies, M C Willingham, M Yamaguchi, R M Robson, I Pastan, Filamin-actin interaction. Dissociation of binding from gelation by Ca2+-activated proteolysis. Journal of Biological Chemistry. ,vol. 253, pp. 4036- 4042 ,(1978) , 10.1016/S0021-9258(17)34795-6
J R Sellers, Mechanism of the phosphorylation-dependent regulation of smooth muscle heavy meromyosin. Journal of Biological Chemistry. ,vol. 260, pp. 15815- 15819 ,(1985) , 10.1016/S0021-9258(17)36331-7
P. Cassidy, P.E. Hoar, W.G. Kerrick, Irreversible thiophosphorylation and activation of tension in functionally skinned rabbit ileum strips by [35S]ATP gamma S. Journal of Biological Chemistry. ,vol. 254, pp. 11148- 11153 ,(1979) , 10.1016/S0021-9258(19)86642-5
J.R. Sellers, M.D. Pato, R.S. Adelstein, Reversible phosphorylation of smooth muscle myosin, heavy meromyosin, and platelet myosin. Journal of Biological Chemistry. ,vol. 256, pp. 13137- 13142 ,(1981) , 10.1016/S0021-9258(18)43018-9
P K Ngai, M P Walsh, Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon. Journal of Biological Chemistry. ,vol. 259, pp. 13656- 13659 ,(1984) , 10.1016/S0021-9258(18)89793-9