نتایج جستجو برای: myosin light chain kinase

تعداد نتایج: 898607  

Journal: :The Journal of biological chemistry 1983
J A Hammer J P Albanesi E D Korn

In previous work from this laboratory, a partially purified protein kinase from the soil amoeba Acanthamoeba castellanii was shown to phosphorylate the heavy chain of the two single-headed Acanthamoeba myosin isoenzymes, myosin IA and IB, resulting in a 10- to 20-fold increase in their actin-activated Mg2+-ATPase activities (Maruta, H., and Korn, E.D. (1977) J. Biol. Chem. 252, 8329-8332). A my...

Journal: :Arteriosclerosis, thrombosis, and vascular biology 2017
Dianna M Milewicz Kathleen M Trybus Dong-Chuan Guo H Lee Sweeney Ellen Regalado Kristine Kamm James T Stull

The importance of maintaining contractile function in aortic smooth muscle cells (SMCs) is evident by the fact that heterozygous mutations in the major structural proteins or kinases controlling contraction lead to the formation of aneurysms of the ascending thoracic aorta that predispose to life-threatening aortic dissections. Force generation by SMC requires ATP-dependent cyclic interactions ...

2015
Masaya Taniguchi Ryuji Okamoto Masaaki Ito Itaru Goto Satoshi Fujita Katsuhisa Konishi Hideo Mizutani Kaoru Dohi David J. Hartshorne Takeo Itoh Agustín Guerrero-Hernandez

BACKGROUND & AIMS Cardiac myosin light chain kinase (cMLCK) plays an obligatory role in maintaining the phosphorylation levels of regulatory myosin light chain (MLC2), which is thought to be crucial for regulation of cardiac function. To test this hypothesis, the role played by ventricular MLC2 (MLC2v) phosphorylation was investigated in the phenylephrine-induced increase in twitch tension usin...

Journal: :The Journal of biological chemistry 1987
M Ikebe D J Hartshorne M Elzinga

Smooth muscle heavy meromyosin (HMM) is phosphorylated by the Ca2+-activated phospholipid-dependent protein kinase, i.e. protein kinase C, at three sites on each 20,000-dalton light chain. Phosphorylation of three sites also is observed with isolated 20,000-dalton light chain and HMM subfragment 1. The phosphorylation sites are serine 1, serine 2, and threonine 9. Threonine is phosphorylated mo...

Journal: :Blood 1991
M Higashihara K Takahata K Kurokawa

Human platelet myosin forms 10S and 6S conformations, and its Ca(2+)- and Mg(2+)-ATPase activities are parallel with the transition between 10S and 6S conformation, as judged by the gel filtration, intrinsic fluorescence, and viscosity methods. The 20,000-dalton myosin light chain (LC20) is phosphorylated by both myosin light chain kinase (MLC kinase) and Ca2+, phospholipid-dependent protein ki...

Journal: :The Biochemical journal 1986
B P Herring P J England

The rate of exchange of phosphate bound to ventricular myosin light chain-2 (LC2-P) was measured in rat hearts perfused with [32P]Pi at various levels of perfusate Ca2+. Computer simulations of the light-chain labelling suggested the presence of two isotopically distinct pools of LC2-P, one large pool comprising 90% of the total and a small pool consisting of the remaining 10%. At control level...

Journal: :American journal of physiology. Heart and circulatory physiology 2010
Tao Li Yuqiang Fang Guangming Yang Yu Zhu Jing Xu Liangming Liu

RhoA, an important member of the Rho family of GTPases, has been implicated in many cellular processes. Our pilot study found that RhoA participated in the regulation of vascular reactivity after shock, but the mechanism was incompletely understood. Whether RhoA regulates vascular reactivity through the Rho kinase-myosin light-chain phosphatase (MLCP) and Rac1-p21-activated kinase (PAK)-myosin ...

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