Myosin light chain kinases
نویسندگان
چکیده
منابع مشابه
Phosphorylation of Mammalian Myosin Light Chain Kinases
The phosphorylation of the calmodulin-dependent enzyme myosin light chain kinase, purified from bovine tracheal smooth muscle and human blood platelets, by the catalytic subunit of CAMP-dependent protein kinase and by cGMP-dependent protein kinase was investigated. When myosin light chain kinase which has calmodulin bound is phosphorylated by the catalytic subunit of CAMP-dependent protein kina...
متن کاملAlterations in expression of myosin and myosin light chain kinases in response to vascular injury.
Histochemical analysis of balloon-injured rat carotid arteries revealed a coordinated expression of nonmuscle myosin heavy chain-A and -B (NM-A and NM-B) in response to injury. Expression of these nonmuscle myosin forms shifts from the media to the adventitia and intima. In contrast, expression of smooth muscle myosin heavy chain-1 (SM-1) within the media is not altered, whereas smooth muscle m...
متن کاملMyosin light-chain phosphatase.
1. A method for the isolation of a new enzyme, myosin light-chain phosphatase, from rabbit white skeletal muscle by using a Sepharose-phosphorylated myosin light-chain affinity column is described. 2. The enzyme migrated as a single component on electrophoresis in sodium dodecyl sulphate/polyacrylamide gel at pH7.0, with apparent mol.wt. 70000. 3. The enzyme was highly specific for the phosphor...
متن کاملMyosin light-chain kinase of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain.
Myosin light-chain kinase (MLCK) of smooth muscle is multifunctional, being composed of N-terminal actin-binding domain, central kinase domain, and C-terminal myosin-binding domain. The kinase domain is the best characterized; this domain activates the interaction of smooth-muscle myosin with actin by phosphorylating the myosin light chain. We have recently shown that the Met-1-Pro-41 sequence ...
متن کاملEffects of relaxin on rat uterine myosin light chain kinase activity and myosin light chain phosphorylation.
Isometrically suspended uteri from estrogen-primed rats were stimulated with prostaglandin F2 alpha and then exposed to relaxin. Relaxin-dependent decreases in the ratio of phosphorylated to total myosin light chains (MLC) and in MLC kinase activity, measured in the presence of 0.5 mg/ml of uterine myosin and the absence and presence of Ca2+-calmodulin (CaM), were observed. The time-course and ...
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ژورنال
عنوان ژورنال: Cell Adhesion & Migration
سال: 2009
ISSN: 1933-6918,1933-6926
DOI: 10.4161/cam.3.3.8212