نتایج جستجو برای: mlck

تعداد نتایج: 574  

Journal: :The Journal of Cell Biology 1991
A K Wilson G Gorgas W D Claypool P de Lanerolle

Myosin II purified from mammalian non-muscle cells is phosphorylated on the 20-kD light chain subunit (MLC20) by the Ca2+/calmodulin-dependent enzyme myosin light chain kinase (MLCK). The importance of MLC20 phosphorylation in regulating cell motility was investigated by introducing either antibodies to MLCK (MK-Ab) or a Ca2+/calmodulin-independent, constitutively active form of MLCK (MK-) into...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1984
W G Kerrick L Y Bourguignon

Several characteristics of receptor capping in lymphocyte membranes suggest similarities with mechanisms underlying control of contraction in smooth muscle fibers. Both capping and contraction are Ca2+ dependent and require metabolic energy. Contractile proteins such as actin and myosin are associated with the cap, as is calmodulin, which mediates the Ca2+ dependence of smooth muscle contractio...

Journal: :The Biochemical journal 2010
Olga V Shcherbakova Daria V Serebryanaya Alexander B Postnikov Mechthild M Schroeter Stefan Zittrich Angelika A Noegel Vladimir P Shirinsky Alexander V Vorotnikov Gabriele Pfitzer

KRP (kinase-related protein), also known as telokin, has been proposed to inhibit smooth muscle contractility by inhibiting the phosphorylation of the rMLC (regulatory myosin light chain) by the Ca2+-activated MLCK (myosin light chain kinase). Using the phosphatase inhibitor microcystin, we show in the present study that KRP also inhibits Ca2+-independent rMLC phosphorylation and smooth muscle ...

Journal: :Anesthesiology 2001
M Hanazaki K A Jones W J Perkins D O Warner

BACKGROUND Halothane relaxes airway smooth muscle, in part, by decreasing the force produced for a given intracellular [Ca(2+)] (i.e., Ca(2+) sensitivity) during muscarinic stimulation, an effect produced by a decrease in regulatory myosin light-chain (rMLC) phosphorylation. The authors tested the hypothesis that halothane reduces rMLC phosphorylation during muscarinic stimulation at constant i...

2002
David P. Wilson Cindy Sutherland Michael P. Walsh

Smooth muscle contraction is activated by phosphorylation of the 20-kDa light chains of myosin catalyzed by Ca /calmodulin (CaM)-dependent myosin light chain kinase (MLCK). According to popular current theory, the CaM involved in MLCK regulation is Ca -free and dissociated from the kinase at resting cytosolic free Ca concentration ([Ca ]i). An increase in [Ca 2 ]i saturates the four Ca -binding...

Journal: :Plant physiology 1989
D M Roberts

By using a synthetic peptide, KM-14, a protein kinase was detected and partially purified from Mougeotia sp. The peptide contains the sequence of the regulatory light chain of smooth muscle myosin that is phosphorylated by calcium-calmodulin-dependent myosin light chain kinase (MLCK). The Mougeotia kinase was stimulated 40-fold by calcium with half-maximal stimulation occurring at 1.5 micromola...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2016
Audrey N Chang Pravin Mahajan Stefan Knapp Hannah Barton H Lee Sweeney Kristine E Kamm James T Stull

The well-known, muscle-specific smooth muscle myosin light chain kinase (MLCK) (smMLCK) and skeletal muscle MLCK (skMLCK) are dedicated protein kinases regulated by an autoregulatory segment C terminus of the catalytic core that blocks myosin regulatory light chain (RLC) binding and phosphorylation in the absence of Ca(2+)/calmodulin (CaM). Although it is known that a more recently discovered c...

Journal: :The Journal of physiology 2003
A Wirth M Schroeter C Kock-Hauser E Manser J M Chalovich P De Lanerolle G Pfitzer

The p21-activated protein kinases (PAKs) have been implicated in cytoskeletal rearrangements and modulation of non-muscle contractility. Little, however, is known about the role of the PAK family members in smooth muscle contraction. Therefore, we investigated the effect of the predominant isoform in vascular smooth muscle cells, PAK1, on contraction and phosphorylation of the regulatory light ...

Journal: :The Journal of Cell Biology 2001
Kazuo Katoh Yumiko Kano Mutsuki Amano Hirofumi Onishi Kozo Kaibuchi Keigi Fujiwara

It is widely accepted that actin filaments and the conventional double-headed myosin interact to generate force for many types of nonmuscle cell motility, and that this interaction occurs when the myosin regulatory light chain (MLC) is phosphorylated by MLC kinase (MLCK) together with calmodulin and Ca(2+). However, recent studies indicate that Rho-kinase is also involved in regulating the smoo...

2016
Shoujiao Ye Zhenqiang Song Jing Li Chunshen Li Juhong Yang Bai Chang

In the study, type 2 diabetic rat model was established using streptozotocin (STZ) combined with a high-fat diet, and the rats were divided into control and diabetic groups. Diabetic groups were further divided into nonintervening, simvastatin, Didang Decoction (DDD) early-phase intervening, DDD mid-phase intervening, and DDD late-phase intervening groups. The expression level of MLCK was detec...

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