Literature DB >> 3160691

Phosphorylation of myosin light chain and the actin-activated ATPase activity of adrenal medullary myosin.

K Kanda, K Sobue, S Kakiuchi.   

Abstract

Myosin light chain kinase was partially purified from bovine adrenal medulla. A polypeptide of Mr 165,000 dalton was identified as kinase by using anti-gizzard myosin light chain kinase IgG on immunoreplica. Phosphorylation of medullary myosin was Ca2+- and calmodulin-dependent. The phosphorylated myosin was showed to enhance the actin-activated Mg2+-ATPase activity. In contrast, the myosin ATPase activity was dramatically decreased by dephosphorylation of myosin.

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Year:  1985        PMID： 3160691     DOI： 10.1093/oxfordjournals.jbchem.a135138

Source DB:  PubMed          Journal:  J Biochem        ISSN： 0021-924X            Impact factor:   3.387


  3 in total

1.  Naphthalenesulfonamide derivatives ML9 and W7 inhibit catecholamine secretion in intact and permeabilized chromaffin cells.

Authors:  J A Reig; S Viniegra; J J Ballesta; M Palmero; L M Guitierrez
Journal:  Neurochem Res       Date:  1993-03       Impact factor: 3.996

2.  Phosphorylation of myosin light chain from adrenomedullary chromaffin cells in culture.

Authors:  L M Gutierrez; M J Hidalgo; M Palmero; J J Ballesta; J A Reig; A G Garcia; S Viniegra
Journal:  Biochem J       Date:  1989-12-01       Impact factor: 3.857

3.  Rho kinase inhibitors stimulate the migration of human cultured osteoblastic cells by regulating actomyosin activity.

Authors:  Xuejiao Zhang; Cheng Li; Huiling Gao; Hiroaki Nabeka; Tetsuya Shimokawa; Hiroyuki Wakisaka; Seiji Matsuda; Naoto Kobayashi
Journal:  Cell Mol Biol Lett       Date:  2011-03-09       Impact factor: 5.787
  3 in total

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