Diphosphorylation of myosin light chain in smooth muscle cells in culture

FEBS Letters

Komatsu, Ken-Ichi¹  Sasaki, Yasuharu¹  Seto, Minoni¹ 

[1] Biochemical Research Laboratory, Life Science Research Center, Asahi Chemical Industry, Co. Ltd., Asahi-machi 6-2700, Nobeoka, Miyazaki 882, Japan

关键词: Myosin light chain;    Protein kinase C;    Down-regulation;    Staurosporine;    Smooth muscle cell line;    MLC;    myosin light chain;    SM-3;    smooth muscle cell line;    MLCK;    myosin light chain kinase;    PGF2α;    prostaglandin F2α;    PDBu;    phorbol dibutyrate;    Str;    staurosporine;   

DOI  :  10.1016/0014-5793(90)80532-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Prostaglandin (PG) F_2α (30 μM) stimulated both monophosphorylation and diphosphorylation of myosin light chain (MLC) in a smooth muscle cell line (SM-3). The diphosphorylation was significantly decreased by treatment with the protein kinase C inhibitor staurosporine (30 nM, 30 min) from 20.1% of total MLC to 4.5%. The protein kinase C down-regulation treatment of SM-3 cells with phorbol dibutyrate suppressed to 8.7% the MLC diphosphorylation activity in the SM-3 cells. This down-regulation treatment had little effect on the monophosphorylation. We propose that the MLC diphosphorylation in PGF_2α-stimulated SM-3 cells in culture may be regulated through mechanisms sensitive to protein kinase C.

【 授权许可】

Unknown