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Regulation of Myosin Phosphatase Through Phosphorylation of the Myosin-Binding Subunit in Platelet Activation
Keiji Nakai,
Yoshinori Suzuki,
Hisakazu Kihira,
Hideo Wada,
Masanori Fujioka,
Masaaki Ito,
Takeshi Nakano,
Kozo Kaibuchi,
Hiroshi Shiku, and
Masakatsu Nishikawa
From the 2nd and the 1st Departments of Internal Medicine, Mie University School of Medicine, Tsu Mie, Japan; Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma Nara, Japan.
Human platelets were found to contain myosin phosphatase consisting of a 38-kD catalytic subunit of protein phosphatase type 1 , a 130-kD myosin-binding subunit (MBS) and a 20-kD subunit, all of which cross-reacted with antibodies against these subunits of smooth muscle myosin phosphatase. Anti-MBS antibody coimmunoprecipitated RhoA and Rho-kinase of human platelets. Platelets MBS is a substrate for Rho-kinase and phosphorylation of MBS decreases the activity of myosin phosphatase. Treatment of intact platelets with 9,11-epithio-11,12-methano-thromboxane A2 led to a dramatic increase in phosphorylation of MBS and a significant decrease in the activity of myosin phosphatase. These findings suggest a putative mechanism for agonist-induced regulation of myosin phosphatase activity in platelets.
Blood, Vol. 90 No. 10 (November 15), 1997:
pp. 3936-3942
© 1997 by The American Society of Hematology.
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