Filamin inhibits actomyosin ATPase activity in platelet.
Filamin, an actin cross-linker protein, has been shown to exist in platelet. The role of this protein in the platelet has remained unclear. In this report, we show that filamin inhibits the actin-activated Mg2+ -ATPase activity of platelet myosin. The activation caused by platelet actin is inhibited by 50% at the molar ratio of filamin to actin of 1/50. Platelet tropomyosin, which we showed to enhance the ATPase activity, does not abolish the effect of filamin. The results support the view that filamin stabilizes the actin network in the resting platelet.
Onji
T
T
Takagi
M
M
Shibata
N
N
D000199:Actins / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000818:Animals; D001792:Blood Platelets / Q000201:enzymology*; D017301:Ca(2+) Mg(2+)-ATPase / Q000037:antagonists & inhibitors; D003285:Contractile Proteins / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D064448:Filamins; D008840:Microfilament Proteins / Q000494:pharmacology*; D008854:Microscopy, Electron; D013552:Swine; D014335:Tropomyosin / Q000378:metabolism
D000199:Actins; D003285:Contractile Proteins; D064448:Filamins; D008840:Microfilament Proteins; D014335:Tropomyosin; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase