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• W2078794352 abstract "The structural and functional properties of the aa (2 × 97 kDa) and cc (2 × 94 kDa) isoforms of platelet α-actinin have been compared. Structural differences between aa and cc are revealed by their peptide maps, obtained from limited proteolysis, and by their immunological cross-reactivity. Both isoforms stimulate the Mg ATPase activity of actomyosin, bind to F-actin (high-speed sedimentation) and cross-link or gel actin filaments (low-speed sedimentation and viscometry), in a calcium-dependent manner. The study of the interaction with F-actin indicates that the binding of 1 molecule of aa or ccα-actinin/9-11 actin monomers is sufficient to produce maximal gelation in the presence of EGTA. CaCl2 at 0.1 mM strongly inhibits the binding of aa to F-actin and weakly that of cc, while it inhibits similarly the cross-linking of either aa or cc. The cross-linking efficiency of cc is 9, 7, 1.7 and 1.3 times higher than that of aa at 4, 20, 30 and 37°C, respectively. The bb form (2 × 96 kDa), which is a proteolytic product of aa [Y. Gache et al. (1984) Biochem. Biophys. Res. Commun. 124, 877-881], behaves roughly as aa, but the calcium sensitivity of its binding to F-actin is intermediate between that of aa and cc. These results suggest that the effect of Ca2+ concentration on the binding of platelet α-actinin to F-actin may be partly dissociated from the effect on the cross-linking." @default.
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• W2078794352 date "1985-12-01" @default.
• W2078794352 modified "2023-09-25" @default.
• W2078794352 title "Properties of two isoforms of human blood platelet alpha-actinin" @default.
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• W2078794352 doi "https://doi.org/10.1111/j.1432-1033.1985.tb09291.x" @default.
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