Reversible binding of actin to gelsolin and profilin in human platelet extracts.
نویسندگان
چکیده
منابع مشابه
Reversible binding of actin to gelsolin and profilin in human platelet extracts
This paper documents the reversible appearance of high-affinity complexes of profilin and gelsolin with actin in extracts of platelets undergoing activation and actin assembly. Sepharose beads coupled to either monoclonal anti-gelsolin antibodies or to polyproline were used to extract gelsolin and profilin, respectively, from EGTA-containing platelet extracts and determine the proportion of the...
متن کاملMechanism of the interaction of human platelet profilin with actin
We have reexamined the interaction of purified platelet profilin with actin and present evidence that simple sequestration of actin monomers in a 1:1 complex with profilin cannot explain many of the effects of profilin on actin assembly. Three different methods to assess binding of profilin to actin show that the complex with platelet actin has a dissociation constant in the range of 1 to 5 mic...
متن کاملKinetic analysis of F-actin depolymerization in the presence of platelet gelsolin and gelsolin-actin complexes
Platelet gelsolin (G), a 90,000-mol-wt protein, binds tightly to actin (A) and calcium at low ionic strength to form a 1:2:2 complex, GA2Ca2 (Bryan, J., and M. Kurth, 1984, J. Biol. Chem. 259:7480-7487). Chromatography of actin and gelsolin mixtures in EGTA-containing solutions isolates a stable binary complex, GA1Ca1 (Kurth, M., and J. Bryan, 1984, J. Biol. Chem. 259:7473-7479). The effects of...
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Profilin is a conserved, widely distributed actin monomer binding protein found in eukaryotic cells. Mammalian profilin reversibly sequesters actin monomers in a high affinity profilactin complex. In vitro, the complex is dissociated in response to treatment with the polyphosphoinositides, phosphatidylinositol monophosphate, and phosphatidylinositol 4,5-bisphosphate. Here, we demonstrate the ul...
متن کاملCoordinated Inhibition of Actin-Induced Platelet Aggregation by Plasma Gelsolin and Vitamin D-Binding Protein
Actin is an abundant intracellular protein that is released into the blood during tissue injury and its injection into rats causes microthrombi to form in the vasculature. This report and others have shown that actin filaments are able to aggregate platelets in an adenosine diphosphate (ADP)dependent manner. The effects on this process of two plasma actin-binding proteins, vitamin D-binding pro...
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ژورنال
عنوان ژورنال: The Journal of Cell Biology
سال: 1987
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.105.2.833