Abstract
We have purified the high molecular weight actin-binding protein, filamin from guinea pig vas deferens. We find this mammalian filamin is very similar to chicken gizzard filamin in subunit molecular weight, amnio acid composition, actin-binding properties, immunological cross-reactivity, and the ability to be phosphorylated by cyclic AMP-dependent protein kinase. Anti-filamin antibodies cross-react with a high molecular weight macrophage actin-binding protein, and with a high molecular weight protein in platelets and fibroblasts. Furthermore like filamin, these proteins are also phosphorylated and cyclic AMP stimulates their phosphorylation. Anti-filamin antibodies do not cross-react with the erythrocyte membrane protein spectrin or with high molecular weight proteins in brain extracts. We conclude that filamin from avian and mammalian smooth muscle are very similar proteins and furthermore that many, but not all, non-muscle cells contain a protein closely related to filamin.
Highlights
Biology, We have purified the high molecular weight a&in-binding protein. filamin from guinea pig vas deferens
We find this mammalian filamin is very similar to chicken gizzard filamin in subunit molecular weight, amino acid composition, actin-binding properties, immunological cross-reactivity. and the ability to be phosphorylated by cyclic AMP-dependent protein kinase
Smooth Muscle Filamins-The objective of these studies was to obtain highly purified filamin from a mammalian source and to use it to clarify the relationship between the various high molecular weight actin-binding proteins
Summary
We have purified the high molecular weight a&in-binding protein. filamin from guinea pig vas deferens. We find this mammalian filamin is very similar to chicken gizzard filamin in subunit molecular weight, amino acid composition, actin-binding properties, immunological cross-reactivity. Anti-filamin antibodies cross-react with a high molecular weight macrophage a&in-binding protein, and with a high molecular weight protein in platelets and fibroblasts Like filamin, these proteins are phosphorylated and cyclic AMP stimulates their phosphorylation. The relatedness of these different high molecular weight actin-binding proteins tion we have purified is not clear To investigate this quesfilamin from guinea pig vas deferens and chicken gizzard and compared these proteins with spectrin in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. In contrast filamin and spectrin have different electrophoretic mobilities and do not show immunological cross-reactivity
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