Literature DB >> 3918890

Purification of a 175-kDa membrane protein, its localization in smooth and cardiac muscles. Interaction with cytoskeletal protein - vinculin.

V E Koteliansky, G N Gneushev, A M Belkin.   

Abstract

A new 175-kDa membrane protein was isolated from chicken gizzard smooth muscle. Antibodies to 175-kDa protein were used for localization of this protein in smooth and cardiac muscles. In both types of muscle 175-kDa protein was localized near plasma membrane. 175-kDa protein was able to interact specifically with vinculin immobilized on polysterene surface. It is suggested that this 175-kDa protein may be involved in physical connection between microfilaments and cell membrane.

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Year:  1985        PMID: 3918890     DOI: 10.1016/0014-5793(85)81155-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Temporo-spatial distribution of matrix and microfilament components during odontoblast and ameloblast differentiation.

Authors:  Marie-Dominique Kubler; Hervé Lesot; Jean Victor Ruch
Journal:  Rouxs Arch Dev Biol       Date:  1988-07

2.  Immunolocalization of meta-vinculin in human smooth and cardiac muscles.

Authors:  A M Belkin; O I Ornatsky; M A Glukhova; V E Koteliansky
Journal:  J Cell Biol       Date:  1988-08       Impact factor: 10.539

3.  Human smooth muscle VLA-1 integrin: purification, substrate specificity, localization in aorta, and expression during development.

Authors:  V M Belkin; A M Belkin; V E Koteliansky
Journal:  J Cell Biol       Date:  1990-11       Impact factor: 10.539

4.  Identification of two distinct functional domains on vinculin involved in its association with focal contacts.

Authors:  R Bendori; D Salomon; B Geiger
Journal:  J Cell Biol       Date:  1989-06       Impact factor: 10.539

  4 in total

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