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Studies on proteins that co-purify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells

Membrane extracts from chicken smooth muscle contain, along with filamin, vinculin and alpha actinin, a group of polypeptides that have the ability to interact with the "barbed end" of actin filaments. These low molecular mass polypeptides were designated as HA1 (Wilkins, J.A., and S. Lin,...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1986
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114356/
https://www.ncbi.nlm.nih.gov/pubmed/3095336
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description Membrane extracts from chicken smooth muscle contain, along with filamin, vinculin and alpha actinin, a group of polypeptides that have the ability to interact with the "barbed end" of actin filaments. These low molecular mass polypeptides were designated as HA1 (Wilkins, J.A., and S. Lin, 1986, J. Cell Biol., 102:1085-1092). In this study, polyclonal antibodies raised against the HA1 preparation were used to study the cellular localization and tissue distribution of these polypeptides. Immunofluorescence experiments revealed a primary localization of staining at the ends of stress fibers on the ventral surface of cultured chicken embryo fibroblasts, i.e., those areas known as the focal adhesions. Specific staining was also seen at the Z-lines of both skeletal muscle myofibrils and cultured embryonic heart cells. Immunoblotting analyses of proteins from different tissues prepared to avoid proteolytic degradation showed a much different pattern than that of HA1 itself. Immunoreactive polypeptides with reduced molecular masses of 200,000 and 150,000 D were found in smooth muscle and fibroblasts while 200 and 60 kD polypeptides were found in cardiac muscle tissue. The antibodies recognized 60- and 31-kD polypeptides on immunoblots of chicken breast muscle. The results from this study strongly suggest that the polypeptides in HA1 arose from proteolysis of high molecular mass molecules. The studies also raise the possibility that immunologically related proteins in muscle and nonmuscle cells may be involved in linking actin filaments to Z-lines and membranes, respectively.
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spelling pubmed-21143562008-05-01 Studies on proteins that co-purify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells J Cell Biol Articles Membrane extracts from chicken smooth muscle contain, along with filamin, vinculin and alpha actinin, a group of polypeptides that have the ability to interact with the "barbed end" of actin filaments. These low molecular mass polypeptides were designated as HA1 (Wilkins, J.A., and S. Lin, 1986, J. Cell Biol., 102:1085-1092). In this study, polyclonal antibodies raised against the HA1 preparation were used to study the cellular localization and tissue distribution of these polypeptides. Immunofluorescence experiments revealed a primary localization of staining at the ends of stress fibers on the ventral surface of cultured chicken embryo fibroblasts, i.e., those areas known as the focal adhesions. Specific staining was also seen at the Z-lines of both skeletal muscle myofibrils and cultured embryonic heart cells. Immunoblotting analyses of proteins from different tissues prepared to avoid proteolytic degradation showed a much different pattern than that of HA1 itself. Immunoreactive polypeptides with reduced molecular masses of 200,000 and 150,000 D were found in smooth muscle and fibroblasts while 200 and 60 kD polypeptides were found in cardiac muscle tissue. The antibodies recognized 60- and 31-kD polypeptides on immunoblots of chicken breast muscle. The results from this study strongly suggest that the polypeptides in HA1 arose from proteolysis of high molecular mass molecules. The studies also raise the possibility that immunologically related proteins in muscle and nonmuscle cells may be involved in linking actin filaments to Z-lines and membranes, respectively. The Rockefeller University Press 1986-10-01 /pmc/articles/PMC2114356/ /pubmed/3095336 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Studies on proteins that co-purify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells
title Studies on proteins that co-purify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells
title_full Studies on proteins that co-purify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells
title_fullStr Studies on proteins that co-purify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells
title_full_unstemmed Studies on proteins that co-purify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells
title_short Studies on proteins that co-purify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells
title_sort studies on proteins that co-purify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and z-lines of muscle cells
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114356/
https://www.ncbi.nlm.nih.gov/pubmed/3095336