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Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle
The sarcolemma of the smooth muscle cell displays two alternating structural domains in the electron microscope: densely-staining plaques that correspond to the adherens junctions and intervening uncoated regions which are rich in membrane invaginations, or caveolae. The adherens junctions serve as...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1993
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119721/ https://www.ncbi.nlm.nih.gov/pubmed/8436588 |
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collection | PubMed |
description | The sarcolemma of the smooth muscle cell displays two alternating structural domains in the electron microscope: densely-staining plaques that correspond to the adherens junctions and intervening uncoated regions which are rich in membrane invaginations, or caveolae. The adherens junctions serve as membrane anchorage sites for the actin cytoskeleton and are typically marked by antibodies to vinculin. We show here by immunofluorescence and immunoelectron microscopy that dystrophin is specifically localized in the caveolae-rich domains of the smooth muscle sarcolemma, together with the caveolae-associated molecule caveolin. Additional labeling experiments revealed that beta 1 integrin and fibronectin are confined to the adherens junctions, as indicated by their codistribution with vinculin and tensin. Laminin, on the other hand, is distributed around the entire cell perimeter. The sarcolemma of the smooth muscle cell is thus divided into two distinct domains, featuring different and mutually exclusive components. This simple bipartite domain organization contrasts with the more complex organization of the skeletal muscle sarcolemma: smooth muscle thus offers itself as a useful system for localizing, among other components, potential interacting partners of dystrophin. |
format | Text |
id | pubmed-2119721 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1993 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21197212008-05-01 Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle J Cell Biol Articles The sarcolemma of the smooth muscle cell displays two alternating structural domains in the electron microscope: densely-staining plaques that correspond to the adherens junctions and intervening uncoated regions which are rich in membrane invaginations, or caveolae. The adherens junctions serve as membrane anchorage sites for the actin cytoskeleton and are typically marked by antibodies to vinculin. We show here by immunofluorescence and immunoelectron microscopy that dystrophin is specifically localized in the caveolae-rich domains of the smooth muscle sarcolemma, together with the caveolae-associated molecule caveolin. Additional labeling experiments revealed that beta 1 integrin and fibronectin are confined to the adherens junctions, as indicated by their codistribution with vinculin and tensin. Laminin, on the other hand, is distributed around the entire cell perimeter. The sarcolemma of the smooth muscle cell is thus divided into two distinct domains, featuring different and mutually exclusive components. This simple bipartite domain organization contrasts with the more complex organization of the skeletal muscle sarcolemma: smooth muscle thus offers itself as a useful system for localizing, among other components, potential interacting partners of dystrophin. The Rockefeller University Press 1993-03-01 /pmc/articles/PMC2119721/ /pubmed/8436588 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 Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle |
title | Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle |
title_full | Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle |
title_fullStr | Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle |
title_full_unstemmed | Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle |
title_short | Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle |
title_sort | complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119721/ https://www.ncbi.nlm.nih.gov/pubmed/8436588 |