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Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers
Immunofluorescent staining of bovine and avian cardiac tissue with affinity-purified antibody to chicken gizzard vinculin reveals two new sites of vinculin reactivity. First, vinculin is organized at the sarcolemma in a striking array of rib-like bands, or costameres. The costameres encircle the car...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1983
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112590/ https://www.ncbi.nlm.nih.gov/pubmed/6413511 |
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collection | PubMed |
description | Immunofluorescent staining of bovine and avian cardiac tissue with affinity-purified antibody to chicken gizzard vinculin reveals two new sites of vinculin reactivity. First, vinculin is organized at the sarcolemma in a striking array of rib-like bands, or costameres. The costameres encircle the cardiac muscle cell perpendicular to the long axis of the fiber and overlie the I bands of the immediately subjacent sarcomeres. The second new site of vinculin reactivity is found in bovine cardiocytes at tubular invaginations of the plasma membrane. The frequency and location of these invaginations correspond to the known frequency and distribution of the transverse tubular system in bovine atrial, ventricular, and Purkinje fibers. We do not detect tubular invaginations that stain with antivinculin in avian cardiocytes and, in fact, a transverse tubular system has not been found in avian cardiac fibers. Apparent lateral Z-line attachments to the sarcolemma and its invaginations have been observed in cardiac muscle by electron microscopy in the same regions where we find vinculin. On the basis of these previous ultrastructural findings and our published evidence for a physical connection between costameres and the underlying myofibrils in skeletal muscle, we interpret the immunofluorescence data of this study to mean that, in cardiac muscle, vinculin is a component of an extensive system of lateral attachment of myofibrils to the plasma membrane and its invaginations. |
format | Text |
id | pubmed-2112590 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1983 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21125902008-05-01 Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers J Cell Biol Articles Immunofluorescent staining of bovine and avian cardiac tissue with affinity-purified antibody to chicken gizzard vinculin reveals two new sites of vinculin reactivity. First, vinculin is organized at the sarcolemma in a striking array of rib-like bands, or costameres. The costameres encircle the cardiac muscle cell perpendicular to the long axis of the fiber and overlie the I bands of the immediately subjacent sarcomeres. The second new site of vinculin reactivity is found in bovine cardiocytes at tubular invaginations of the plasma membrane. The frequency and location of these invaginations correspond to the known frequency and distribution of the transverse tubular system in bovine atrial, ventricular, and Purkinje fibers. We do not detect tubular invaginations that stain with antivinculin in avian cardiocytes and, in fact, a transverse tubular system has not been found in avian cardiac fibers. Apparent lateral Z-line attachments to the sarcolemma and its invaginations have been observed in cardiac muscle by electron microscopy in the same regions where we find vinculin. On the basis of these previous ultrastructural findings and our published evidence for a physical connection between costameres and the underlying myofibrils in skeletal muscle, we interpret the immunofluorescence data of this study to mean that, in cardiac muscle, vinculin is a component of an extensive system of lateral attachment of myofibrils to the plasma membrane and its invaginations. The Rockefeller University Press 1983-10-01 /pmc/articles/PMC2112590/ /pubmed/6413511 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 Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers |
title | Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers |
title_full | Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers |
title_fullStr | Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers |
title_full_unstemmed | Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers |
title_short | Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers |
title_sort | vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112590/ https://www.ncbi.nlm.nih.gov/pubmed/6413511 |