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Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes
Hemidesmosomes (HDs) mediate cell adhesion to the extracellular matrix and have morphological association with intermediate-sized filaments (IFs) through cytoplasmic plaques. Though several proteins have been located in HDs, most of them have not been well characterized, with the exception of the 23...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1992
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289367/ https://www.ncbi.nlm.nih.gov/pubmed/1541639 |
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collection | PubMed |
description | Hemidesmosomes (HDs) mediate cell adhesion to the extracellular matrix and have morphological association with intermediate-sized filaments (IFs) through cytoplasmic plaques. Though several proteins have been located in HDs, most of them have not been well characterized, with the exception of the 230-kD antigen of bullous pemphigoid (BP), an autoimmune skin blistering disease. Only recently we have succeeded in isolating HDs from bovine corneal epithelial cells and in identifying five major components on SDS-PAGE (Owaribe K., Y. Nishizawa, and W. W. Franke. 1991. Exp. Cell Res. 192:622-630). In this study we report on immunological characterization of one of the major components, termed HD1, with an apparent molecular mass of 500 kD. Immunofluorescence microscopy showed colocalization of HD1 with BP antigen at the basement membrane zone of those tissues that have typical HDs, including skin epidermis, corneal and tracheal epithelia, and myoepithelium. In cultured keratinocytes, HD1 demonstrated colocalization with BP antigen in the precise way, while being absent from focal adhesions. Immunoelectron microscopy revealed that an epitope of HD1 was located on the cytoplasmic side of HDs. Taking all these results together, we conclude that HD1 is a new hemidesmosomal component. Interestingly, HD1 also exists in endothelial and glial cells, which lack typical HDs. |
format | Text |
id | pubmed-2289367 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1992 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22893672008-05-01 Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes J Cell Biol Articles Hemidesmosomes (HDs) mediate cell adhesion to the extracellular matrix and have morphological association with intermediate-sized filaments (IFs) through cytoplasmic plaques. Though several proteins have been located in HDs, most of them have not been well characterized, with the exception of the 230-kD antigen of bullous pemphigoid (BP), an autoimmune skin blistering disease. Only recently we have succeeded in isolating HDs from bovine corneal epithelial cells and in identifying five major components on SDS-PAGE (Owaribe K., Y. Nishizawa, and W. W. Franke. 1991. Exp. Cell Res. 192:622-630). In this study we report on immunological characterization of one of the major components, termed HD1, with an apparent molecular mass of 500 kD. Immunofluorescence microscopy showed colocalization of HD1 with BP antigen at the basement membrane zone of those tissues that have typical HDs, including skin epidermis, corneal and tracheal epithelia, and myoepithelium. In cultured keratinocytes, HD1 demonstrated colocalization with BP antigen in the precise way, while being absent from focal adhesions. Immunoelectron microscopy revealed that an epitope of HD1 was located on the cytoplasmic side of HDs. Taking all these results together, we conclude that HD1 is a new hemidesmosomal component. Interestingly, HD1 also exists in endothelial and glial cells, which lack typical HDs. The Rockefeller University Press 1992-03-02 /pmc/articles/PMC2289367/ /pubmed/1541639 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 Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes |
title | Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes |
title_full | Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes |
title_fullStr | Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes |
title_full_unstemmed | Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes |
title_short | Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes |
title_sort | identification of a new hemidesmosomal protein, hd1: a major, high molecular mass component of isolated hemidesmosomes |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289367/ https://www.ncbi.nlm.nih.gov/pubmed/1541639 |