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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1988-8-10
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pubmed:abstractText |
Further biochemical investigations on the hemidesmosome-associated epidermal basement membrane component recognized by the monoclonal antibody GB3 are presented in this study. We previously found that the expression of this constituent is impaired in a severe genodermatosis termed lethal junctional epidermolysis bullosa. We demonstrate now that this factor is a very large glycoprotein (apparent molecular weight, 600 kDa) made up of polypeptides in the range of 93.5 to 150 kDa, and containing N-linked oligosaccharide chains. Both endo-beta-N-acetylglucosaminidases and neuraminidase hydrolysis, as well as concanavalin A binding experiments were performed on the GB3 radioimmunoprecipitated polypeptides from cultured human keratinocytes. They showed that the antigen subunits probably bear both 'high-mannose' and 'complex' type glycosidic chains. The chronic exposure of cultured human keratinocytes to retinoic acid (10(-8) to 10(-6) M) resulted in no apparent changes in the overall bulk of these glycosidic chains, but a dose-dependent increase of synthesis and secretion of the antigen was observed. A relative induction factor of 4 was obtained in cultures treated with 10(-6) M retinoic acid. This induction was also observed morphologically by indirect immunofluorescence at the basement membrane zone from cultured human keratinocytes grown on dead de-epidermized dermis. These results further emphasize the influence of glycoproteins in cell-cell and cell-substratum attachment. Furthermore, the ability to modulate this antigen may be relevant for the understanding of the molecular defect involved in lethal junctional epidermolysis bullosa.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Concanavalin A,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin,
http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
942
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
45-56
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2454667-Antibodies, Monoclonal,
pubmed-meshheading:2454667-Basement Membrane,
pubmed-meshheading:2454667-Cells, Cultured,
pubmed-meshheading:2454667-Concanavalin A,
pubmed-meshheading:2454667-Desmosomes,
pubmed-meshheading:2454667-Epitopes,
pubmed-meshheading:2454667-Fluorescent Antibody Technique,
pubmed-meshheading:2454667-Glycoside Hydrolases,
pubmed-meshheading:2454667-Humans,
pubmed-meshheading:2454667-Immunologic Techniques,
pubmed-meshheading:2454667-Macromolecular Substances,
pubmed-meshheading:2454667-Membrane Glycoproteins,
pubmed-meshheading:2454667-Molecular Weight,
pubmed-meshheading:2454667-Oxidation-Reduction,
pubmed-meshheading:2454667-Tretinoin,
pubmed-meshheading:2454667-Tunicamycin
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pubmed:year |
1988
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pubmed:articleTitle |
The new basement membrane antigen recognized by the monoclonal antibody GB3 is a large size glycoprotein: modulation of its expression by retinoic acid.
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pubmed:affiliation |
Laboratoire de Recherches Dermatologiques, UER Médecine, Nice, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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