Source:http://linkedlifedata.com/resource/pubmed/id/11133187
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2001-1-30
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pubmed:abstractText |
We have studied the synthesis of laminins (Ln) and determined the specific integrins mediating the adhesion of immortalized human corneal epithelial cells to mouse Ln-1, and human Lns-5 and -10. Immunofluorescence microscopy of the cells demonstrated integrin alpha(2), alpha(3), alpha(6), beta(1)and beta(4)subunits, integrins alpha(6)and beta(4)being found in a typical 'leopard-skin' like manner. Immunoprecipitation studies showed that the cells produced alpha 3, beta 3 and gamma 2 chains of Ln-5, but not Lns-1 or -10. In culture Ln-5 was found as small plaques beneath the adhering cells within 1 hr, while in 4 hr widely spread Ln-5 plaques were observed in colocalization with beta(4)integrin subunit. By using a quantitative cell adhesion assay and function-blocking monoclonal antibodies we showed that integrin beta(1)subunit plays a role in mediating corneal epithelial cell adhesion to mouse Ln-1. However, none of the available function-blocking antibodies to integrin alpha-subunits inhibited the adhesion. Integrin alpha(3)beta(1)complex mediated the adhesion of corneal epithelial cells to human Lns-5 and -10. Integrin complex alpha(3)beta(1), as well as laminin alpha(3)chain, was also shown to mediate cell adhesion to newly produced endogenous Ln-5. The present results show that integrin alpha(3)beta(1)complex mediates the adhesion of corneal epithelial cells to Lns-5 and -10, while a yet unknown integrin alpha subunit appears to play a role in the adhesion to Ln-1. The results also show that among corneal basement membrane laminins, Ln-5 is synthetized by epithelial cells while Ln-10 may be a product of keratocytes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-4835
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:volume |
72
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
93-103
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11133187-Animals,
pubmed-meshheading:11133187-Antibodies, Monoclonal,
pubmed-meshheading:11133187-Blotting, Western,
pubmed-meshheading:11133187-Cell Adhesion,
pubmed-meshheading:11133187-Cells, Cultured,
pubmed-meshheading:11133187-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11133187-Epithelium, Corneal,
pubmed-meshheading:11133187-Humans,
pubmed-meshheading:11133187-Integrins,
pubmed-meshheading:11133187-Laminin,
pubmed-meshheading:11133187-Mice,
pubmed-meshheading:11133187-Precipitin Tests,
pubmed-meshheading:11133187-Protein Isoforms
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pubmed:year |
2001
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pubmed:articleTitle |
Laminin synthesis and the adhesion characteristics of immortalized human corneal epithelial cells to laminin isoforms.
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pubmed:affiliation |
Department of Anatomy, Institute of Biomedicine, University of Helsinki, Helsinki, Finland. hasenson@hytti.uku.fi
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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