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Heterotrimeric configuration is essential to the adhesive function of laminin

✍ Scribed by J. C. Lissitzky; P. Cantau; P. M. Martin


Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
753 KB
Volume
48
Category
Article
ISSN
0730-2312

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✦ Synopsis


Mouse PFHR9 larninin, B1 B2-heterodimers, and free B1-chains were separated from one another by gel filtration on Superose 6. The cell attachment promoting activity of these species was measured after imrnunoprecipitation with monoclonal anti-larninin antibodies coupled to Sepharose 6MB beads. These antibodies, which did not react with the laminin E 8 fragment, were directed against epitopes in the NH2-terminus of the laminin B1 -chain and in the central region of larninin. After incubation with purified EHS larninin, the irnmunosorbents revealed efficient adhesion substrates for a rat rhabdomyosarcoma cell line which attached preferentially to the larninin E8 fragment. Although both were irnrnunoprecipitated efficiently, B1 B2-heterodimers and B1 -chains, unlike PFHR9 larninin, did not support the attachment of RMS cells. On a molar basis B1 B2-heterodimers were 24 times less efficient than PFHR9 laminin or EHS larninin in supporting cell attachment. These data suggest that heterotrirneric configuration is essential to the adhesive function of the laminin E8 fragment.


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