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pubmed-article:2140985pubmed:abstractTextThe smooth muscle cells of chicken gizzard harbor the ectoenzyme 5'-nucleotidase. The purified enzyme was reconstituted into 3H-labeled proteoliposomes which were used as a model to study the association of a membrane protein with fibronectin. We demonstrated that the binding process between proteoliposomes and fibronectin has the qualities of a receptor-ligand interaction, i.e., is saturable and specific. In contrast to the association of fibronectin with integrins, the interaction with 5'-nucleotidase does not require divalent metal ions. Synthetic peptides containing the RGD-sequence or a monoclonal antibody interfering with binding of other receptors to the cell-binding domain of fibronectin did not abolish the interaction with 5'-nucleotidase. This indicates that the RGDS-sequence does not represent the major contact site for the AMPase and that the 5'-nucleotidase belongs to a separate class of fibronectin receptors with distinct properties as compared to the integrins.lld:pubmed
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pubmed-article:2140985pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:2140985pubmed:articleTitleChicken gizzard 5'-nucleotidase is a receptor for the extracellular matrix component fibronectin.lld:pubmed
pubmed-article:2140985pubmed:affiliationInstitut für Anatomie und Zellbiologie der Universität, Marburg/Bundesrepublik Deutschland.lld:pubmed
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