PMID: 9443892Apr 4, 1998Paper

The alphavbeta5 integrin functions as an endocytic receptor for vitronectin

Journal of Cell Science
L M Memmo, P J McKeown-Longo

Abstract

Endocytosis and degradation of vitronectin by human skin fibroblasts are regulated by the beta5 integrin. To determine whether the beta5 integrin is directly mediating the internalization of vitronectin, both vitronectin and the beta5 integrin were localized by indirect immunofluorescence during the endocytic process. This analysis showed that both vitronectin and beta5 were found in intracellular vesicles within 5 minutes of the addition of exogenous vitronectin to fibroblast cell layers. By 15 minutes, approximately 20% of the vitronectin-containing vesicles stained positively for beta5. In contrast, the beta3 integrin was not found in any intracellular vesicles. Within 30 minutes, more than 50% of vitronectin-containing vesicles also stained for lamp-1, indicating that internalized vitronectin traveled to lysosomes. Inhibition of clathrin assembly by either potassium depletion or hypertonic buffer inhibited vitronectin internalization, suggesting that vitronectin internalization occurred through coated pits. Confocal analysis confirmed the colocalization of vitronectin and alphavbeta5 in intracellular compartments and further demonstrated that the highest colocalization of the two proteins occurred within 1.8 microm from the...Continue Reading

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