Integrin VLA-3: ultrastructural localization at cell-cell contact sites of human cell cultures.

Abstract

Abstract. The integrin VLA-3 is a cell surface receptor, which binds to fibronectin, laminin, collagen type

Antibodies to β1‐integrins cause alterations of aortic vasculogenesis, in vivo

“…Although it is known that integrins can mediate cell-cell adhesions (Kaufmann et al, 1989;Larjarva et al, 1990), we feel that the most reasonable interpretation of our data is that the CSAT antibodies interfere with integrin-mediated angioblast adhesion to the surrounding ECM. This speculation is based on the fact that PI-integrins recognize a wide variety of ECM ligands, and that multiple ECM constituents are available for binding.…”

“…It is likely that during vasculogenesis, angioblasts engage in cell-cell adhesions similar to other cell types (Hatta et al, 1987;Edelman, 1985;Kaufmann et al, 1989;Larjarva et al, 1990). We speculate that the disruption of angioblast-ECM adhesions by CSAT allows cell-cell adhesions to predominate.…”

“…Most recently, it has become apparent that integrins can also mediate cell-cell adhesions. (Kaufmann et al, 1989;Lajarva et al, 1990).…”

Low expression of collagen receptors in moderate and poorly differentiated colorectal adenocarcinomas

“…The establishment and maintenance of a polarised and differentiated epithelial cell phenotype is a multistage process that appears to depend on the expression of proteins mediating cell-matrix and cell-cell interactions (Boulan & Nelson, 1989). Since it has been suggested that both VLA-2 and VLA-3 may be involved not only in cell-matrix but also in cell-cell interaction (Kaufmann et al, 1989;Zutter & Santoro, 1989), our findings may, at least in part, explain the morphological changes towards a more undifferentiated and malignant phenotype occurring in colorectal cancer. Direct expression of cell adhesion molecules mediating morphological differentiation would probably limit the growth potential of a developing tumour because of the inverse relationship between growth and differentiation.…”

Expression of beta 1, beta 3, beta 4, and beta 5 integrins by human epidermal keratinocytes and non-differentiating keratinocytes.

“…a3ß, and a2 ß, may also function in cell-cell adhesion (Kaufmann et al ., 1989;Larjava et al ., 1990 ;Carter et al ., 1990a) . It seems possible that ß, integrins in keratinocytes function in initial adhesive contacts to extracellular matrix glycoproteins and then relocate to cell-cell contact areas (Carter et al, 1990a) .…”