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Vol. 13, Issue 1, 1-11, January 2002
6
1 Integrin
Complex during Cellular Morphogenesis
Dana-Farber Cancer Institute and Department of Pathology, Harvard
Medical School, Boston, Massachusetts 02115
Upon plating on basement membrane Matrigel, NIH3T3 cells formed an
anastomosing network of cord-like structures, inhibitable by
anti-
6
1 integrin antibodies. For NIH3T3 cells transfected with human CD151 protein, the formation of a cord-like network was also
inhibitable by anti-CD151 antibodies. Furthermore, CD151 and 61
were physically associated within NIH3T3 cells. On removal of the short
8-amino acid C-terminal CD151 tail (by deletion or exchange), exogenous
CD151 exerted a dominant negative effect, as it almost completely
suppressed 61-dependent cell network formation and NIH3T3 cell
spreading on laminin-1 (an 61 ligand). Importantly, mutant CD151
retained 61 association and did not alter 61-mediated cell
adhesion to Matrigel. In conclusion, the CD151-61
integrin complex acts as a functional unit that markedly
influences cellular morphogenesis, with the CD151 tail being of
particular importance in determining the "outside-in" functions of
61-integrin that follow ligand engagement. Also, antibodies to 61 and CD151 inhibited formation of endothelial cell cord-like networks, thus pointing to possible relevance of CD151-61 complexes during angiogenesis.
Corresponding author. E-mail address:
martin_hemler{at}dfci.harvard.edu.
*
Present address: Vascular Biology Center, University of
Tennessee Health Science Center, Memphis, TN 38163.
These authors made equal contributions.
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