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Vol. 10, Issue 2, 271-282, February 1999
1 and 2 Integrins Mediate Invasive Activity of
Mouse Mammary Carcinoma Cells through Regulation of Stromelysin-1
Expression
*Life Sciences Division, Lawrence Berkeley National Laboratory,
University of California, Berkeley, California 94720;
Tumor cell invasion relies on cell migration and extracellular
matrix proteolysis. We investigated the contribution of different integrins to the invasive activity of mouse mammary carcinoma cells. Antibodies against integrin subunits Affymax Research Institute, Santa Clara, California
95051; and
§Department of Anatomy, University of
California, San Francisco, California 94143
6 and 
1, but
not against 1 and 2, inhibited cell locomotion on a reconstituted basement membrane in two-dimensional cell migration assays, whereas antibodies against 1, but not against 6 or 2, interfered with cell adhesion to basement membrane constituents. Blocking antibodies against 1 integrins impaired only cell adhesion to type IV
collagen. Antibodies against 1, 2, 6, and 1, but not 5,
integrin subunits reduced invasion of a reconstituted basement
membrane. Integrins 1 and 2, which contributed only
marginally to motility and adhesion, regulated proteinase production.
Antibodies against 1 and 2, but not 6 and 1,
integrin subunits inhibited both transcription and protein
expression of the matrix metalloproteinase stromelysin-1. Inhibition of
tumor cell invasion by antibodies against 1 and 2 was reversed by
addition of recombinant stromelysin-1. In contrast, stromelysin-1 could
not rescue invasion inhibited by anti-6 antibodies. Our data
indicate that 1 and 2 integrins confer invasive behavior by regulating stromelysin-1 expression, whereas 6 integrins
regulate cell motility. These results provide new insights into the
specific functions of integrins during tumor cell invasion.
Corresponding author. E-mail address:
mjbissell{at}lbl.gov.
Present address: Center for Clinical and Basic
Research, Department of Basic Research, Ballerup Byvej 222, DK-2750
Ballerup, Denmark.
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