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Volume 272, Number 5, Issue of January 31, 1997 pp. 2736-2743
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Ligation of Integrin alpha 5beta 1 Is Required for Internalization of Vitronectin by Integrin alpha vbeta 3

(Received for publication, March 28, 1996, and in revised form, November 4, 1996)

Vivian Pijuan-Thompson and Candece L. Gladson

From the Department of Pathology, Division of Neuropathology, University of Alabama at Birmingham, Birmingham, Alabama 35294

Remodeling of the matrix by tumor cells is necessary for tumor invasion. We have shown previously that malignant astrocytomas, in contrast to normal astrocytes, synthesize vitronectin and express integrins alpha vbeta 3 and alpha vbeta 5. The activity states of these two integrins are differentially controlled. Thus, we investigated the regulation of the activity of integrins alpha vbeta 3 and alpha vbeta 5 with regard to their role in vitronectin internalization in U-251MG astrocytoma cell monolayers adherent to fibronectin, collagen, or laminin in serum-free conditions. Binding of [125I]vitronectin occurred in a specific, saturable manner that was partially inhibitable by monoclonal antibodies (mAbs) specific for integrins alpha vbeta 3 or alpha vbeta 5. Specific, lysosomally-mediated degradation of [125I]vitronectin was detectable at 1 h and increased over the 24-h assay period. The cell substrate affected the rate of turnover of [125I]vitronectin, which was 3.0 ng/min for cells plated on fibronectin but 0.35 ng/min for cells plated on collagen. Furthermore, although mAbs specific for either integrin alpha vbeta 3 or alpha vbeta 5 inhibited degradation (30%; combined effect 70%) of [125I]vitronectin by cells plated on fibronectin, only mAb anti-alpha vbeta 5 inhibited degradation (70-90%) by cells plated on collagen or laminin. To determine the requirement for integrin alpha 5beta 1 ligation in order for integrin alpha vbeta 3 to internalize its ligand, cells were plated on mAbs anti-integrin alpha 5 or anti-integrin alpha 3. When plated on mAb anti-alpha 5, mAbs anti-alpha vbeta 3 and anti-alpha vbeta 5 both inhibited degradation. However, when plated on mAb anti-alpha 3, mAb anti-alpha vbeta 3 had no effect whereas mAb anti-alpha vbeta 5 inhibited degradation. These data indicate that a signal from integrin alpha 5beta 1 is necessary for integrin alpha vbeta 3 to internalize vitronectin, whereas integrin alpha vbeta 5 constitutively internalizes vitronectin.


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