Negative Cooperativity between α3β1and α2β1Integrins in Human Mammary Carcinoma MDA MB 231 Cells

The α3β1integrin has been implicated as a receptor for several matrix components, including collagen, fibronectin, and laminins. The function of α3β1seems to be very versatile involving cell adhesion to or migration on ECM, establishment of cell–cell contacts in aggregates, as well as linkage to int...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Experimental cell research 1998-05, Vol.240 (2), p.368-376
Hauptverfasser: Lichtner, Rosemarie B., Howlett, Anthony R., Lerch, Melanie, Xuan, Jian-Ai, Brink, Jody, Langton-Webster, Beatrice, Schneider, Martin R.
Format: Artikel
Sprache:eng
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:The α3β1integrin has been implicated as a receptor for several matrix components, including collagen, fibronectin, and laminins. The function of α3β1seems to be very versatile involving cell adhesion to or migration on ECM, establishment of cell–cell contacts in aggregates, as well as linkage to intracellular tyrosine phosphorylation cascades. Here we report a strong induction of attachment of α3β1integrin expressing human breast carcinoma cell line MDA MB 231 to matrix proteins by two α3integrin subunit function-blocking monoclonal antibodies (P1B5 and ASC-1). In contrast, stimulation of adhesion to ECM by inhibitory α3integrin-specific antibodies was not observed in the α3β1integrin-expressing nonmalignant human mammary epithelial cell line MCF-10A or the human breast carcinoma cell line MDA MB 468 that expressed relatively low amounts of α3β1integrin at the cell surface. This increase was specific for collagens and not observed on fibronectin or laminin. Physiological concentrations of bivalent cations were not required. MAb P1B5 did not induce homotypic aggregation of MDA MB 231 cells. The P1B5-induced increase in cell attachment to collagens could be prevented but not reduced below control levels by blocking mAb to the α2integrin subunit. Function blocking anti-α5integrin subunit mAb was without effect while anti-β1-mAb completely abolished adhesion. Our data indicate that negative cooperativity between integrins results in transdominant inhibition of α2β1function by α3β1in human MDA MB 231 but not MDA MB 468 tumor cells or nonmalignant MCF-10A cells.
ISSN:0014-4827
1090-2422
DOI:10.1006/excr.1998.4012