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Biochemistry |
vß3 as Two Receptors for the 3(IV) Chain of Type IV Collagen on Tumor Cells1
Department of Medicine, University of Pennsylvania School of Medicine [T. A. S., N. A. K.] and The Connective Tissue Research Institute, University City Science Center, Philadelphia, Pennsylvania 19104 [T. A. S., Z. Z., N. A. K.]; and the Laboratoíre de Biochimie Medicale et Biologie Moleculaire, University of Reims-Champagne-Ardenne, CNRS UPRESA 6021, IFR 53 Biomolecules, UFR Médicine, 51095 Reims, France [S. P., A. F., G. B., J-C. M.]
Previous studies from our laboratories demonstrated that a peptide from the noncollagenous domain of the 
3 chain of basement membrane collagen (COL IV), comprising residues 185–203, inhibits polymorphonuclear leukocyte activation and melanoma cell proliferation independently of its ability to promote cell adhesion; these properties require the presence of the triplet -SNS- at residues 189–191 (J. C. Monboisse et al., J. Biol. Chem., 269: 25475–25482, 1994; J. Han et al., J. Biol. Chem., 272: 20395–20401, 1997). More recently, we demonstrated that native COL IV and -SNS-containing synthetic peptides (10 µg/ml) added to culture medium inhibit the proliferation of not only melanoma cells but also breast, pancreas, and stomach tumor cells up to 82% and prostate tumor cells by 15%. This inhibition was shown to be dependent on a COL IV- or peptide-induced increase in intracellular cAMP (T. A. Shahan et al., Connect. Tissue Res., 40: 221–232, 1999). Attempts to identify the putative receptor(s) on tumor cells led to the isolation of five proteins (Mr 33,000, 52,000, 72,000, 95,000, and 250,000) from melanoma and prostate cells by affinity purification with the 3(IV)179–208 peptide. The Mr 52,000, 95,000, and 250,000 proteins were shown to be CD47/integrin-associated protein(IAP), the integrin ß3 subunit, and the vß3 integrin complex, respectively. The Mr 33,000 and 72,000 proteins have not yet been identified. To confirm the specificity of ligand binding to the receptors, cell membranes from either melanoma or prostate tumor cells were pretreated with the unlabeled ligand 3(IV)187–191 (-YYSNS-); alternatively, the peptide was pretreated with a peptide-reactive monoclonal antibody (A5D7) before receptor isolation. These treatments inhibited the purification of CD47/IAP, the integrin ß3 subunit, and the vß3 integrin complex from tumor cells. Furthermore, cells treated with CD47/IAP- or the vß3 integrin-reactive antibodies prevented the 3(IV)185–203 peptide from inhibiting cell proliferation and the subsequent rise in intracellular cAMP. Pretreating cells with the 3(IV)187–191 (-YYSNS-) peptide also inhibited their adhesion to the 3(IV)185–203 peptide substrate, whereas the inactive 1(IV)185–203 peptide, from the same region of the 1 chain as the 3(IV)185–203 peptide, had no effect. Incubation of cells with either CD47/IAP and/or vß3 integrin-reactive antibodies inhibited their adhesion to the 3(IV)185–203 peptide, whereas antibodies to the ß1 and ß2 integrin subunits were without effect. These data suggest that ALC-COL IV, through its 3(IV) chain, inhibits tumor cell proliferation using the receptors CD47/IAP and the vß3 integrin.
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