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Suramin inhibition of growth factor receptor binding and mitogenicity in AKR-2B cells.

Coffey RJ, Leof EB, Shipley GD, Moses HL
J Cell Physiol. 1987 132 (1): 143-8

PMID: 3496343 · DOI:10.1002/jcp.1041320120

Suramin, a polyanionic compound, has previously been shown to dissociate platelet-derived growth factor (PDGF) from its receptor. In the present study suramin was found to inhibit the growth of sparse cultures of AKR-2B cells in fetal bovine serum (FBS)-supplemented medium in a dose-dependent, reversible fashion. Suramin also inhibited the ability of FBS, transforming growth factor beta (TGF beta), heparin-binding growth factor type-2 (HBGF-2), and epidermal growth factor (EGF) to stimulate DNA synthesis in density-arrested cultures of AKR-2B cells. The inhibition of growth factor-stimulated mitogenicity was directly correlated to the dose of suramin required to inhibit the binding of 125I-labeled TGF beta, HBGF-2, and EGF to their cell surface receptors. Suramin affected TGF beta and HBGF-2-related events at a 10-15-fold lower dose than that required for EGF-related events. It was also noted that suramin inhibited TGF beta-stimulated soft agar colony formation of AKR-2B (clone 84A) cells as well as the spontaneous colony formation of AKR-MCA cells, a chemically transformed derivative of AKR-2B cells. This demonstrates that suramin's spectrum of action for growth factors and their receptors should be extended to include TGF beta, HBGF-2, and EGF as well as PDGF. The data further suggest that the spontaneous growth of AKR-MCA cells in soft agar is dependent on growth factor binding to cell surface receptors.

MeSH Terms (18)

Agar Animals Blood Cell Line Cells, Cultured DNA Replication Dose-Response Relationship, Drug Epidermal Growth Factor Fibroblast Growth Factor 2 Growth Substances Heparin Male Mice Mitosis Peptides Receptors, Somatotropin Suramin Transforming Growth Factors

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