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J Biol Chem, Vol. 274, Issue 10, 6711-6717, March 5, 1999

Interactions of High Affinity Insulin-like Growth Factor-binding Proteins with the Type V Transforming Growth Factor- Receptor in Mink Lung Epithelial Cells

From the Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, St. Louis, Missouri 63104

High affinity insulin-like growth factor-binding proteins (IGFBP-1 to -6) are a family of structurally homologous proteins that induce cellular responses by insulin-like growth factor (IGF)-dependent and -independent mechanisms. The IGFBP-3 receptor, which mediates the IGF-independent growth inhibitory response, has recently been identified as the type V transforming growth factor- receptor (TR-V) (Leal, S. M., Liu, Q. L., Huang, S. S., and Huang, J. S. (1997) J. Biol. Chem. 272, 20572-20576). To characterize the interactions of high affinity IGFBPs with TR-V, mink lung epithelial cells (Mv1Lu cells) were incubated with ¹²⁵I-labeled recombinant human IGFBPs (¹²⁵I-IGFBP-1 to -6) in the presence of the cross-linking agent disuccinimidyl suberate and analyzed by 5% SDS-polyacrylamide gel electrophoresis and autoradiography. ¹²⁵I-IGFBP-3, -4, and -5 but not ¹²⁵I-IGFBP-1, -2, and -6 bound to TR-V as demonstrated by the detection of the ~400-kDa ¹²⁵I-IGFBP·TR-V cross-linked complex in the cell lysates and immunoprecipitates. The analyses of ¹²⁵I-labeled ligand binding competition and DNA synthesis inhibition revealed that IGFBP-3 was a more potent ligand for TR-V than IGFBP-4 or -5. Most of the high affinity ¹²⁵I-IGFBPs formed dimers at the cell surface. The cell-surface dimer of ¹²⁵I-IGFBP-3 preferentially bound to and was cross-linked to TR-V in the presence of disuccinimidyl suberate. IGFBP-3 did not stimulate the cellular phosphorylation of Smad2 and Smad3, key transducers of the transforming growth factor- type I/type II receptor (TR-I·TR-II) heterocomplex-mediated signaling. These results suggest that IGFBP-3, -4, and -5 are specific ligands for TR-V, which mediates the growth inhibitory response through a signaling pathway(s) distinct from that mediated by the TR-I and TR-II heterocomplex.

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