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Identification of Vitronectin as a Novel Insulin-Like Growth Factor-II Binding Protein

Cooperative Research Centre for Tissue Growth and Repair and CSIRO Human Nutrition (Z.U., H.W., K.H., C.A.Y., G.I.F., F.J.B.), Adelaide BC, SA 5000, Australia; United States Department of Agriculture (J.P.M.), Growth Laboratory, Agricultural Research Service, Beltsville, Maryland 20705

Address all correspondence and requests for reprints to: Zee Upton, Flinders University of South Australia, GPO Box 2100, School of Biology, Adelaide, South Australia, Australia.

We have previously reported the presence of a 70 kDa insulin-like growth factor (IGF)-II-specific binding protein in chicken serum using Western ligand blotting approaches. In order to ascertain the identity of this 70 kDa IGF-II binding species, the protein has been purified from chicken serum using a combination of ion-exchange and gel-permeation chromatography. Interestingly, amino acid sequencing of the purified protein revealed that it has the same N-terminal sequence as chicken vitronectin (VN). The protein has the ability to specifically bind IGF-II and not IGF-I as determined by ligand blotting, cross-linking and competitive binding assay approaches. In addition, the protein binds ¹²⁵I-des(1-6)-IGF-II, suggesting that the interaction with IGF-II is different to those with other characterized IGF-binding proteins. Importantly, we have ascertained that both human and bovine VN also specifically bind IGF-II. These results are particularly relevant in the light of the recent report that the urokinase-type plasminogen activator receptor, a protein that also binds VN, has been shown to associate with the cation-independent mannose-6-phosphate/IGF-II receptor and suggest a possible role for IGF-II in cell adhesion and invasion.

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