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Am J Physiol Endocrinol Metab 273: E1005-E1013, 1997;
0193-1849/97 $5.00
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Vol. 273, Issue 5, E1005-E1013, November 1997

Insulin-like growth factor (IGF)-binding protein-5-(201---218) region regulates hydroxyapatite and IGF-I binding

Phil G. Campbell and Dennis L. Andress

Orthopaedic Research Laboratory, Allegheny University of the Health Sciences, Pittsburgh, Pennsylvania 15212; and Departments of Medicine, Veterans Affairs Medical Center and University of Washington, Seattle, Washington 98108

Insulin-like growth factor-binding protein-5 (IGFBP-5), the major bone IGFBP, modifies the biological activity of IGFs within the osteoblastic pericellular environment. Because glycosaminoglycans modulate IGFBP-5 binding to osteoblast organic extracellular matrix (ECM), we assessed whether the heparin binding domain of IGFBP-5, IGFBP-5-(102---218), modifies the interaction of IGFBP-5 with the inorganic bone ECM hydroxyapatite (HA). Synthetic IGFBP-5-(201---218) peptide increased the binding of IGFBP-5 to HA as well as the binding of IGF-I to HA-bound IGFBP-5. This action was specific for the heparin-binding domain, because IGFBP-5-(130---138), IGFBP-5-(138---152), and IGFBP-5-(1---169) were without effect. IGFBP-5-(201---218) was found to bind directly to IGFBP-5 and cause a threefold enhancement of the IGF-I binding affinity for IGFBP-5, whether IGFBP-5 was bound to HA or was in a matrix-free fluid phase. Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201---218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.

bone; extracellular matrix; osteoblast


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