THE NOMENCLATURE for the insulin-like growth factor (IGF) binding proteins (IGFBP) was established at the 2nd and 3rd International IGF Symposia (1, 2). The IGFBPs constitute a family of six structurally related proteins that bind IGF peptides with high affinity (typical Kd in the 10−10 to 10−11m range). They share an overall protein sequence identity of approximately 50% and contain 16–18 conserved cysteines in the NH2- and COOH-terminal regions (3). Recently, the predicted protein product of the mac25 complementary DNA (4) was shown to be structurally related to the IGFBPs, especially in the amino-terminal region, where 11–12 of the 12 cysteines found in IGFBPs 1–6 are conserved (5). The protein was synthesized in a baculovirus expression system (5), found to be identical to previously described tumor-derived adhesion factor (6) and prostacyclin-stimulating factor (7), and to bind IGF-I, IGF-II, and insulin, but with relatively low affinity. It was, accordingly, provisionally named IGFBP-7 (5, 8).
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Baxter et al. (1998) studied this question.
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