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Physiological role of the insulin-like growth factor binding proteins

The original observation that insulin-like growth factors (IGFs) are present in native serum as high-molecular-weight forms (1–3) had not attracted particular attention for a surprisingly long period of time. All efforts had then concentrated on the biological and chemical characterization of a low-molecular-weight component with a non-suppressible insulin-like activity (NSILA-s; s stands for the material that was soluble in acid–ethanol during one of the first steps of purification). Even the finding, several years later, that NSILA-s bound with high specificity and affinity to high-molecular-weight serum proteins, suggesting the presence of specific IGF binding proteins (IGFBPs) (4, 5) received relatively little attention. The main interest, rather, centered around the newly identified constituents of NSILA-s, i.e. IGF-I and IGF-II (6), whose complete amino acid sequences had been published in 1978 (7, 8). Thus, it took nearly another 10 years until the first two human IGFBPs had been isolated and characterized by their

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