Insulin-like Growth Factors type I and II are small proteins structurally related to insulin that have both growth promoting and differentiation activity on a variety of cells (1). Their action is mediated through binding of the IGF-I receptor (IGF-I R). IGF-I R is a tetramer consisting of two extracellular 125 kDa α chains and 2 transmembrane 95 kDa β chains (2). IGF-I R has tyrosine kinase activtity, which is linked to the ras-raf-MAPK signaling pathway. IGF-I and IGF-II bind IGF-IR with a Ks of approximately 1 - 10 nM (3). Two other receptors have also been reported to bind IGFs: insulin receptor and IGF-II R. A number of IGF binding proteins present in plasma are involved in IGF transport and they appear to also regulate the interaction of IGFs with their receptors by controlling the amount of free IGFs available for receptor interactions (4). IGF-I Rs have been implicated in promoting tumor growth through their anti-apoptotic action. Furthermore, IGF-I R may associate with collagen-binding integrins to regulate cell adhesion (5). These properties make the monitoring of IGF-I R on cell surfaces an important exercise in understanding malignant cell transformation and tumor progression.
MAB391 is a monoclonal directed to the extracellular domain of the IGF-I R. This monoclonal has also been shown to neutralize IGF activity on the human MCF breast epithelial tumor cell line.
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4. Johnson, D.E. and L.T. Williams (1993) Adv. Cancer Res. 60:1.
5. Murgue, B. et al. (1994) Cancer Res. 54:5206.
1. Rotwein, P. (1991) Growth Factors 5:3.
2. LeRoith, D. et al. (1993) Ann. New York Acad. Sci. 692:22.
3. Rosenfeld, R.G. et al. (1987) Bioechem. Biophys. Res. Comm. 143:199.
4. Bach, L.A. et al. (1993) J. Biol. Chem. 268:9246.
5. Shakibaei, M. et al. (1999) Biochem. J. 342:615.
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