Abstract
The insulin like growth factor-II/mannose-6-phosphate (IGF-II/M6P) receptor is a bifunc-tional binding protein that binds lysosomal enzymes bearing the M6P recognition marker and IGF-II at distinct binding sites (45, 52). In addition, transforming growth factor (TGF) beta precursor, thyroglobulin and proliferin, a protein which is expressed in rapidly proliferating cells are also recognized by this receptor (Table 1). In avian and amphibian cells the receptor lacks the binding site for IGF-II but serves as a binding protein for M6P bearing ligands (7,9,76). Almost all mammalian cells described until today express IGF-II/M6P receptors that bind both classes of ligands, namely M6P-containing glycoproteins and IGF-II (55–59).
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Kiess, W., Hoeflich, A., Yang, Y., Kessler, U., Flyvbjerg, A., Barenton, B. (1994). The Insulin-Like Growth Factor-II/Mannose-6-Phosphate Receptor: Structure, Function and Differential Expression. In: Le Roith, D., Raizada, M.K. (eds) Current Directions in Insulin-Like Growth Factor Research. Advances in Experimental Medicine and Biology, vol 343. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2988-0_18
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