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IGF2 — M6PR

Text-mined interactions from Literome

Damke et al., Biochem J 1992 : IGF-I, IGF-II and phorbol ester increased the surface expression of the M6P/IGF-II receptor and of MPR46
von Figura et al., Curr Opin Cell Biol 1991 (Mucolipidoses) : Recent studies have established that in mammalian cells insulin-like growth factor-II can couple the large mannose-6-phosphate receptor to a GTP binding protein and that the insulin-like growth factor-II induced activation of the GTP binding protein is inhibited by mannose-6-phosphate and lysosomal enzymes
Williams et al., Structure 2007 : The insulin-like growth factor II/mannose-6-phosphate receptor ( IGF2R ) mediates trafficking of mannose-6-phosphate ( M6P ) -containing proteins and the mitogenic hormone IGF2
Kiess et al., J Biol Chem 1989 : Insulin-like growth factor-II (IGF-II) inhibits both the cellular uptake of beta-galactosidase and the binding of beta-galactosidase to purified IGF-II/mannose 6-phosphate receptor
Bach et al., Endocrinology 1995 : IGF-II induced concentration dependent proliferation with a maximum increase of 47 % ; half-maximal proliferation was seen with approximately 50 ng/ml. [ Arg54, Arg55 ] IGF-II bound to the IGF-I receptor with slightly lower affinity than IGF-II, did not bind to the IGF-II/mannose 6-phosphate receptor , and bound to IGFBPs secreted by myoblasts with approximately 16-fold decreased affinity ... These results suggest that 1 ) IGF-II induced proliferation and differentiation of L6A1 myoblasts are predominantly mediated by the IGF-I receptor ; 2 ) the IGF-II/mannose 6-phosphate receptor is not required for these actions of IGF-II ; 3 ) nevertheless, the IGF-II/mannose 6-phosphate receptor may be capable of mediating these actions ; and 4 ) IGFBPs secreted by myoblasts inhibit IGF actions