Abstract:
:The insulin-like growth factor-II (IGF-II)/Mannose 6-P receptor (Man 6-P) is a multifunctional receptor that binds two unrelated ligands, IGF-II and lysosomal enzymes that contain Man 6-P recognition markers. Although this receptor has been extensively characterized in mammalian cells, binding of radiolabeled IGF-II to this receptor in avian cells and tissues has not been reported. In the present study, we demonstrate that chick embryo fibroblasts (CEFs) bind and internalize lysosomal enzymes in a Man 6-P-inhibitable fashion, and possess a protein immunologically related to the mammalian IGF-II/Man 6-P receptor that binds lysosomal enzymes with Man 6-P recognition markers but does not bind IGF-II. 1) When lysates of biosynthetically labeled CEFs were affinity-purified on beta-galactosidase-Sepharose, an approximately 250 kilodalton protein was observed in the Man 6-P eluate but not in the Glc 1-P or mannose eluates, that was precipitated by antisera to purified rat and bovine IGF-II/Man 6-P receptors, but not by nonimmune serum. 2) When CEFs were incubated with [35S]proteins enriched in lysosomal enzymes, Man 6-P inhibited binding (0 C) and uptake (34 C) in a dose-dependent fashion. Binding was unchanged in the absence of divalent cations. At low sugar concentrations, binding and uptake were inhibited selectively by Man 6-P and the conformationally similar sugar phosphate, Fru 1-P, a specificity similar to that of mammalian cation-independent Man 6-P receptors. 3) When affinity-purified lysates from biosynthetically labeled CEFs were incubated with antiserum to the rat IGF-II/Man 6-P receptor, a 245 kilodalton protein was immunoprecipitated from lysates that had been affinity purified on beta-galactosidase-Sepharose but not after purification on IGF-II-Sepharose. By contrast, a truncated IGF-II/Man 6-P receptor, presumably internalized from the fetal bovine serum used to feed the cells, was purified from lysates of unlabeled CEFs on IGF-II-Sepharose. Thus, CEFs possess a cation-independent Man 6-P receptor that is similar in size and immunological reactivity to the mammalian IGF-II/Man 6-P receptor, and binds and internalizes lysosomal enzymes but, unlike the mammalian receptor, does not bind IGF-II.
journal_name
Endocrinologyjournal_title
Endocrinologyauthors
Yang YW,Robbins AR,Nissley SP,Rechler MMdoi
10.1210/endo-128-2-1177subject
Has Abstractpub_date
1991-02-01 00:00:00pages
1177-89issue
2eissn
0013-7227issn
1945-7170journal_volume
128pub_type
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