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• W2051859439 endingPage "8800" @default.
• W2051859439 startingPage "8796" @default.
• W2051859439 abstract "The biosynthesis of the receptor for platelet-derived growth factor (PDGF) was examined in metabolically labeled human foreskin fibroblasts. The receptor was synthesized as a 145-kDa precursor, which, when incubated with endo-beta-N-acetylglucosaminidase H (endo H), underwent a 15-kDa decrease in molecular mass. This indicates that the size of the core protein is about 130 kDa and that the 145-kDa form represents a receptor precursor carrying high-mannose N-linked oligosaccharide groups. Within 15 min after synthesis, the receptor was converted to a 165-kDa form. This form was entirely resistant to endo H treatment and probably represents a receptor molecule that has undergone further posttranslational modification, including O-linked glycosylation. Subsequently, within 30 min, a molecule of 170 kDa--i.e., the size of the mature receptor--appeared. A slightly larger molecule, of 175 kDa, which could be immunoprecipitated from PDGF-stimulated 32P-labeled cells, probably represents a receptor further modified by autophosphorylation. The 170-kDa molecule had an isoelectric point of about 4.5. Addition of PDGF increased the turnover rate of the 170-kDa PDGF receptor." @default.
• W2051859439 created "2016-06-24" @default.
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• W2051859439 date "1987-12-01" @default.
• W2051859439 modified "2023-10-17" @default.
• W2051859439 title "Biosynthesis and intracellular transport of the receptor for platelet-derived growth factor." @default.
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• W2051859439 doi "https://doi.org/10.1073/pnas.84.24.8796" @default.
• W2051859439 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/299637" @default.
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