Abstract
We have found that the major excreted protein (MEP) of transformed mouse fibroblasts, a phosphoglycoprotein of Mr = 35,000, carries the mannose 6-phosphate recognition marker. MEP secreted by Kirsten virus-transformed NIH 3T3 cells binds to a purified preparation of lysosomal enzyme phosphomannosyl receptor, and this binding is specifically inhibited by mannose 6-phosphate. 32Pi introduced into MEP by metabolic labeling of intact cells is exclusively associated with asparagine-linked oligosaccharides as indicated by sensitivity to endohexosaminidase H. Labeling studies utilizing [2-3H]mannose indicate that approximately one-fifth of the mannose residues of MEP are phosphorylated. Comparative studies of the synthesis, secretion, and uptake of MEP and the lysosomal enzyme beta-galactosidase indicate that MEP made by Kirsten virus-transformed NIH 3T3 cells is not handled in the same manner as are other lysosomal enzymes. MEP may be an unusual lysosomal protein, or both.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cathepsin L
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Cathepsins
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Cell Transformation, Neoplastic*
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Cells, Cultured
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Cysteine Endopeptidases
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Endopeptidases*
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Glycoproteins / isolation & purification
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Glycoproteins / metabolism*
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Hexosaminidases
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Hexosephosphates / metabolism*
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Hexosephosphates / pharmacology*
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Kirsten murine sarcoma virus / genetics*
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Lysosomes / metabolism*
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Mannosephosphates / metabolism*
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Mannosephosphates / pharmacology*
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
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Mice
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Oligosaccharides / analysis
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Receptor, IGF Type 2
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Receptors, Cell Surface / metabolism*
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Sarcoma Viruses, Murine / genetics*
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beta-Galactosidase / metabolism
Substances
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Glycoproteins
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Hexosephosphates
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Mannosephosphates
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Oligosaccharides
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Receptor, IGF Type 2
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Receptors, Cell Surface
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mannose-6-phosphate
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Hexosaminidases
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beta-Galactosidase
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
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Cathepsins
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Endopeptidases
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Cysteine Endopeptidases
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Cathepsin L
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Ctsl protein, mouse