Abstract
Cathepsin D, arylsulfatase A and the alpha-chain of beta-hexosaminidase are synthesized in human fibroblasts as sulfated polypeptides. The sulfate is added posttranslationally. Its half-life is less than one-tenth of that of the respective polypeptide chains. The sulfate residues were found on asparagine-linked oligosaccharides sensitive to endoglycosidase F and peptide: N-glycosidase F and resistant to endoglycosidase H. Inhibition of formation of complex type oligosaccharides by 1-deoxy-manno-nojirimycin prevented sulfation, indicating that the sulfate residues were added to complex type oligosaccharides.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylglucosaminidase
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Asparagine
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Cathepsin D / genetics*
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Cells, Cultured
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Cerebroside-Sulfatase / genetics*
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Cycloheximide / pharmacology
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Fibroblasts / enzymology
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Half-Life
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Humans
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Lysosomes / enzymology*
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
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Oligosaccharides / isolation & purification*
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Protein Processing, Post-Translational / drug effects
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Sulfuric Acids / isolation & purification
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beta-N-Acetylhexosaminidases / genetics*
Substances
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Oligosaccharides
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Sulfuric Acids
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Asparagine
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Cycloheximide
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Cerebroside-Sulfatase
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Acetylglucosaminidase
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beta-N-Acetylhexosaminidases
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
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Cathepsin D