Abstract
A secreted glycoprotein (GP) with apparent molecular mass of 90 kDa produced by cultured embryonic cells of Drosophila melanogaster was isolated and partially characterized. GP is enriched by Ser + Thr and Pro residues that constitute up to 30% of the total number of amino acids. An abundant carbohydrate moiety (40% of molecular mass) is mainly represented by vertebrate mucin-type O-linked disaccharide units Gal(beta 1-3)-GalNAc, occupying about a half of the total number of Ser+Thr residues and rendering the GP molecule high resistance to protease action. A few of N-glycans are also present in GP. These characteristics allow to consider the Drosophila GP (termed 'mucin-D') as a first representative of invertebrate mucin-type glycoproteins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amidohydrolases / metabolism
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Amidohydrolases / pharmacology
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Amino Acids / analysis
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Animals
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Blotting, Western
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Borohydrides / chemistry
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Carbohydrate Sequence
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Carbohydrates / analysis
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Cells, Cultured
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Chemical Fractionation
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Concanavalin A / pharmacology
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Drosophila melanogaster / embryology*
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Embryo, Nonmammalian / chemistry*
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Embryo, Nonmammalian / cytology*
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Glycosylation
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Hexosaminidases / chemistry
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Hexosaminidases / metabolism
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Molecular Sequence Data
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Mucins / chemistry*
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Mucins / metabolism
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Oligosaccharides / analysis
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Oligosaccharides / chemistry
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
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Tunicamycin / pharmacology
Substances
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Amino Acids
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Borohydrides
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Carbohydrates
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Mucins
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Oligosaccharides
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Concanavalin A
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Tunicamycin
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sodium borohydride
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Hexosaminidases
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glycopeptide alpha-N-acetylgalactosaminidase
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Amidohydrolases
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Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase