Mucin‐type glycoprotein from Drosophila melanogaster embryonic cells: characterization of carbohydrate component
- 15 January 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 378 (3) , 213-218
- https://doi.org/10.1016/0014-5793(95)01444-6
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(β1–3)‐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.Keywords
This publication has 27 references indexed in Scilit:
- Mucins: Structure, function, and associations with malignancyBioEssays, 1992
- Characterisation of oligosaccharides from Drosophila melanogaster glycoproteinsBiochimica et Biophysica Acta (BBA) - General Subjects, 1991
- GDP‐fucose: β‐N‐acetylglucosamine (Fuc to (Fucα1 → 6GlcNAc)‐Asn‐peptide) α1 → 3‐fucosyltransferase activity in honeybee (Apis mellifica) venom glandsEuropean Journal of Biochemistry, 1991
- Cell surface mucin-type glycoproteins and mucin-like domainsGlycobiology, 1991
- Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.The Journal of cell biology, 1987
- Isolation and characterization of mosquito cell membrane glycoproteinsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1981
- Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycinBiochimica et Biophysica Acta (BBA) - Biomembranes, 1981
- The Structure of Pentasaccharides and Hexasaccharides from Blood Group Substance HEuropean Journal of Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970