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Post-translational fate of a mucin-like leukocyte sialoglycoprotein (CD43) aberrantly expressed in a colon carcinoma cell line.

Artikel i vetenskaplig tidskrift
Författare Dan Baeckström
Publicerad i The Journal of biological chemistry
Volym 272
Nummer/häfte 17
Sidor 11503-9
ISSN 0021-9258
Publiceringsår 1997
Publicerad vid Institutionen för medicinsk och fysiologisk kemi
Sidor 11503-9
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Adenocarcinoma, metabolism, Antigens, CD, biosynthesis, immunology, Antigens, CD43, Antigens, Tumor-Associated, Carbohydrate, biosynthesis, immunology, Carbohydrate Sequence, Colonic Neoplasms, metabolism, Gangliosides, biosynthesis, immunology, Glycosylation, HL-60 Cells, Humans, Leukocytes, Membrane Proteins, biosynthesis, Molecular Sequence Data, Mucins, metabolism, Phosphoproteins, biosynthesis, immunology, Phosphorylation, Protein Processing, Post-Translational, Sialoglycoproteins, biosynthesis, immunology, Tumor Cells, Cultured
Ämneskategorier Cellbiologi, Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

Sammanfattning

This paper describes the biosynthesis of L-CanAg, a mucin-like glycoprotein which carries the carcinoma-associated carbohydrate epitope sialyl-Lewis a and is secreted by the colon adenocarcinoma cell line COLO 205. Recently, it has been shown that L-CanAg is a novel glycoform of CD43, a surface sialoglycoprotein normally found only on hematopoietic cells. Immunoprecipitation with alpha-GPEP18, a novel antiserum against the cytoplasmic domain of CD43, detected a transmembrane form of L-CanAg carrying sialyl-Lewis a. Cell surface biotinylation experiments demonstrated the presence of transmembrane L-CanAg at the plasma membrane and that COLO 205, unlike the leukocyte cell line HL-60, contained significant amounts of glycosylated intracellular CD43. Immunoprecipitation of phosphate-labeled COLO 205 cells revealed that membrane-bound L-CanAg, like leukocyte CD43, is a phosphoprotein. Interestingly, both surface- and phosphate-labeled L-CanAg were eluted earlier from a gel filtration column than their unlabeled counterparts, indicating that this method could separate membrane-bound L-CanAg from its soluble form. Immunoprecipitations of pulse-chase-labeled COLO 205 lysates fractionated by gel filtration showed that decrease in membrane-bound L-CanAg was concomitant with an increase in the intracellular soluble form. Together, these data indicate that transmembrane L-CanAg is fully glycosylated and phosphorylated before the extracellular domain is cleaved off and stored inside the cell before exocytosis.

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