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Expression of the leukocyte-associated sialoglycoprotein CD43 by a colon carcinoma cell line.

Artikel i vetenskaplig tidskrift
Författare Dan Baeckström
K Zhang
Noomi Asker
Ulla Rüetschi
M Ek
Gunnar C. Hansson
Publicerad i The Journal of biological chemistry
Volym 270
Nummer/häfte 23
Sidor 13688-92
ISSN 0021-9258
Publiceringsår 1995
Publicerad vid Institutionen för medicinsk och fysiologisk kemi
Institutionen för laboratoriemedicin, Avdelningen för klinisk kemi/transfusionsmedicin
Sidor 13688-92
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Adenocarcinoma, chemistry, Amino Acid Sequence, Animals, Antigens, CD, Antigens, CD43, Colonic Neoplasms, chemistry, Humans, Molecular Sequence Data, Precipitin Tests, Protein Precursors, immunology, RNA, Messenger, analysis, Rabbits, Sialoglycoproteins, analysis, genetics, immunology, Tumor Cells, Cultured
Ämneskategorier Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

Sammanfattning

The colon adenocarcinoma cell line COLO 205 secretes L-CanAg, a mucin-like glycoprotein carrying the carcinoma-associated sialyl-Lewis a carbohydrate epitope. In an attempt to identify its apoprotein, an NH2-terminal peptide sequence was obtained from purified L-CanAg. In all interpretable positions, this sequence showed 100% identity to the NH2-terminal of human CD43 (leukosialin, sialophorin), a plasma membrane-bound sialoglycoprotein hitherto only identified in leukocytes and other hematopoietic cells. An antiserum against deglycosylated L-CanAg and an anti-CD43 antiserum both immunoprecipitated a 61-kDa band, interpreted as the CD43 precursor, from COLO 205 cells as well as from the known CD43-expressing cell line HL-60. Results from immunoprecipitations following pulse-chase experiments and tunicamycin treatments were in agreement with earlier studies on the CD43 precursor. RNA blot analysis confirmed the expression of CD43 by the COLO 205 cell line, whereas three other colon carcinoma cell lines were negative. The glycosylation-dependent monoclonal antibody Leu-22, which recognizes leukocyte CD43, failed to bind L-CanAg, probably due to its much more extensive glycosylation. We conclude that L-CanAg is the secreted extracellular domain of a novel glycoform of CD43 and that CD43, if expressed in other carcinoma cells, may have escaped notice in studies relying on glycosylation-dependent monoclonal antibodies against leukocyte CD43.

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