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A secreted mucin carrying sialyl-Lewis a from colon carcinoma cells binds to E-selectin and inhibits HL-60 cell adhesion.

Artikel i vetenskaplig tidskrift
Författare K Zhang
Dan Baeckström
Gunnar C. Hansson
Publicerad i International journal of cancer. Journal international du cancer
Volym 59
Nummer/häfte 6
Sidor 823-9
ISSN 0020-7136
Publiceringsår 1994
Publicerad vid Institutionen för medicinsk och fysiologisk kemi
Sidor 823-9
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Antigens, Neoplasm, immunology, metabolism, Cell Adhesion, Cell Adhesion Molecules, immunology, metabolism, Colonic Neoplasms, immunology, metabolism, E-Selectin, Gangliosides, immunology, metabolism, Humans, Immunoglobulin Fab Fragments, immunology, metabolism, Immunoglobulin G, immunology, metabolism, Leukocytes, immunology, Microscopy, Fluorescence, Mucins, immunology, metabolism, Tumor Cells, Cultured
Ämneskategorier Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

Sammanfattning

Sialyl-Lewis x and a are known as ligands for E-selectin (ELAM-I) involved in leukocyte-endothelial adhesion. L-CanAg (light cancer antigen), secreted by a colon carcinoma cell line COLO 205, is a soluble mucin-type glycoprotein expressing sialyl-Lewis a antigens. L-CanAg was purified from spent culture medium by trichloracetic acid precipitation and Superose 6 gel filtration. With a monoclonal antibody against E-selectin (BBAI) as a positive control, the purified L-CanAg was shown to bind to E-selectin-Fc coated into plastic microtiter wells and to the surface of transiently E-selectin-transfected COS-I cells in a Ca(2+)-dependent way. Immunofluorescent double labelling showed that both BBAI and L-CanAg stained the same cells and morphological co-localization on E-selectin-transfected COS-I cells. Like BBAI, L-CanAg can inhibit leukocyte HL-60 cell adhesion to E-selectin-transfected COS-I cells, and this inhibition can be blocked by a F(ab')2 fragment directed against the sialyl-Lewis a epitope.

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