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Secreted MUC1 mucins lacking their cytoplasmic part and carrying sialyl-Lewis a and x epitopes from a tumor cell line and sera of colon carcinoma patients can inhibit HL-60 leukocyte adhesion to E-selectin-expressing endothelial cells.

Artikel i vetenskaplig tidskrift
Författare K Zhang
Dan Baeckström
Hans Brevinge
Gunnar C. Hansson
Publicerad i Journal of cellular biochemistry
Volym 60
Nummer/häfte 4
Sidor 538-49
ISSN 0730-2312
Publiceringsår 1996
Publicerad vid Institutionen för de kirurgiska disciplinerna
Institutionen för medicinsk och fysiologisk kemi
Sidor 538-49
Språk en
Länkar dx.doi.org/10.1002/(SICI)1097-4644(...
Ämnesord Antigens, CD15, immunology, Antigens, Neoplasm, immunology, physiology, Antigens, Tumor-Associated, Carbohydrate, immunology, Cell Adhesion, immunology, Colonic Neoplasms, immunology, Cytoplasm, E-Selectin, analysis, Endothelium, Vascular, chemistry, Epitopes, immunology, HL-60 Cells, Humans, Leukocytes, immunology, Lewis Blood-Group System, immunology, Mucin-1, immunology, physiology, Tumor Cells, Cultured
Ämneskategorier Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

Sammanfattning

A secreted MUC1 mucin from the spent medium of the colon carcinoma cell line COLO 205 carrying sialyl-Lewis a and x epitopes (H-CanAg) was purified by trichloroacetic acid precipitation and Superose 6 gel filtration. The purified H-CanAg inhibited adhesion of the leukocyte cell line HL-60 to E-selectin transfected COS-1 cells or interleukin-1 beta (IL-1 beta)-activated human umbilical vein endothelial cells. Sera from two patients with advanced colon carcinoma containing high concentrations of sialyl-Lewis a and x activity inhibited HL-60 cell adhesion to E-selectin-expressing COS-1 cells and IL-1 beta-activated endothelial cells. After affinity column absorption of the sialyl-Lewis a activity, the sera also lost most of their sialyl-Lewis x activity and at the same time their adhesion inhibitory effect. A large part of the sialyl-Lewis a/x activity in the two patients was found in fractions containing mucins having a MUC1 apoprotein, as shown by its size, and reactivity with the two anti-MUC1 apoprotein monoclonal antibodies, Ma552 and HMFG-2. The cell-adhesion inhibitory effect of the purified sialyl-Lewis a-carrying MUC1 mucin fraction from the sera of the two patients was stronger than that of smaller sized sialyl-Lewis a-carrying mucin-type glycoproteins also found in the patient sera. The MUC1 mucin fraction secreted by the COLO 205 cells and from the two sera were all shown to lack their C-terminal portion, in contrast to the MUC1 mucin from cells. It is hypothesized that sialyl-Lewis a- and/or x-containing mucins, especially MUC1, secreted by tumors can interact with E-selectin on endothelial cells and thus inhibit leukocyte adhesion.

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