TY - JOUR
T1 - Oligosaccharides expressed on MUC1 produced by pancreatic and colon tumor cell lines
AU - Burdick, Michael D.
AU - Harris, Ann
AU - Reid, Colm J.
AU - Iwamura, Takeshi
AU - Hollingsworth, Michael A.
PY - 1997/9/26
Y1 - 1997/9/26
N2 - MUC1 is expressed at the apical surface of ductal epithelia of tissues, including breast, pancreas, airway, and the gastrointestinal tract, where its functions include lubrication and protection of the epithelia. In addition, roles for MUC1 have been suggested in both adhesive and antiadhesive properties of tumor cells, and extensive O-glycosylation of the MUC1 tandem repeat domain may contribute to these functions. Little information is available on the specific O-glycosylation of MUC1. One problem in identifying different MUC1 glycoforms has been that monoclonal antibodies raised against the MUC1 core protein recognize epitopes in the tandem repeat domain, which is often glycosylated to an extent that obscures these epitopes. We developed an epitope-tagged form of MUC1 that allowed the detection of multiple MUC1 glycoforms and established the presence of a number of important blood group and tumor-associated carbohydrate antigens on MUC1 expressed by two pancreatic tumor cell lines (Panc-1 and S2-013) and two colon tumor cell lines (Caco-2 and HT-29). Antigens detected include sialyl-Lewis(a), sialyl- Lewis(c), sialyl-Lewis(x), and sialyl-Tn.
AB - MUC1 is expressed at the apical surface of ductal epithelia of tissues, including breast, pancreas, airway, and the gastrointestinal tract, where its functions include lubrication and protection of the epithelia. In addition, roles for MUC1 have been suggested in both adhesive and antiadhesive properties of tumor cells, and extensive O-glycosylation of the MUC1 tandem repeat domain may contribute to these functions. Little information is available on the specific O-glycosylation of MUC1. One problem in identifying different MUC1 glycoforms has been that monoclonal antibodies raised against the MUC1 core protein recognize epitopes in the tandem repeat domain, which is often glycosylated to an extent that obscures these epitopes. We developed an epitope-tagged form of MUC1 that allowed the detection of multiple MUC1 glycoforms and established the presence of a number of important blood group and tumor-associated carbohydrate antigens on MUC1 expressed by two pancreatic tumor cell lines (Panc-1 and S2-013) and two colon tumor cell lines (Caco-2 and HT-29). Antigens detected include sialyl-Lewis(a), sialyl- Lewis(c), sialyl-Lewis(x), and sialyl-Tn.
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U2 - 10.1074/jbc.272.39.24198
DO - 10.1074/jbc.272.39.24198
M3 - Article
C2 - 9305871
AN - SCOPUS:0030827120
SN - 0021-9258
VL - 272
SP - 24198
EP - 24202
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 39
ER -