CANCER-ASSOCIATED CARBOHYDRATES IDENTIFIED BY MONOCLONAL-ANTIBODIES

被引:163
作者
SELL, S
机构
[1] Department of Pathology, Laboratory Medicine, University of Texas Health Science Center at Houston, Houston, TX
关键词
cancer; carbohydrates; markers; monoclonal antibodies;
D O I
10.1016/0046-8177(90)90250-9
中图分类号
R36 [病理学];
学科分类号
100104 ;
摘要
"New" carbohydrate structures on the surface of or secreted by cancer cells, identified as epitopes by monoclonal antibodies, are reviewed. These structures may represent the accumulation of precursor chains because of decreased acivity of synthesizing enzymes, the production of new oligosaccharides due to increased or aberrant glycosylation of carbohydrate chains, a change in density of carbohydrates on the cell surface, or exposure of chains usually covered by other structures. Alterations in glycolipid synthesis include aberrant fucosylation and/or sialyation of the lacto series, sialylation or fucosylation of the globo series, and sialyation of the ganglio series. Many of these carbohydrate epitopes have become useful for the diagnosis, prognosis, and monitoring of patients with cancer. Some of the important markers include CA 15.3, CA 19.9, CA 50, CA 125, CA 242, MCA, SLEX, etc. Incomplete glycosylation of O-linked mucin oligosaccharide is recognized as the important "cancer antigen" B72.3, which is sialyated Tn. The oligosaccharide components of α-fetoprotein, carcinoembryonic antigen, and epidermal growth factor receptor are also reviewed. In many instances the glycosylation seen in cancer cells or their products reflects patterns seen during normal development. Thus, cancer-associated oligosaccharides are oncodevelopmental in nature. The biologic significance of carbohydrates on cell surfaces is not known, but several possibilities include a role in cell to cell recognition, intracellular processing of glycoproteins, cell activation, and ability of cancer cells to metastasize. © 1990.
引用
收藏
页码:1003 / 1019
页数:17
相关论文
共 157 条
[1]  
ABE K, 1983, J BIOL CHEM, V258, P1793
[2]  
Abelev G I, 1971, Adv Cancer Res, V14, P295, DOI 10.1016/S0065-230X(08)60523-0
[3]  
ALPERT E, 1972, J BIOL CHEM, V247, P3792
[4]   BLOOD-GROUP-RELATED ANTIGENS IN COLONIC CARCINOGENESIS [J].
BARA, J ;
DECAENS, C .
ANNALES DE L INSTITUT PASTEUR-IMMUNOLOGY, 1987, 138 (06) :891-899
[5]   STUDIES OF MAMMARY-CARCINOMA METASTASIS IN A MOUSE MODEL SYSTEM .2. LECTIN BINDING-PROPERTIES OF CELLS IN RELATION TO THE INCIDENCE AND ORGAN DISTRIBUTION OF METASTASES [J].
BARNETT, SC ;
ECCLES, SA .
CLINICAL & EXPERIMENTAL METASTASIS, 1984, 2 (04) :297-310
[6]  
BHARGAVA A K, 1988, Journal of Tumor Marker Oncology, V3, P379
[7]   LEWIS BLOOD-GROUP ANTIGENS DEFINED BY MONOCLONAL ANTI-COLON CARCINOMA ANTIBODIES [J].
BLASZCZYK, M ;
HANSSON, GC ;
KARLSSON, KA ;
LARSON, G ;
STROMBERG, N ;
THURIN, J ;
HERLYN, M ;
STEPLEWSKI, Z ;
KOPROWSKI, H .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1984, 233 (01) :161-168
[8]   MICROHETEROGENEITY OF HUMAN ALPHAFETOPROTEIN [J].
BREBOROWICZ, J .
TUMOR BIOLOGY, 1988, 9 (01) :3-14
[9]  
BREMER EG, 1984, J BIOL CHEM, V259, P4773
[10]   A MONOCLONAL-ANTIBODY AGAINST HUMAN COLONIC ADENOMA RECOGNIZES DIFUCOSYLATED TYPE-2-BLOOD-GROUP CHAINS [J].
BROWN, A ;
FEIZI, T ;
GOOI, HC ;
EMBLETON, MJ ;
PICARD, JK ;
BALDWIN, RW .
BIOSCIENCE REPORTS, 1983, 3 (02) :163-170