Conflicting views on the molecular structure of the cancer antigen CA125/MUC16

Article type: Research Article

Authors: Bouanene, Houda^; | Miled, Abdelhédi^;

Affiliations: Laboratory of Biochemistry and Molecular Biology, Faculty of Pharmacy, Monastir, Tunisia | Laboratory of Biochemistry, CHU Farhat Hached Sousse, Tunisia

Note: [] Corresponding author: Houda Bouanene, Laboratory of Biochemistry and Molecular Biology, Faculty of Pharmacy- 5000, Moanstir, Tunisia. Tel.: +216 73 21 95 03; Fax: +216 73 22 67 02; E-mail: [email protected]

Abstract: CA125 is a tumor antigen used to monitor the progression and regression of epithelial ovarian cancer. Despite the widespread use of CA125, the biochemical and molecular nature of this antigen is poorly understood. Analysis of the structure of CA125 is essential for determining the physiological role of this very significant tumor marker. Accumulated experimental evidence has shown that CA125 epitopes reside on a molecule of very complex architecture in terms of both protein backbone and oligosaccharide structures. It is not clear whether the heterogeneity of CA125 molecular characteristics are due to the variability of biological sources from which the molecule was isolated or to the different biophysical methods used for the characterization of all the oligosaccharides linked to CA125 or to the presence of glycoisoforms for this protein. This review attempts to summarize emerging data related to molecular characteristics of CA125 and to compare approaches undertaken to reach a better understanding of molecular features of this tumor marker.

Keywords: CA125 antigen, MUC16, glycosylation

DOI: 10.3233/DMA-2010-0719

Journal: Disease Markers, vol. 28, no. 6, pp. 385-394, 2010