Ovarian
carcinoma is the leading cause of death from gynecological
cancers in many Western countries. Aberrant glycosylation is an important aspect in malignant transformation and consequently in
ovarian cancer. In this study, a detailed structure analysis of the N-linked
glycans from total
glycoproteins from the SKOV3 ovarian
carcinoma cell line and from a recombinantly expressed secretory
glycoprotein,
erythropoietin (EPO), produced from the same cells has been performed using high-performance
anion exchange chromatography with pulsed amperometric detection and matrix-assisted
laser desorption/ionization time-of-flight mass spectrometry. Total cellular N-
glycans contained high-
mannose type and proximally fucosylated complex type partially agalactosylated structures. On the other hand, the recombinant human EPO secreted from SKOV3 cells contained predominantly core-fucosylated tetraantennary structures, which were partially lacking one or two
galactose residues, and partially contained the
LacdiNAc motif. Only minor amounts of di- and triantennary complex-type
glycans were found, and high-
mannose-type
glycans were not present in the secreted EPO
protein. A large amount of
N-acetylneuraminic acid in α2,3-linkage was detected as well. Endogenous
glycoproteins were also found to contain the
LacdiNAc motif in N-linked
glycans. This work contributes to the knowledge of the glycosylation of a human
ovarian cancer cell line. It also establishes the basis to further explore high-
mannose-type
glycans, and the
LacdiNAc motif as possible markers of ovarian
carcinoma.