Vol 50, No 3 (2012)
Original paper
Published online: 2012-10-08
Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin
DOI: 10.5603/FHC.2012.0054
Folia Histochem Cytobiol 2012;50(3):398-406.
Abstract
In cervical cancer, glycosylation has been suggested as being involved in both its carcinogenesis and
invasive capacity. In this work, we analyzed mucin type O-glycosylation in biopsies of invasive cervical cancer in
FIGO stage II B through histochemistry using lectins specific for O-glycosidically linked glycans. Our results
reveal that the lectin Machaerocereus eruca (MeA, specific for Gal in a Fuca1,2 (GalNAca1,3) Galb1,4) showed
increased recognition of tumoral cells and tumoral stroma tissue compared to other lectins with similar specificity;
healthy cervical tissue was negative for MeA. Trypsin treatment of recognized tissues abolished MeA’s recognition;
moreover, interaction of MeA was inhibited with oligosaccharides from mucin. As demonstrated by
Western blot of 2-D electrophoresis, MeA recognized ten glycoproteins in the range from 122 to 42 kDa in
cervical cancer lysates. The LC-ESI-MS/MS analysis of the MeAs’ recognized peptides revealed that the latter
matched mainly with the amino acid sequences of lamin A/C, vimentin, elongation factor 2, keratin 1, and beta
actin. Our results suggest that MeA recognizes a complex of over-expressed O-glycosidically-linked proteins that
play a relevant role in cervical cancer’s invasive capacity. O-glycosylation participates in the disassembly of intercellular
junctions favoring cancer progression.
invasive capacity. In this work, we analyzed mucin type O-glycosylation in biopsies of invasive cervical cancer in
FIGO stage II B through histochemistry using lectins specific for O-glycosidically linked glycans. Our results
reveal that the lectin Machaerocereus eruca (MeA, specific for Gal in a Fuca1,2 (GalNAca1,3) Galb1,4) showed
increased recognition of tumoral cells and tumoral stroma tissue compared to other lectins with similar specificity;
healthy cervical tissue was negative for MeA. Trypsin treatment of recognized tissues abolished MeA’s recognition;
moreover, interaction of MeA was inhibited with oligosaccharides from mucin. As demonstrated by
Western blot of 2-D electrophoresis, MeA recognized ten glycoproteins in the range from 122 to 42 kDa in
cervical cancer lysates. The LC-ESI-MS/MS analysis of the MeAs’ recognized peptides revealed that the latter
matched mainly with the amino acid sequences of lamin A/C, vimentin, elongation factor 2, keratin 1, and beta
actin. Our results suggest that MeA recognizes a complex of over-expressed O-glycosidically-linked proteins that
play a relevant role in cervical cancer’s invasive capacity. O-glycosylation participates in the disassembly of intercellular
junctions favoring cancer progression.
