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Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin
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Abstract
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.
Abstract
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.
About this articleTitle
Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin
Journal
Folia Histochemica et Cytobiologica
Issue
Article type
Original paper
Pages
398-406
Published online
2012-10-08
Page views
2483
Article views/downloads
3118
DOI
10.5603/FHC.2012.0054
Bibliographic record
Folia Histochem Cytobiol 2012;50(3):398-406.
Authors
Carlos Solórzano
Miguel Ángel Mayoral
María de los Angeles Carlos
Jaime Berumen
Jorge Guevara
Francisco Raúl Chávez
Guillermo Mendoza-Hernández
Concepción Agundis
Edgar Zenteno
