open access

Vol 50, No 3 (2012)
Original paper
Submitted: 2012-10-08
Accepted: 2012-10-08
Published online: 2012-10-08
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Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin

Carlos Solórzano, Miguel Ángel Mayoral, María de los Angeles Carlos, Jaime Berumen, Jorge Guevara, Francisco Raúl Chávez, Guillermo Mendoza-Hernández, Concepción Agundis, Edgar Zenteno
DOI: 10.5603/FHC.2012.0054
·
Folia Histochem Cytobiol 2012;50(3):398-406.

open access

Vol 50, No 3 (2012)
ORIGINAL PAPERS
Submitted: 2012-10-08
Accepted: 2012-10-08
Published online: 2012-10-08

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.

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.
Get Citation
About this article
Title

Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin

Journal

Folia Histochemica et Cytobiologica

Issue

Vol 50, No 3 (2012)

Article type

Original paper

Pages

398-406

Published online

2012-10-08

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

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