Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin
In cervical cancer, glycosylation has been suggested as being involved in both its carcinogenesis and<br />invasive capacity. In this work, we analyzed mucin type O-glycosylation in biopsies of invasive cervical cancer in<br />FIGO stage II B through histochemistry using...
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| Format: | Article |
| Language: | English |
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Via Medica
2012-10-01
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| Series: | Folia Histochemica et Cytobiologica |
| Online Access: | http://czasopisma.viamedica.pl/fhc/article/view/19748 |
| _version_ | 1811306561786609664 |
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| author | Carlos Solórzano Miguel Ángel Mayoral María de los Angeles Carlos Jaime Berumen Jorge Guevara Francisco Raúl Chávez Guillermo Mendoza-Hernández Concepción Agundis Edgar Zenteno |
| author_facet | Carlos Solórzano Miguel Ángel Mayoral María de los Angeles Carlos Jaime Berumen Jorge Guevara Francisco Raúl Chávez Guillermo Mendoza-Hernández Concepción Agundis Edgar Zenteno |
| author_sort | Carlos Solórzano |
| collection | DOAJ |
| description | In cervical cancer, glycosylation has been suggested as being involved in both its carcinogenesis and<br />invasive capacity. In this work, we analyzed mucin type O-glycosylation in biopsies of invasive cervical cancer in<br />FIGO stage II B through histochemistry using lectins specific for O-glycosidically linked glycans. Our results<br />reveal that the lectin Machaerocereus eruca (MeA, specific for Gal in a Fuca1,2 (GalNAca1,3) Galb1,4) showed<br />increased recognition of tumoral cells and tumoral stroma tissue compared to other lectins with similar specificity;<br />healthy cervical tissue was negative for MeA. Trypsin treatment of recognized tissues abolished MeA’s recognition;<br />moreover, interaction of MeA was inhibited with oligosaccharides from mucin. As demonstrated by<br />Western blot of 2-D electrophoresis, MeA recognized ten glycoproteins in the range from 122 to 42 kDa in<br />cervical cancer lysates. The LC-ESI-MS/MS analysis of the MeAs’ recognized peptides revealed that the latter<br />matched mainly with the amino acid sequences of lamin A/C, vimentin, elongation factor 2, keratin 1, and beta<br />actin. Our results suggest that MeA recognizes a complex of over-expressed O-glycosidically-linked proteins that<br />play a relevant role in cervical cancer’s invasive capacity. O-glycosylation participates in the disassembly of intercellular<br />junctions favoring cancer progression.<br>In cervical cancer, glycosylation has been suggested as being involved in both its carcinogenesis and<br />invasive capacity. In this work, we analyzed mucin type O-glycosylation in biopsies of invasive cervical cancer in<br />FIGO stage II B through histochemistry using lectins specific for O-glycosidically linked glycans. Our results<br />reveal that the lectin Machaerocereus eruca (MeA, specific for Gal in a Fuca1,2 (GalNAca1,3) Galb1,4) showed<br />increased recognition of tumoral cells and tumoral stroma tissue compared to other lectins with similar specificity;<br />healthy cervical tissue was negative for MeA. Trypsin treatment of recognized tissues abolished MeA’s recognition;<br />moreover, interaction of MeA was inhibited with oligosaccharides from mucin. As demonstrated by<br />Western blot of 2-D electrophoresis, MeA recognized ten glycoproteins in the range from 122 to 42 kDa in<br />cervical cancer lysates. The LC-ESI-MS/MS analysis of the MeAs’ recognized peptides revealed that the latter<br />matched mainly with the amino acid sequences of lamin A/C, vimentin, elongation factor 2, keratin 1, and beta<br />actin. Our results suggest that MeA recognizes a complex of over-expressed O-glycosidically-linked proteins that<br />play a relevant role in cervical cancer’s invasive capacity. O-glycosylation participates in the disassembly of intercellular<br />junctions favoring cancer progression. |
| first_indexed | 2024-04-13T08:46:25Z |
| format | Article |
| id | doaj.art-47d46fc6228b448eb0fa504cab1267b0 |
| institution | Directory Open Access Journal |
| issn | 0239-8508 1897-5631 |
| language | English |
| last_indexed | 2024-04-13T08:46:25Z |
| publishDate | 2012-10-01 |
| publisher | Via Medica |
| record_format | Article |
| series | Folia Histochemica et Cytobiologica |
| spelling | doaj.art-47d46fc6228b448eb0fa504cab1267b02022-12-22T02:53:38ZengVia MedicaFolia Histochemica et Cytobiologica0239-85081897-56312012-10-0150339840610.5603/19748Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutininCarlos SolórzanoMiguel Ángel MayoralMaría de los Angeles CarlosJaime BerumenJorge GuevaraFrancisco Raúl ChávezGuillermo Mendoza-HernándezConcepción AgundisEdgar ZentenoIn cervical cancer, glycosylation has been suggested as being involved in both its carcinogenesis and<br />invasive capacity. In this work, we analyzed mucin type O-glycosylation in biopsies of invasive cervical cancer in<br />FIGO stage II B through histochemistry using lectins specific for O-glycosidically linked glycans. Our results<br />reveal that the lectin Machaerocereus eruca (MeA, specific for Gal in a Fuca1,2 (GalNAca1,3) Galb1,4) showed<br />increased recognition of tumoral cells and tumoral stroma tissue compared to other lectins with similar specificity;<br />healthy cervical tissue was negative for MeA. Trypsin treatment of recognized tissues abolished MeA’s recognition;<br />moreover, interaction of MeA was inhibited with oligosaccharides from mucin. As demonstrated by<br />Western blot of 2-D electrophoresis, MeA recognized ten glycoproteins in the range from 122 to 42 kDa in<br />cervical cancer lysates. The LC-ESI-MS/MS analysis of the MeAs’ recognized peptides revealed that the latter<br />matched mainly with the amino acid sequences of lamin A/C, vimentin, elongation factor 2, keratin 1, and beta<br />actin. Our results suggest that MeA recognizes a complex of over-expressed O-glycosidically-linked proteins that<br />play a relevant role in cervical cancer’s invasive capacity. O-glycosylation participates in the disassembly of intercellular<br />junctions favoring cancer progression.<br>In cervical cancer, glycosylation has been suggested as being involved in both its carcinogenesis and<br />invasive capacity. In this work, we analyzed mucin type O-glycosylation in biopsies of invasive cervical cancer in<br />FIGO stage II B through histochemistry using lectins specific for O-glycosidically linked glycans. Our results<br />reveal that the lectin Machaerocereus eruca (MeA, specific for Gal in a Fuca1,2 (GalNAca1,3) Galb1,4) showed<br />increased recognition of tumoral cells and tumoral stroma tissue compared to other lectins with similar specificity;<br />healthy cervical tissue was negative for MeA. Trypsin treatment of recognized tissues abolished MeA’s recognition;<br />moreover, interaction of MeA was inhibited with oligosaccharides from mucin. As demonstrated by<br />Western blot of 2-D electrophoresis, MeA recognized ten glycoproteins in the range from 122 to 42 kDa in<br />cervical cancer lysates. The LC-ESI-MS/MS analysis of the MeAs’ recognized peptides revealed that the latter<br />matched mainly with the amino acid sequences of lamin A/C, vimentin, elongation factor 2, keratin 1, and beta<br />actin. Our results suggest that MeA recognizes a complex of over-expressed O-glycosidically-linked proteins that<br />play a relevant role in cervical cancer’s invasive capacity. O-glycosylation participates in the disassembly of intercellular<br />junctions favoring cancer progression.http://czasopisma.viamedica.pl/fhc/article/view/19748 |
| spellingShingle | Carlos Solórzano Miguel Ángel Mayoral María de los Angeles Carlos Jaime Berumen Jorge Guevara Francisco Raúl Chávez Guillermo Mendoza-Hernández Concepción Agundis Edgar Zenteno Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin Folia Histochemica et Cytobiologica |
| title | Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin |
| title_full | Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin |
| title_fullStr | Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin |
| title_full_unstemmed | Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin |
| title_short | Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin Overexpression of glycosylated proteins in cervical cancer recognized by the Machaerocereus eruca agglutinin |
| title_sort | overexpression of glycosylated proteins in cervical cancer recognized by the machaerocereus eruca agglutinin overexpression of glycosylated proteins in cervical cancer recognized by the machaerocereus eruca agglutinin |
| url | http://czasopisma.viamedica.pl/fhc/article/view/19748 |
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