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Prep Biochem Biotechnol ; 37(3): 219-28, 2007.
Artigo em Inglês | MEDLINE | ID: mdl-17516251

RESUMO

Alterations in O-glycosylation of proteins in cell surfaces can originate disorder in cellular function, as well as in cell transformation and tumoral differentiation. In this work, we investigate changes in O-glycosylation in cervical intraepithelial dysplasia (CIN) at different stages of differentiation (CIN I, CIN II, and CIN III) using lectins specific for O-glycosidically linked glycans. Twenty cases with CIN I, CIN II, and CIN III dysplasias each, and 20 normal cases were studied by lectin histochemistry and evaluated under optical microscopy. The lectins from Glycine max and Griffonia simplicifolia showed no differences in their recognition pattern among the different CIN stages and normal tissue. Dolichos Biflorus lectin recognized CIN I dysplasia. Lectin from Amaranthus leucocarpus showed increased reactivity in the presence of CIN II dysplasia, compared with CIN I and CIN III. These results suggest that subtle modifications in the O-glycosylation pattern could be considered in diagnosis or prognosis of cervical precancerous stages.


Assuntos
Biomarcadores Tumorais/análise , Glicoproteínas/análise , Neoplasias de Células Escamosas/química , Lectinas de Plantas/análise , Displasia do Colo do Útero/patologia , Neoplasias do Colo do Útero/patologia , Amaranthus/química , Biópsia por Agulha , Diferenciação Celular , Dolichos/química , Feminino , Griffonia/química , Histocitoquímica , Humanos , Estadiamento de Neoplasias/métodos , Neoplasias de Células Escamosas/patologia , Ligação Proteica , Displasia do Colo do Útero/química , Displasia do Colo do Útero/diagnóstico , Neoplasias do Colo do Útero/química
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