Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 379, Issue 4, Pages 1091-1096Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.01.024
Keywords
E cadherin; N glycosylation; Mammary gland tumor; Adenoma; Carcinoma; Canine
Categories
Funding
- FCT [FFDC/CVT/65537/2006, SFRH/BD/21693/2005]
- financiado no Ambito do POCI [2010]
- do Quadro Comunitario de Apoio III e comparticipado pelo FEDER
- FLAD
- Fundação para a Ciência e a Tecnologia [SFRH/BD/21693/2005] Funding Source: FCT
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Modifications in cell surface glycosylation affecting cell adhesion are common characteristics of transformed cells. This study characterizes the N-glycosylation profile of E-cadherin in models of canine mammary gland adenoma and carcinoma evaluating the importance of these glycosylation modifications in the malignant phenotype. Our results show that the pattern of E-cadherin N-glycosylation in mammary carcinoma is characterized by highly branched N-glycans, increase in sialylation and an expression of few high mannose structures. Detailed mass spectrometry analysis demonstrated a new N-glycosylation site containing a potential complex type N-glycan in E-cadherin from a mammary carcinoma cell line. Our study demonstrates the importance of E-cadherin N-glycans in the process of tumor development and in the transformation to the malignant phenotype. (C) 2009 Elsevier Inc. All rights reserved.
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