



@article {3324,
	title = {DNAJB4 molecular chaperone distinguishes WT from mutant E-cadherin, determining their fate in vitro and in vivo},
	journal = {Human Molecular Genetics},
	volume = {23},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {2094 - 2105},
	abstract = {E-cadherin (Ecad) is a well-known invasion suppressor and its loss of expression is common in invasive carcinomas. Germline Ecad mutations are the only known genetic cause of hereditary diffuse gastric cancer (HDGC), demonstrating the causative role of Ecad impairment in gastric cancer. HDGC-associated Ecad missense mutations can lead to folding defects and premature proteasome-dependent endoplasmic reticulum-associated degradation (ERAD), but the molecular determinants for this fate were unidentified. Using a Drosophilabased genetic screen, we found that Drosophila DnaJ-1 interacts with wild type (WT) and mutant human Ecad in vivo. DnaJ (Hsp40) homolog, subfamily B, member 4 (DNAJB4), the human homolog of DnaJ-1, influences Ecad localization and stability even in the absence of Ecad endogenous promoter, suggesting a post-transcriptional level of regulation. Increased expression of DNAJB4 leads to stabilization of WT Ecad in the plasma membrane, while it induces premature degradation of unfolded HDGC mutants in the proteasome. The interaction between DNAJB4 and Ecad is direct, and is increased in the context of the unfolded mutant E757K, especially when proteasome degradation is inhibited, suggesting that DNAJB4 is a molecular mediator of ERAD. Post-translational regulation of native Ecad by DNAJB4 molecular chaperone is sufficient to influence cell adhesion in vitro. Using a chick embryo chorioallantoic membrane assay with gastric cancer derived cells, we demonstrate that DNAJB4 stimulates the anti-invasive function of WT Ecad in vivo. Additionally, the expression of DNAJB4 and Ecad is concomitantly decreased in human gastric carcinomas. Altogether, we demonstrate that DNAJB4 is a sensor of Ecad structural features that might contribute to gastric cancer progression. {\textcopyright} The Author 2013. Published by Oxford University Press. All rights reserved.},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84897831766\&partnerID=40\&md5=c7651a5372b8a46de1f028888590b3f3},
	author = {Sim{\~o}es-Correia, J. and Silva, D.I. and Melo, S. and Figueiredo, J. and Caldeira, J. and Pinto, M.T. and Gir{\~a}o, H. and Pereira, P. and Seruca, R.}
}
@article {2189,
	title = {E-cadherin dysfunction in gastric cancer - Cellular consequences, clinical applications and open questions},
	journal = {FEBS LettersFEBS Lett.},
	volume = {586},
	year = {2012},
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},
	month = {2012///},
	pages = {2981 - 2989},
	abstract = {E-cadherin plays a major role in cell-cell adhesion and inactivating germline mutations in its encoding gene predispose to hereditary diffuse gastric cancer. Evidence indicates that aside from its recognized role in early tumourigenesis, E-cadherin is also pivotal for tumour progression, including invasion and metastization. Herein, we discuss E-cadherin alterations found in a cancer context, associated cellular effects and signalling pathways, and we raise new key questions that will impact in the management of GC patients and families. {\textcopyright} 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.},
	keywords = {Adhesion, Cadherins, cancer growth, cancer invasion, cancer patient, cancer susceptibility, cell adhesion, complex formation, conference paper, E-cadherin, embryo development, endocytosis, epigenetics, epithelial mesenchymal transition, Gastric cancer, gene mutation, gene silencing, genetic susceptibility, Germ-Line Mutation, HDGC, Helicobacter infection, Helicobacter Infections, Helicobacter pylori, histone deacetylase inhibitor, human, Humans, Invasion, metastasis, molecular pathology, nonhuman, priority journal, protein analysis, protein depletion, protein expression, protein function, protein structure, regulatory mechanism, signal transduction, Signalling, stomach cancer, stomach carcinogenesis, Stomach Neoplasms, Tumour, uvomorulin},
	isbn = {00145793 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84864922992\&partnerID=40\&md5=455ae054dc6c8f95dc9e81d77fec1ad9},
	author = {Carneiro, P. and Fernandes, M.S. and Figueiredo, J. and Caldeira, J. and Carvalho, J. and Pinheiro, H. and Leite, M. and Melo, S. and Oliveira, P. and Sim{\~o}es-Correia, J. and Oliveira, M.J. and Carneiro, F. and Figueiredo, C. and Paredes, J. and Oliveira, C. and Seruca, R.}
}
@article {2177,
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	journal = {Biochimica et Biophysica Acta - Reviews on CancerBiochim. Biophys. Acta Rev. Cancer},
	volume = {1826},
	year = {2012},
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},
	month = {2012///},
	pages = {297 - 311},
	abstract = {E-cadherin and P-cadherin are major contributors to cell-cell adhesion in epithelial tissues, playing pivotal roles in important morphogenetic and differentiation processes during development, and in maintaining integrity and homeostasis in adult tissues. It is now generally accepted that alterations in these two molecules are observed during tumour progression of most carcinomas. Genetic or epigenetic alterations in E- and P-cadherin-encoding genes (CDH1 and CDH3, respectively), or alterations in their proteins expression, often result in tissue disorder, cellular de-differentiation, increased invasiveness of tumour cells and ultimately in metastasis. In this review, we will discuss the major properties of E- and P-cadherin molecules, its regulation in normal tissue, and their alterations and role in cancer, with a specific focus on gastric and breast cancer models. {\textcopyright} 2012 Elsevier B.V.},
	keywords = {antineoplastic activity, antineoplastic agent, Breast, breast cancer, Cancer, cancer chemotherapy, cancer model, cancer survival, drug effect, E-cadherin, Gastric, gene expression regulation, gene function, gene location, gene overexpression, gene structure, genetic association, genetic code, Helicobacter infection, Hereditary diffuse gastric cancer, human, in vivo study, loss of function mutation, lymph node metastasis, malignant neoplastic disease, molecular dynamics, molecular pathology, molecularly targeted therapy, nonhuman, P cadherin, P cadherin gene, P-cadherin, pf 03732010, priority journal, protein expression, protein function, protein inhibitor, protein processing, review, signal transduction, stomach cancer, transcription regulation, tumor gene, unclassified drug, uvomorulin, uvomorulin gene, vasculotropin inhibitor},
	isbn = {0304419X (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84861800037\&partnerID=40\&md5=2d52be63f4168a561b1bda1315e1f429},
	author = {Paredes, J. and Figueiredo, J. and Albergaria, A. and Oliveira, P. and Carvalho, J. and Ribeiro, A.S. and Caldeira, J. and Costa, A.M. and Sim{\~o}es-Correia, J. and Oliveira, M.J. and Pinheiro, H. and Pinho, S.S. and Mateus, R. and Reis, C.A. and Leite, M. and Fernandes, M.S. and Schmitt, F. and Carneiro, F. and Figueiredo, C. and Oliveira, C. and Seruca, R.}
}
