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OncogeneVolume 30, Issue 11, 17 March 2011, Pages 1302-1317

Chromosomal, epigenetic and microRNA-mediated inactivation of LRP1B, a modulator of the extracellular environment of thyroid cancer cells(Article)(Open Access)

  • Prazeres, H.,
  • Torres, J.,
  • Rodrigues, F.,
  • Pinto, M.,
  • Pastoriza, M.C.,
  • Gomes, D.,
  • Cameselle-Teijeiro, J.,
  • Vidal, A.,
  • Martins, T.C.,
  • Sobrinho-Simões, M.,
  • Soares, P.
  • View Correspondence (jump link)
  • aDepartment of Cancer Biology, Institute of Molecular Pathology and Immunology, University of Porto (IPATIMUP), Rua Dr Roberto Frias s/n, Porto 4200-465, Portugal
  • bMedical Faculty, University of Porto, Porto, Portugal
  • cDepartment of Molecular Pathology, Service of the Portuguese Institute of Oncology of Coimbra, EPE, Coimbra, Portugal
  • dDepartment of Endocrinology, Service of the Portuguese Institute of Oncology of Coimbra, EPE, Coimbra, Portugal
  • eDepartment of Physiology, School of Medicine, University of Santiago de Compostela-Institute of Sanitary Research (IDIS), Santiago de Compostela, Spain
  • fAnatomic Pathology Service, Portuguese Institute of Oncology of Coimbra, EPE, Coimbra, Portugal
  • gDepartment of Anatomic Pathology, Clinical University Hospital (CHUS), University of Santiago de Compostela, Santiago de Compostela, Spain

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Corrigendum: Chromosomal, epigenetic and microRNA-mediated inactivation of LRP1B, a modulator of the extracellular environment of thyroid cancer cells (Oncogene (2010) 30 (1302-1317) DOI: 10.1038/onc.2010.512)

(2017) Oncogene, 36 (1), p. 146.

Abstract

The low-density lipoprotein receptor-related protein (LRP1B), encoding an endocytic LDL-family receptor, is among the 10 most significantly deleted genes across 3312 human cancer specimens. However, currently the apparently crucial role of this lipoprotein receptor in carcinogenesis is not clear. Here we show that LRP1B inactivation (by chromosomal, epigenetic and microRNA (miR)-mediated mechanisms) results in changes to the tumor environment that confer cancer cells an increased growth and invasive capacity. LRP1B displays frequent DNA copy number loss and CpG island methylation, resulting in mRNA underexpression. By using CpG island reporters methylated in vitro, we found that DNA methylation disrupts a functional binding site for the histone-acetyltransferase p300 located at intron 1. We identified and validated an miR targeting LRP1B (miR-548a-5p), which is overexpressed in cancer cell lines as a result of 8q22 DNA gains. Restoration of LRP1B impaired in vitro and in vivo tumor growth, inhibited cell invasion and led to a reduction of matrix metalloproteinase 2 in the extracellular medium. We emphasized the role of an endocytic receptor acting as a tumor suppressor by modulating the extracellular environment composition in a way that constrains the invasive behavior of the cancer cells. © 2011 Macmillan Publishers Limited All rights reserved.

Author keywords

endocytosis and tumor microenvironmentEP300 histone-acetyltransferaselow-density lipoprotein receptor familymatrix metalloproteinase 2microRNAtumor suppressor gene

Indexed keywords

EMTREE drug terms:histone acetyltransferaselow density lipoprotein receptor related proteinmatrix metalloproteinasemicroRNA
EMTREE medical terms:animal cellarticlebinding sitecancer cell culturecancer inhibitioncancer invasionchromosomecontrolled studyCpG islandDNA methylationembryoendosomeepigeneticsextracellular matrixgene dosagegene expressionhumanhuman cellin vitro studyintronnonhumanpriority journalthyroid cancertumor growthtumor microenvironmenttumor suppressor gene

Chemicals and CAS Registry Numbers:

histone acetyltransferase, 9054-51-7

Funding details

Funding sponsor Funding number Acronym
Ministry of Science, Technology and Space
Ministerio de Ciencia e InnovaciónMICINN
SFRH/BD30041/2006,PTDC/SAU-OBD/101242/2008
Instituto de Salud Carlos III
PS09/02050-FEDER,13/2007

  • 1

    We would like to acknowledge funding from grants from the Portuguese Foundation for Science and Technology (SFRH/BD30041/2006 and PTDC/SAU-OBD/101242/2008), the Portuguese Society of Endocrinology and Metabolism (Edward Limber Prize) and the Portuguese Ministry of Health (project 13/2007). José Cameselle-Teijeiro was supported by Grant PS09/02050-FEDER, from the Ministry of Science and Innovation (Instituto de Salud Carlos III), Spain. IPATIMUP is an associated laboratory of the Portuguese Ministry of Science, Technology and Higher Education and is partially supported by the Portuguese Foundation for Science and Technology.

  • ISSN: 09509232
  • CODEN: ONCNE
  • Source Type: Journal
  • Original language: English
  • DOI: 10.1038/onc.2010.512
  • PubMed ID: 21057533
  • Document Type: Article
  • Publisher: Nature Publishing Group

  Soares, P.; Department of Cancer Biology, Institute of Molecular Pathology and Immunology, University of Porto (IPATIMUP), Rua Dr Roberto Frias s/n, Portugal;
© Copyright 2017 Elsevier B.V., All rights reserved.

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