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O-glycan sialylation alters galectin-3 subcellular localization and decreases chemotherapy sensitivity in gastric cancer.
Santos, Sofia N; Junqueira, Mara S; Francisco, Guilherme; Vilanova, Manuel; Magalhães, Ana; Dias Baruffi, Marcelo; Chammas, Roger; Harris, Adrian L; Reis, Celso A; Bernardes, Emerson S.
Afiliação
  • Santos SN; Department of Radiopharmacy, Nuclear Energy Research Institute, Radiopharmacy Center, São Paulo, Brazil.
  • Junqueira MS; Department of Center for Translational Oncology Cellular, Biology Group, Center for Translational Oncology, Cancer Institute of the State of Sao Paulo-ICESP, Brazil.
  • Francisco G; Department of Center for Translational Oncology Cellular, Biology Group, Center for Translational Oncology, Cancer Institute of the State of Sao Paulo-ICESP, Brazil.
  • Vilanova M; I3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Portugal.
  • Magalhães A; IBMC Instituto de Biologia Molecular e Celular, Universidade do Porto, Portugal.
  • Dias Baruffi M; ICBAS-UP - Instituto de Ciências Biomédicas Abel Salazar, University of Porto, Porto, Portugal.
  • Chammas R; I3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Portugal.
  • Harris AL; Department of Glycobiology in Cancer, IPATIMUP - Institute of Molecular Pathology and Immunology from the University of Porto, Porto, Portugal.
  • Reis CA; Department of Clinical, Toxicological and Bromatological Analysis, Faculdade de Ciências Farmaceuticas de Ribeirão Preto, Universidade de São Paulo, Brazil.
  • Bernardes ES; Department of Center for Translational Oncology Cellular, Biology Group, Center for Translational Oncology, Cancer Institute of the State of Sao Paulo-ICESP, Brazil.
Oncotarget ; 7(50): 83570-83587, 2016 Dec 13.
Article em En | MEDLINE | ID: mdl-27835877
ST6GalNAc-I, the sialyltransferase responsible for sialyl-Tn (sTn) synthesis, has been previously reported to be positively associated with cancer aggressiveness. Here we describe a novel sTn-dependent mechanism for chemotherapeutic resistance. We show that sTn protects cancer cells against chemotherapeutic-induced cell death by decreasing the interaction of cell surface glycan receptors with galectin-3 and increasing its intracellular accumulation. Moreover, exogenously added galectin-3 potentiated the chemotherapeutics-induced cytotoxicity in sTn non-expressing cells, while sTn overexpressing cells were protected. We also found that the expression of sTn was associated with a reduction in galectin-3-binding sites in human gastric samples tumors. ST6GalNAc-I knockdown restored galectin-3-binding sites on the cell surface and chemotherapeutics sensibility. Our results clearly demonstrate that an interruption of O-glycans extension caused by ST6GalNAc-I enzymatic activity leads to tumor cells resistance to chemotherapeutic drugs, highlighting the need for the development of novel strategies to target galectin-3 and/or ST6GalNAc-I.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Neoplasias Gástricas / Cisplatino / Resistencia a Medicamentos Antineoplásicos / Galectina 3 / Antineoplásicos Tipo de estudo: Diagnostic_studies Limite: Animals / Humans Idioma: En Revista: Oncotarget Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos
Texto completo
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Neoplasias Gástricas / Cisplatino / Resistencia a Medicamentos Antineoplásicos / Galectina 3 / Antineoplásicos Tipo de estudo: Diagnostic_studies Limite: Animals / Humans Idioma: En Revista: Oncotarget Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos