Shaping the Immune Landscape in Cancer by Galectin-Driven Regulatory Pathways

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Along with the discovery of tumor-driven inflammatory pathways, there has been a considerable progress over the past 10 years in understanding the mechanisms leading to cancer immunosurveillance and immunoediting. Several regulatory pathways, typically involved in immune cell homeostasis, are co-opt...

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Autor principal: Rabinovich, G.A
Otros Autores: Conejo-García, J.R
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Academic Press 2016
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-84975256659 
024 7 |2 cas  |a galectin 1, 258495-34-0; galectin 3, 208128-56-7; galectin 8, 220452-97-1; interleukin 2, 85898-30-2; leukosialin, 123897-54-1; n acetylglucosaminyltransferase, 9054-49-3; protein, 67254-75-5; Galectins; Ligands 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a JMOBA 
100 1 |a Rabinovich, G.A. 
245 1 0 |a Shaping the Immune Landscape in Cancer by Galectin-Driven Regulatory Pathways 
260 |b Academic Press  |c 2016 
270 1 0 |m Rabinovich, G.A.; Laboratorio de Inmunopatología, Instituto de Biología y Medicina Experimental (IBYME), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Vuelta de Obligado 2490, Argentina; email: gabyrabi@gmail.com 
506 |2 openaire  |e Política editorial 
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504 |a Novak, R., Dabelic, S., Dumic, J., Galectin-1 and galectin-3 expression profiles in classically and alternatively activated human macrophages (2012) Biochim. Biophys. Acta., 1820, pp. 1383-1390 
504 |a Cubillos-Ruiz, J.R., Silberman, P.C., Rutkowski, M.R., Chopra, S., Perales-Puchalt, A., Song, M., ER stress sensor XBP1 controls antitumor immunity by disrupting dendritic cell homeostasis (2015) Cell., 161, pp. 1527-1538 
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504 |a Ivanov, I.I., Frutos Rde, L., Manel, N., Yoshinaga, K., Rifkin, D.B., Sartor, R.B., Specific microbiota direct the differentiation of IL-17-producing T-helper cells in the mucosa of the small intestine (2008) Cell Host Microbe., 4, pp. 337-349 
504 |a Wei, B., Wingender, G., Fujiwara, D., Chen, D.Y., McPherson, M., Brewer, S., Commensal microbiota and CD8 + T cells shape the formation of invariant NKT cells (2010) J. Immunol., 184, pp. 1218-1226 
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504 |a Sivan, A., Corrales, L., Hubert, N., Williams, J.B., Aquino-Michaels, K., Earley, Z.M., Commensal Bifidobacterium promotes antitumor immunity and facilitates anti-PD-L1 efficacy (2015) Science, 110, pp. 1084-1089 
504 |a Vetizou, M., Pitt, J.M., Daillere, R., Lepage, P., Waldschmitt, N., Flament, C., Anticancer immunotherapy by CTLA-4 blockade relies on the gut microbiota (2015) Science., 350, pp. 1079-1084 
504 |a Rabinovich, G.A., Thijssen, V.L., Introduction to special issue: Galectins go with the flow (2014) Glycobiology., 24, p. 885 
504 |a Thijssen, V.L., Griffioen, A.W., Galectin-1 and − 9 in angiogenesis: a sweet couple (2014) Glycobiology., 24, pp. 915-920 
504 |a Funasaka, T., Raz, A., Nangia-Makker, P., Galectin-3 in angiogenesis and metastasis (2014) Glycobiology., 24, pp. 886-891 
504 |a Troncoso, M.F., Ferragut, F., Bacigalupo, M.L., Cardenas Delgado, V.M., Nugnes, L.G., Gentilini, L., Galectin-8: a matricellular lectin with key roles in angiogenesis (2014) Glycobiology., 24, pp. 907-914 
504 |a Le, Q.T., Shi, G., Cao, H., Nelson, D.W., Wang, Y., Chen, E.Y., Galectin-1: a link between tumor hypoxia and tumor immune privilege (2005) J. Clin. Oncol., 23, pp. 8932-8941 
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504 |a Rabinovich, G.A., Cumashi, A., Bianco, G.A., Ciavardelli, D., Iurisci, I., D'Egidio, M., Synthetic lactulose amines: novel class of anticancer agents that induce tumor-cell apoptosis and inhibit galectin-mediated homotypic cell aggregation and endothelial cell morphogenesis (2006) Glycobiology., 16, pp. 210-220 
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504 |a Iurisci, I., Cumashi, A., Sherman, A.A., Tsvetkov, Y.E., Tinari, N., Piccolo, E., Consorzio Interuniversitario Nazionale Per la, B.-O., Synthetic inhibitors of galectin-1 and -3 selectively modulate homotypic cell aggregation and tumor cell apoptosis (2009) Anticancer Res., 29, pp. 403-410 
504 |a Stannard, K.A., Collins, P.M., Ito, K., Sullivan, E.M., Scott, S.A., Gabutero, E., Darren Grice, I., Ralph, S.J., Galectin inhibitory disaccharides promote tumour immunity in a breast cancer model (2010) Cancer Lett., 299, pp. 95-110 
504 |a Thijssen, V.L., Postel, R., Brandwijk, R.J., Dings, R.P., Nesmelova, I., Satijn, S., Galectin-1 is essential in tumor angiogenesis and is a target for antiangiogenesis therapy (2006) Proc. Natl. Acad. Sci. U. S. A., 103, pp. 15975-15980 
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504 |a Nangia-Makker, P., Hogan, V., Honjo, Y., Baccarini, S., Tait, L., Bresalier, R., Raz, A., Inhibition of human cancer cell growth and metastasis in nude mice by oral intake of modified citrus pectin (2002) J. Natl. Cancer Inst., 94, pp. 1854-1862 
520 3 |a Along with the discovery of tumor-driven inflammatory pathways, there has been a considerable progress over the past 10 years in understanding the mechanisms leading to cancer immunosurveillance and immunoediting. Several regulatory pathways, typically involved in immune cell homeostasis, are co-opted by cancer cells to thwart the development of effective antitumor responses. These regulatory circuits include the engagement of inhibitory checkpoint pathways (CTLA-4, PD-1/PD-L1, LAG-3 and TIM-3), secretion of immunosuppressive cytokines (TGF-β, IL-10), and expansion and/or recruitment of myeloid or lymphoid regulatory cell populations. Elucidation of these pathways has inspired the design and implementation of novel immunotherapeutic modalities, which have already generated clinical benefits in an important number of cancer patients. Galectins, a family of glycan-binding proteins widely expressed in the tumor microenvironment (TME), have emerged as key players in immune evasion programs that differentially control the fate of effector and regulatory lymphoid and myeloid cell populations. How do galectins translate glycan-containing information into cellular programs that control immune regulatory cancer networks? Here, we uncover the selective roles of individual members of the galectin family in cancer-promoting inflammation, immunosuppression, and angiogenesis. Moreover, we highlight the relevance of corresponding glycosylated ligands and counter-receptors and the emerging function of these lectins as biological liaisons connecting commensal microbiota, systemic inflammation, and distal tumor growth. Understanding the molecular and cellular components of galectin-driven regulatory circuits, the implications of different glycosylation pathways in their functions and their clinical relevance in human cancer might lead to the development of new therapeutic approaches in a broad range of tumor types. © 2016 Elsevier Ltd  |l eng 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: PICT 2012-2440, PICT V 2014-367 
536 |a Detalles de la financiación: National Cancer Institute, P30CA10815, R01CA157664, R01CA178687, R01CA124515 
536 |a Detalles de la financiación: We would like to thank Diego Croci and Juan P. Cerliani for their insightful discussions and figures design. Work in G.A.R's lab is supported by grants from the Argentinean Agency for Promotion of Science and Technology ( PICT V 2014-367 ; PICT 2012-2440 ), University of Buenos Aires and Sales, Bunge & Born, Kenneth Raynin and René Baron Foundations. Work in J.R.C.G's lab is supported by NCI grants R01CA157664 , R01CA124515 , R01CA178687 , and P30CA10815 , and The Jayne Koskinas & Ted Giovanis Breast Cancer Research Consortium at Wistar. 
593 |a Laboratorio de Inmunopatología, Instituto de Biología y Medicina Experimental (IBYME), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Vuelta de Obligado 2490, Buenos Aires, C1428, Argentina 
593 |a Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Buenos Aires, C1428, Argentina 
593 |a Tumor Microenvironment and Metastasis Program, The Wistar Institute, Philadelphia, PA 19104, United States 
690 1 0 |a CANCER 
690 1 0 |a GALECTINS 
690 1 0 |a GLYCANS 
690 1 0 |a IMMUNOTHERAPY 
690 1 0 |a TUMOR IMMUNITY 
690 1 0 |a ACTIVATED LEUKOCYTE CELL ADHESION MOLECULE 
690 1 0 |a B LYMPHOCYTE RECEPTOR 
690 1 0 |a CD45 ANTIGEN 
690 1 0 |a CD7 ANTIGEN 
690 1 0 |a CYTOKINE RECEPTOR 
690 1 0 |a CYTOTOXIC T LYMPHOCYTE ANTIGEN 4 
690 1 0 |a ECALECTIN 
690 1 0 |a GALECTIN 
690 1 0 |a GALECTIN 1 
690 1 0 |a GALECTIN 10 
690 1 0 |a GALECTIN 3 
690 1 0 |a GALECTIN 8 
690 1 0 |a GLYCAN 
690 1 0 |a GLYCOLIPID 
690 1 0 |a GLYCOPROTEIN 
690 1 0 |a INTERLEUKIN 10 
690 1 0 |a INTERLEUKIN 15 
690 1 0 |a INTERLEUKIN 2 
690 1 0 |a INTERLEUKIN 4 
690 1 0 |a LAG 3 PROTEIN 
690 1 0 |a LEUKOSIALIN 
690 1 0 |a N ACETYLGLUCOSAMINYLTRANSFERASE 
690 1 0 |a NATURAL KILLER CELL RECEPTOR NKG2D 
690 1 0 |a PROGRAMMED DEATH 1 LIGAND 1 
690 1 0 |a PROTEIN 
690 1 0 |a T LYMPHOCYTE RECEPTOR 
690 1 0 |a TIM 3 PROTEIN 
690 1 0 |a TRANSFORMING GROWTH FACTOR BETA 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a UNINDEXED DRUG 
690 1 0 |a VASCULOTROPIN RECEPTOR 2 
690 1 0 |a GALECTIN 
690 1 0 |a LIGAND 
690 1 0 |a ANGIOGENESIS 
690 1 0 |a ANTIGEN PRESENTING CELL 
690 1 0 |a APOPTOSIS 
690 1 0 |a BONE MARROW CELL 
690 1 0 |a BREAST CANCER 
690 1 0 |a CANCER PATIENT 
690 1 0 |a CARBOHYDRATE SYNTHESIS 
690 1 0 |a CD8+ T LYMPHOCYTE 
690 1 0 |a CELL ADHESION 
690 1 0 |a CELL DIFFERENTIATION 
690 1 0 |a CELL MIGRATION 
690 1 0 |a CHRONIC LYMPHATIC LEUKEMIA 
690 1 0 |a CLASSICAL HODGKIN LYMPHOMA 
690 1 0 |a COMMENSAL 
690 1 0 |a CROSS LINKING 
690 1 0 |a CUTANEOUS T CELL LYMPHOMA 
690 1 0 |a CYTOKINE PRODUCTION 
690 1 0 |a CYTOKINE RELEASE 
690 1 0 |a CYTOTOXIC T LYMPHOCYTE 
690 1 0 |a ENDOTHELIUM CELL 
690 1 0 |a EPITHELIAL MESENCHYMAL TRANSITION 
690 1 0 |a FIBROBLAST 
690 1 0 |a GLYCOSYLATION 
690 1 0 |a HUMAN 
690 1 0 |a IMMUNE EVASION 
690 1 0 |a IMMUNOCOMPETENT CELL 
690 1 0 |a IMMUNOSUPPRESSIVE TREATMENT 
690 1 0 |a IMMUNOSURVEILLANCE 
690 1 0 |a INFLAMMATION 
690 1 0 |a INFLAMMATORY CELL 
690 1 0 |a INFLAMMATORY INFILTRATE 
690 1 0 |a KAPOSI SARCOMA 
690 1 0 |a LUNG ADENOCARCINOMA 
690 1 0 |a LYMPHOID CELL 
690 1 0 |a MALIGNANT NEOPLASTIC DISEASE 
690 1 0 |a MELANOMA 
690 1 0 |a MYCOSIS FUNGOIDES 
690 1 0 |a NATURAL KILLER CELL 
690 1 0 |a NON SMALL CELL LUNG CANCER 
690 1 0 |a NONHUMAN 
690 1 0 |a OVARY CANCER 
690 1 0 |a PANCREAS ADENOCARCINOMA 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROSTATE CARCINOMA 
690 1 0 |a PROTEIN PROTEIN INTERACTION 
690 1 0 |a REGULATORY T LYMPHOCYTE 
690 1 0 |a REVIEW 
690 1 0 |a SEZARY SYNDROME 
690 1 0 |a T CELL LYMPHOMA 
690 1 0 |a TH1 CELL 
690 1 0 |a TH17 CELL 
690 1 0 |a TUMOR GROWTH 
690 1 0 |a TUMOR IMMUNITY 
690 1 0 |a TUMOR MICROENVIRONMENT 
690 1 0 |a UPREGULATION 
690 1 0 |a ANIMAL 
690 1 0 |a IMMUNOLOGY 
690 1 0 |a NEOPLASM 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a ANIMALS 
690 1 0 |a GALECTINS 
690 1 0 |a GLYCOSYLATION 
690 1 0 |a HUMANS 
690 1 0 |a LIGANDS 
690 1 0 |a NEOPLASMS 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a TUMOR MICROENVIRONMENT 
700 1 |a Conejo-García, J.R. 
773 0 |d Academic Press, 2016  |g v. 428  |h pp. 3266-3281  |k n. 16  |p J. Mol. Biol.  |x 00222836  |w (AR-BaUEN)CENRE-1757  |t Journal of Molecular Biology 
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856 4 0 |u https://doi.org/10.1016/j.jmb.2016.03.021  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00222836_v428_n16_p3266_Rabinovich  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00222836_v428_n16_p3266_Rabinovich  |y Registro en la Biblioteca Digital 
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962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
999 |c 76739 

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