Galectin – Reviews:
- Slack, R.J. et al. (2020). Translational pharmacology of TD139, an inhaled small molecule galectin-3 (Gal-3) inhibitor for the treatment of idiopathic pulmonary fibrosis (IPF). The FASEB journal, 34: 1-1.
- Johannes, L., Jacob, R., & Leffler, H. (2018). Galectins at a glance. Journal of cell science, 131(9).
- Sciacchitano, S. et al. (2018). Galectin-3: One Molecule for an Alphabet of Diseases, from A to Z. International journal of molecular science, 19(2), 379
- Nabi, I.R., Shankar, J., & Dennis, J.W. (2015). The galectin lattice at a glance. Journal of cell science,128(13), 2213-2219.
- Li, L.C., Li, J., & Gao, J. Functions of galectin-3 and its role in fibrotic diseases. (2014). Journal of pharmacology and experimental therapeutics, 351(2), 336-343.
- Mackinnon, A., et al. (2014). Design, synthesis, and applications of galectin modulators in human health: In C. Rademacher and P. H. Seeberger, (Eds.).Topics in Medicinal Chemistry: Carbohydrates as Drugs. Springer-Verlag GmbH & Co. KG, Berlin/Heidelberg, 95-121.
- Leffler, H. & Nilsson, U. (2012). Low-Molecular Weight Inhibitors of Galectins. In A. A. Lyosov and P. G. Traber (Eds.). Galectins and Disease – Implications for Targeted Therapies. ACS Symp. Ser. No. 1115, 47-59.
- Leffler, H., Carlsson, S., Hedlund, M., Qian, Y., & Poirier, F. (2004). Introduction to galectins. Glycoconjugate journal, 19(7-9), 433-40.
Galectin-3 & Fibrosis:
- Stegmayr, J., et al. (2019). Extracellular and Intracellular Small-Molecule Galectin-3 Inhibitors. Scientific reports, 9(1), 2186.
- Frangogiannis N. G. (2018). Galectin-3 in the fibrotic response: Cellular targets and molecular mechanisms. International journal of cardiology, 258, 226–227.
- Chen, W. S., Cao, Z., Leffler, H., Nilsson, U. J., & Panjwani, N. (2017). Galectin-3 Inhibition by a Small-Molecule Inhibitor Reduces Both Pathological Corneal Neovascularization and Fibrosis. Investigative ophthalmology & visual science, 58(1), 9–20.
- Meijers, W. C., López-Andrés, N., & de Boer, R. A. (2016). Galectin-3, Cardiac Function, and Fibrosis. The American journal of pathology, 186(8), 2232–2234.
- MacKinnon, A. C., et al. (2012). Regulation of transforming growth factor-β1-driven lung fibrosis by galectin-3. American journal of respiratory and critical care medicine, 185(5), 537–546.
- Mahendran, S., Sethi, T. (2012). Treatments in idiopathic pulmonary fibrosis: time for a more targeted approach? QJM: An international journal of medicine, 105(10), 929–934.
- Henderson, N. C., & Sethi, T. (2009). The regulation of inflammation by galectin-3. Immunological reviews, 230(1), 160–171.
- MacKinnon, A. C., et al. (2008). Regulation of alternative macrophage activation by galectin-3. The journal of immunology, 180(4), 2650-2658.
- Henderson, N. C., at el. (2008). Galectin-3 expression and secretion links macrophages to the promotion of renal fibrosis. The American journal of pathology, 172(2), 288–298.
- Henderson, N. C., at al. (2006). Galectin-3 regulates myofibroblast activation and hepatic fibrosis. Proceedings of the national academy of sciences of the United States of America, 103(13), 5060–5065.
Galectin-3 & Other Diseases:
- MacKinnon, A. C., Liu, X., Hadoke, P. W., Miller, M. R., Newby, D. E., & Sethi, T (2013). Inhibition of galectin-3 reduces atherosclerosis in apolipoprotein E-deficient mice. Glycobiology, 23(6), 654-663.
- Dang, Z., MacKinnon, A., Marson, L. P., & Sethi, T. (2012). Tubular atrophy and interstitial fibrosis after renal transplantation is dependent on galectin-3. Transplantation, 93(5), 477–484.
Galectin Modulators:
- Zetterberg, F. R., et al. (2018). Monosaccharide Derivatives with Low-Nanomolar Lectin Affinity and High Selectivity Based on Combined Fluorine-Amide, Phenyl-Arginine, Sulfur-π, and Halogen Bond Interactions. ChemMedChem, 13(2), 133–137.
- Peterson, K., et al. (2018). Systematic Tuning of Fluoro-Galectin-3 Interactions Provides Thiodigalactoside Derivatives with Single-Digit nM Affinity and High Selectivity. Journal of medicinal chemistry, 61(3), 1164-1175.
- Delaine, T., et al. (2016). Galectin-3-Binding Glycomimetics That Strongly Reduce Bleomycin-Induced Lung Fibrosis and Modulate Intracellular Glycan Recognition. ChemBioChem, 17(18), 1759-1770.
- Diehl, C., et al. (2010). Protein flexibility and conformational entropy in ligand design targeting the carbohydrate recognition domain of galectin-3. Journal of the American chemical society, 132(41), 14577-14589.
- Salameh, B. A., Cumpstey, I., Sundin, A., Leffler, H., & Nilsson, U. J. (2010). 1H-1,2,3-triazol-1-yl thiodigalactoside derivatives as high affinity galectin-3 inhibitors. Bioorganic & medicinal chemistry, 18(14), 5367-5378.
- Cumpstey, I., Sundin, A., Leffler, H., & Nilsson, U. J. (2005). C2-symmetrical thiodigalactoside bis-benzamido derivatives as high-affinity inhibitors of galectin-3: efficient lectin inhibition through double arginine-arene interactions. Angewandte Chemie (International ed. in English), 44(32), 5110–5112.
- Sörme, P., Arnoux, P., Kahl-Knutsson, B., Leffler, H., Rini, J. M., & Nilsson, U. J. (2005). Structural and thermodynamic studies on cation-Pi interactions in lectin-ligand complexes: high-affinity galectin-3 inhibitors through fine-tuning of an arginine-arene interaction. Journal of the American chemical society, 127(6), 1737–1743.
Galectins’ Role in Cancer
- Capalbo, C., Scafetta, G., Filetti, M., Marchetti, P., & Bartolazzi, A. (2019). Predictive Biomarkers for Checkpoint Inhibitor-Based Immunotherapy: The Galectin-3 Signature in NSCLCs. International journal of molecular sciences, 20(7), 1607.
- Ballester, B., Milara, J., & Cortijo, J. (2019). Idiopathic Pulmonary Fibrosis and Lung Cancer: Mechanisms and Molecular Targets. International journal of molecular sciences, 20(3), 593.
- Vuong, L., et al. (2019). An Orally Active Galectin-3 Antagonist Inhibits Lung Adenocarcinoma Growth and Augments Response to PD-L1 Blockade. Cancer research, 79(7), 1480–1492.
- Dubé-Delarosbil, C., & St-Pierre, Y. (2018). The emerging role of galectins in high-fatality cancers. Cellular and molecular life sciences : CMLS, 75(7), 1215–1226.
- Wdowiak, K., et al. (2018). Galectin Targeted Therapy in Oncology: Current Knowledge and Perspectives. International journal of molecular science, 19(1), 210.
- Nangia-Makker, P., Hogan, V., & Raz, A. (2018). Galectin-3 and cancer stemness. Glycobiology, 28(4), 172–181.
- Martinez-Bosch, N., Vinaixa, J., & Navarro, P. (2018). Immune Evasion in Pancreatic Cancer: From Mechanisms to Therapy. Cancers, 10(1), 6.
- Gordon-Alonso, M., Bruger, A. M., & van der Bruggen, P. (2018). Extracellular galectins as controllers of cytokines in hematological cancer. Blood, 132(5), 484–491.
- Gordon-Alonso, M., Hirsch, T., Wildmann, C., & van der Bruggen, P. (2017). Galectin-3 captures interferon-gamma in the tumor matrix reducing chemokine gradient production and T-cell tumor infiltration. Nature communications, 8(1):793.
- Chang, W. A., Tsai, M. J., Kuo, P. L., & Hung, J. Y. (2017). Role of galectins in lung cancer. Oncology letters, 14(5), 5077–5084.
- Ruvolo P. P. (2016). Galectin 3 as a guardian of the tumor microenvironment. Biochimica et biophysica acta, 1863(3), 427–437.
- Song, L., Tang, J. W., Owusu, L., Sun, M. Z., Wu, J., & Zhang, J. (2014). Galectin-3 in cancer. Clinica chimica acta; international journal of clinical chemistry, 431, 185–191.
- Ingrassia, L., et al. (2006). Anti-galectin compounds as potential anti-cancer drugs. Current medicinal chemistry, 13(29), 3513–3527.
LOXL2 – Reviews:
- Vallet, S. D., & Ricard-Blum, S. (2019). Lysyl oxidases: from enzyme activity to extracellular matrix cross-links. Essays in biochemistry, 63(3), 349–364.
- Puente, A., et al. (2019). LOXL2-A New Target in Antifibrogenic Therapy?. International journal of molecular sciences, 20(7), 1634.
- Ikenaga, N., et al. (2017). Selective targeting of lysyl oxidase-like 2 (LOXL2) suppresses hepatic fibrosis progression and accelerates its reversal. Gut, 66(9), 1697–1708. , L., et al. (2019). An Orally Active Galectin-3 Antagonist Inhibits Lung Adenocarcinoma Growth and Augments Response to PD-L1 Blockade. Cancer research, 79(7), 1480–1492.
- Tadmor, T., et al. (2013). The expression of lysyl-oxidase gene family members in myeloproliferative neoplasms. American journal of hematology, 88(5), 355–358.
- Papadantonakis, N., Matsuura, S., & Ravid, K. (2012). Megakaryocyte pathology and bone marrow fibrosis: the lysyl oxidase connection. Blood, 120(9), 1774–1781.
Galecto, Inc. develops small molecules for the treatment of severe diseases, including fibrosis and cancer. The company, founded in 2011, builds on more than 10 years of research centering on the role of galectin-3 and LOXL-2, and the use of modulators of these proteins to treat fibrosis-related diseases and cancer. Combined with a strong patent estate, these assets give Galecto a unique therapeutic platform.
Tel: (+45) 70 70 52 10 – Email: info@galecto.com