Galectin – Reviews:
- Bertuzzi, S., et al. (2020). Targeting Galectins With Glycomimetics. Frontiers in chemistry, 8, 593.
- 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:
- Slack, R.J. et al. (2020). The therapeutic potential of galectin-3 inhibition in fibrotic disease. The international journal of biochemistry & cell biology.
- 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.
- 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:
- Siew, J. J., et al. (2019). Galectin-3 is required for the microglia-mediated brain inflammation in a model of Huntington’s disease. Nature communications, 10(1), 3473.
- Navarro-Alvarez, N., et al. (2018). The effects of galectin-3 depletion apheresis on induced skin inflammation in a porcine model. Journal of clinical apheresis, 33(4), 486-493.
- 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:
- Bertuzzi, S., et al. (2020). Targeting Galectins With Glycomimetics. Frontiers in chemistry, 8, 593.
- 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
- Manero-Rupérez, N., et al. (2020) The Galectin Family as Molecular Targets: Hopes for Defeating Pancreatic Cancer. Cells, 9(3), 689.
- 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.
- 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.
- Martinez-Bosch, N., Vinaixa, J., & Navarro, P. (2018). Immune Evasion in Pancreatic Cancer: From Mechanisms to Therapy. Cancers, 10(1), 6.
- Nangia-Makker, P., Hogan, V., & Raz, A. (2018). Galectin-3 and cancer stemness. Glycobiology, 28(4), 172–181.
- Wdowiak, K., et al. (2018). Galectin Targeted Therapy in Oncology: Current Knowledge and Perspectives. International journal of molecular science, 19(1), 210.
- 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.
- 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.
- Seguin, L., et al. (2017). Galectin-3, a Druggable Vulnerability for KRAS-Addicted Cancers. Cancer discovery, 7(12):1464-1479.
- 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:
- Erasmus, M., et al. (2020). Linking LOXL2 to Cardiac Interstitial Fibrosis. International journal of molecular sciences, 21(16), 5913.
- Klepfish, M., et al. (2020). LOXL2 Inhibition Paves the Way for Macrophage-Mediated Collagen Degradation in Liver Fibrosis. Frontiers in immunology, 11(480).
- Matsuoka, K., et al. (2020). Wnt signaling and Loxl2 promote aggressive osteosarcoma. Cell research.
- Mahjour, F., et al. Mechanism for oral tumor cell lysyl oxidaselike-2 in cancer development: synergy with PDGF-AB. (2019). Oncogenesis, 8(34), 1-17.
- Peng, X., et al. (2019). Inhibition of LOXL2 Enhances the Radiosensitivity of Castration-Resistant Prostate Cancer Cells Associated with the Reversal of the EMT Process. BioMed research international, 2019(4012590).
- Puente, A., et al. (2019). LOXL2-A New Target in Antifibrogenic Therapy?. International journal of molecular sciences, 20(7), 1634.
- Vallet, S. D., & Ricard-Blum, S. (2019). Lysyl oxidases: from enzyme activity to extracellular matrix cross-links. Essays in biochemistry, 63(3), 349–364.
- Stagenberg, S., et al. (2018). Lysyl oxidase-like 2 inhibition ameliorates glomerulosclerosis and albuminuria in diabetic nephropathy. Scientific reports, 8(9423).
- Chang, J., et al. (2017). Pre-clinical evaluation of small molecule LOXL2 inhibitors in breast cancer. Oncotarget, 8(16), 26066-26078.
- 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.
- Wu, L. & Zhu, Y. (2015). The function and mechanisms of action of LOXL2 in cancer (Review). International journal of molecular medicine, 36(5):1200-4.
- 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.