Galectin

About: Galectin is a research topic. Over the lifetime, 2076 publications have been published within this topic receiving 103409 citations. The topic is also known as: IPR001079 & Galectin.

The association between increasing levels of O-GlcNAc and galectins in the liver tissue of hibernating thirteen-lined ground squirrels (Ictidomys tridecemlineatus).

Abstract: Post-translational glycosylation of proteins with O-linked β-N-acetylglucosamine (O-GlcNAcylation) and changes of galectin expression profiles are essential in many cellular stress responses. We examine this regulation in the liver tissue of hibernating thirteen-lined ground squirrels (Ictidomys tridecemlineatus) representing a biological model of hypometabolism and physiological stress resistance. The tissue levels of O-GlcNAcylated proteins as well as galectin-1 and galectin-3 proteins detected by immunodot blot assay were significantly lower by 4.6–5.4-, 2.2–2.3- and 2.5–2.9-fold, respectively, in the non-hibernating summer squirrels compared with those in winter, whether hibernating or aroused. However, there were no differences in the expression of genes encoding enzymes involved in O-GlcNAc cycle (O-GlcNAc transferase and O-GlcNAcase) and such galectins as LGALS1, LGALS2, LGALS3, LGALS4 and LGALS9. Only the expression of LGALS8 gene in the liver tissue was significantly decreased by 37.6 ± 0.1% in hibernating ground squirrels relative to summer animals. Considering that the expression of a proven genetic biomarker ELOVL6 encoding ELOVL fatty acid elongase 6 was readily upregulated in non-hibernating animals by 11.3–32.9-fold, marginal differential changes in the expression of galectin genes cannot be classified as biomarkers of hibernation. Thus, this study provides evidence that hibernation in Ictidomys tridecemlineatus is associated with increasing O-GlcNAcylation of liver proteins and suggests that the contribution of galectins deserves further studies at the protein level.

Selenogalactoside compounds for the prevention and treatment of diseases associated with galectin and the use thereof

Abstract: Aspects of the invention relate to novel synthetic compounds having a binding affinity with galectin proteins.

Structure-Based Development of Galectin- Specific Inhibitors

Abstract: Galectins are a family of β-galactoside-specific lectins with sequence and structure conservation within their carbohydrate recognition domains. Galectins are found in a variety of species such as fungi, fish, birds and mammals. Furthermore, galectins are located in the nucleus, the cytoplasm and the extracellular matrix with their expression and localization regulated by the cell and its environment. Galectins are implicated in a number of disease states such as inflammation and cancer. Galectin-3 contributes to the progression of every step of cancer, from malignant transformation to angiogenesis, metastasis, immune evasion and to drug resistance. In contrast, galectin-4 plays contradicting roles in different cancers, enhancing metastasis of liver and lung cancers but inhibiting metastasis in colon and pancreatic cancers. The development of high-affinity selective inhibitors of galectins to probe their functions and to treat diseases is a major goal within the galectin field. Inhibition of galectins have mostly focused on galectin-3 and galectin-1, as these are the most thorougly studied galectins with significant correlation to disease progression. Divergent strategies have been employed in the inhibition of these galectins including saccharide modification, glycodendrimers with multiple peripheral saccharides, large natural complex polysaccharides such as modified citrus pectin as well as the use of peptides and peptidomimetics. Non-saccharide small molecule inhibitors toward galectins are not yet available. Recent reports regarding the anti-cancer capacity of galectins, such as for galectin-4, have highlighted the need for selective inhibitors. A major challenge in developing selective galectin inhibitors has been the high conservation of the carbohydrate binding site among galectins.

Expression and significance of T-cell immunoglobulin mucin molecule 3 and its ligand galectin-9 in patients with adenomyosis.

Abstract: The T cell immunoglobulin mucin molecule 3 (TIM-3), as a negative regulatory immune checkpoint, plays an important role in cellular immunity by binding to its ligand galectin-9 (Gal-9). Under abnormal conditions, this pathway can regulate the depletion of T cells and suppress the immune response. Abnormal expression of TIM-3 and Gal-9 has been confirmed in a variety of cancers, recurrent miscarriages, chronic infectious diseases and autoimmune diseases. More and more studies have shown that immune factors play an important role in the pathogenesis of adenomyosis. However, few studies have attempted to explore their expression in adenomyosis. The ectopic and eutopic endometrium were collected from 15 women with adenomyosis and 13 women without adenomyosis. TIM-3/Gal-9 expression in endometrial tissue was detected using immunohistochemistry, western blot analysis and real-time PCR. We observed TIM-3/Gal-9 expression in both eutopic and ectopic endometria, with elevated expression in adenomyosis. These data suggest that TIM-3/Gal-9 may be involved in the development and progression of adenomyosis.