Topic
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.
Papers published on a yearly basis
Papers
More filters
TL;DR: To delineate the factors that underlie the specificity of a galectin for its counterreceptor(s) in the cellular context and the details of structure–activity relationships by comparatively analyzing natural and rationally engineered proteins is the main challenge for ongoing research.
Abstract: One route of realizing the information of glycans involves endogenous receptors (lectins). Occurrence at branch ends renders galactosides particularly accessible. Thus, they are suited for such a recognition process. Fittingly, these epitopes serve as physiological ligands. The ga(lactoside-binding) lectins share the β-sandwich fold with a sequence signature around a central tryptophan residue besides this specificity. Three modes of presentation of the carbohydrate recognition domain are known for galectins, and genome monitoring from fungi to mammals discloses that galectins form a network. The extent of its complexity varies considerably between organisms, for chicken reaching seven proteins, more for mammals. The current status of network analysis reveals overlapping and distinct expression profiles. Matching intra- and extracellular galectin presence, they have a broad range of functions at each site depending on their specific counterreceptor(s), with the possibility even for functional antagonism between family members. Orchestration of expression of galectin, the cognate glycan, its scaffold (protein or sphingolipid) and spatial aspects of glycoconjugate presentation has been detected to lead to growth regulation of immune and tumor cells. To delineate the factors that underlie the specificity of a galectin for its counterreceptor(s) in the cellular context and the details of structure-activity relationships by comparatively analyzing natural and rationally engineered proteins is the main challenge for ongoing research.
108 citations
TL;DR: It is found that galectin-9 ligation downregulates multiple immune-activating genes, including eight involved in the NK cell-mediated cytotoxicity pathway, impairs lymphokine-activated killing, and decreases the proportion of gamma interferon (IFN-γ)-producing NK cells that had been stimulated with interleukin-12 (IL-12)/IL-15.
Abstract: Galectin-9 is a pleiotropic immune modulator affecting numerous cell types of innate and adaptive immunity. Patients with chronic infection with either hepatitis C virus (HCV) or HIV have elevated circulating levels. Limited data exist on the regulation of natural killer (NK) cell function through interaction with galectin-9. We found that galectin-9 ligation downregulates multiple immune-activating genes, including eight involved in the NK cell-mediated cytotoxicity pathway, impairs lymphokine-activated killing, and decreases the proportion of gamma interferon (IFN-γ)-producing NK cells that had been stimulated with interleukin-12 (IL-12)/IL-15. We demonstrate that the transcriptional and functional changes induced by galectin-9 are independent of Tim-3. Consistent with these results for humans, we find that the genetic absence of galectin-9 in mice is associated with greater IFN-γ production by NK cells and enhanced degranulation. We also show that in the setting of a short-term (4-day) murine cytomegalovirus infection, terminally differentiated NKs accumulate in the livers of galectin-9 knockout mice, and that hepatic NKs spontaneously produce significantly more IFN-γ in this setting. Taken together, our results indicate that galectin-9 engagement impairs the function of NK cells, including cytotoxicity and cytokine production.
108 citations
TL;DR: Investigation of the expression of these galectins in 38 human bladder transitional‐cell carcinomas of different histological grade and clinical stage and in 5 normal urothelium samples revealed a higher content of galectin‐1 in tumors.
Abstract: Galectin-1 and galectin-3 are galactoside-binding proteins involved in different steps of tumor progression and potential targets for therapy. We have investigated the expression of these galectins in 38 human bladder transitional-cell carcinomas of different histological grade and clinical stage and in 5 normal urothelium samples. Galectin-1 mRNA levels were highly increased in most high-grade tumors compared with normal bladder or low-grade tumors. Western blot and immuno-histochemical analysis of normal and neoplastic tissues revealed a higher content of galectin-1 in tumors. Galectin-3 mRNA levels were also increased in most tumors compared with normal urothelium, but levels were comparable among tumors of different histological grade.
107 citations
09 Oct 2008
TL;DR: An introduction to Animal Lectins and modern approach to Structural Aspects of Lectin-Ligand Interactions is presented, as well as a discussion of Coral Lectins in Morphological Change of Zooxanthellae.
Abstract: INTRODUCTION Introduction to Animal Lectins, G.R. Vasta and H. Ahmed MODERN APPROACHES FOR ASSESSING LECTIN FUNCTION Structural Aspects of Lectin-Ligand Interactions, M.A. Bianchet, H. Ahmed, G.R. Vasta, and L.M. Amzel Thermodynamic Approaches to the Study of Affinity of Clustered Carbohydrate Epitopes in Galectin-Glycoconjugate Interactions, T.K. Dam and C.F. Brewer Deciphering Lectin Ligands through Glycan Arrays, D.F. Smith and R.D. Cummings Chromatography and Related Approaches for Qualitative and Quantitative Analyses of Lectin Specificity, J. Hirabayashi Analysis of Whole-Genome and Other Data Resources to Characterize the Molecular, Structural, and Evolutionary Diversity of C-Lectins and Discover New Genes, A.N. Zelensky and J.E. Gready Animal Models for Assessing the Biological Roles of Lectins, H. Ahmed, G.A. Rabinovich, S.S. Jackson, M. Salatino, K. Saito, G. Bianco, S. Tasumi, S.-J. Du, and G.R. Vasta GLYCOPROTEIN FOLDING, SORTING AND SECRETION, TARGETING, DEGRADATION, AND CLEARANCE Calreticulin and Calnexin as Chaperones in Glycoprotein Folding, J.J. Caramelo and A.J. Parodi Role of L-Type Lectins in Glycoprotein Sorting and Trafficking, B. Nyfeler, M.W. Wendeler, and H.-P. Hauri P-Type Lectins and Lysosomal Enzyme Targeting, N.M. Dahms, L.J. Olson, and J.-J.P. Kim M-Type Lectins as Novel Components of Secretory Pathways, N. Hosokawa and K. Nagata Functional Aspects of the Hyaluronan and Chondroitin Sulfate Receptors, E.N. Harris and P.H. Weigel CELL ADHESION AND CELL SURFACE LATTICE FORMATION Galectin-3 and Cancer, Y. Wang, V. Balan, and A. Raz Myelin-Associated Glycoprotein (Siglec-4): A Nervous System Lectin That Regulates Axon-Myelin Stability and Axon Regeneration, R.L. Schnaar and N.R. Mehta Hyaluronan-Binding Proteoglycans, E.N. Harris and P.H. Weigel Roles of Coral Lectins in Morphological Change of Zooxanthellae, H. Kamiya, M. Jimbo, K. Koike, and R. Sakai CELL-CELL INTERACTIONS, SIGNALING, AND TRANSPORT Siglecs: Roles in Cell-Cell Interactions and Signaling, C.O. and P.R. Crocker Signaling through the Fungal b-Glucan Receptor Dectin-1, A.M. Kerrigan, K.M. Dennehy, and G.D. Brown CD22: A Regulator of B Cell Survival and Signal Transduction, S.H. Smith and T.F. Tedder Galectins and Integrins in Pre-B Cell Development, M. Espeli, L. Gauthier, S. Mancini, F. Mourcin, B. Rossi, and C. Schiff Golgi N-Glycan Processing and Galectin Functions, K.S. Lau, I.R. Nabi, M. Demetriou, and J.W. Dennis RECOGNITION AND EFFECTOR FUNCTIONS IN INNATE IMMUNITY Mannan-Binding Lectin Polymorphisms and Infectious Diseases, M. Moller-Kristensen, S. Thiel, and J.C. Jensenius Immunoregulatory Roles of Lung Surfactant Proteins A and D, N. Palaniyar, G.L. Sorensen, and U. Holmskov C-Type Lectin Receptors on Dendritic Cells, Y. van Kooyk Structural and Functional Roles of C-type Lectin Receptors on Natural Killer Cells, N. Dimasi Activation of Lepidopteran Insect Innate Immune Responses by C-type Immulectins, X.-Q. Yu and M.R. Kanost Galectins as Novel Regulators of Immune Cell Homeostasis and Inflammation, G. A. Rabinovich, M.A. Toscano, J.M. Ilarregui, and L.G. Baum Interactions of Galectins with Leukocytes, S.R. Stowell and R.D. Cummings Regulation of Immune Responses by Galectin-3, D. K. Hsu and F.-T. Liu X-Lectins: A New Family with Homology to the Xenopus laevis Oocyte Lectin XL-35, J.K. Lee and M. Pierce F-Type Lectins: A New Family of Recognition Factors, G.R. Vasta, E.W. Odom, M.A. Bianchet, L.M. Amzel, K. Saito, and H. Ahmed Biology of FREPs: Diversified Lectins with Fibrinogen-Related Domains from Freshwater Snail Biomphalaria glabrata, B.A. Stout, C.M. Adema, S.-M. Zhang, and E.S. Loker Lectins in Sand Fly-Leishmania Interactions, S. Kamhawi and J.G. Valenzuela Ficolins: The Structural Basis for Recognition Plasticity, M. Matsushita, Y. Endo, and T. Fujita Hemolytic Lectin in Marine Invertebrates, T. Hatakeyama Structure-Function Relationship in Mammalian Chitinase-Like Lectins, S. Morroll, S. Turner, and F.H. Falcone Index
107 citations
TL;DR: These distinct binding features of G4-N establish the important concept of affinity enhancement by high density polyvalencies of glycotopes and by introduction of an ABH key sugar to Galbeta1-terminated core glycotope.
107 citations