Lectins and Glycobiology

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Tetramers facilitate the engulfment of apoptotic cells. On the other hand, inhibitory siglecs reduce phagocytosis when they form complexes with sialic acid-containing ligands. Additional lectin receptors such as DC-SIGN and mannose-binding receptor are upregulated on macrophages and dendritic cells and have been proposed to participate in the removal of human apoptotic thymocytes. It is worth noting that APCs engulfing apoptotic cells can secrete soluble mediators and cytokines capable of activating or blunting adaptive immune responses. The study of the cellular glycome has provided new insights into a variety of physiologic processes.

Interactions between endogenous lectins and glycans can set the threshold for cellular activation, differentiation and survival. Here, we discuss the relevance of lectin—glycan recognition systems in the initiation, execution and resolution of cell death and provide selected examples that illustrate their important roles in these processes. While differential glycosylation of death receptors controls the transmission of lethal signals, soluble or cell surface-associated glycan-binding proteins can initiate apoptotic programs indirectly by interacting with death receptors or directly by crosslinking a myriad of cell surface glycoproteins.

In addition, intracellular galectins and glycan-modifying enzymes have important roles in the execution of cell death programs including apoptosis and autophagy. These intracellular galectins and glycan-modifying enzymes not only orchestrate degradation of self or foreign cargo in response to cellular damage and infection but also control immune responses and inflammation. Moreover, incorrect glycan presentation alters autophagy, which contributes to disease severity. The current wealth of information allows the visualization of strategies through which manipulation of lectin—glycan recognition systems may contribute to the control of cell death programs with critical implications in the resolution of inflammation, chronic infection, autoimmunity, neurodegeneration and cancer.

Programmed cell death-I. Cytology of degeneration in the intersegmental muscles of the pernyi silkmoth. J Insect Physiol ; 11 : — Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer ; 26 : — Sharon N, Lis H. History of lectins: from hemagglutinins to biological recognition molecules.

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Glycobiology ; 14 : 53R—62R. Hormone-induced cell death.

Am J Pathol ; : — Macrophage recognition of cells undergoing programmed cell death apoptosis. Immunology ; 56 : — The toxic plant proteins ricin and abrin induce apoptotic changes in mammalian lymphoid tissues and intestine. J Pathol ; : — Wesselborg S, Kabelitz D. Activation-driven death of human T cell clones: time course kinetics of the induction of cell shrinkage, DNA fragmentation, and cell death. Cell Immunol ; : — Induction of apoptosis in human lymphocytes treated with Viscum album L.

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  • Cancer Lett ; 99 : 59— Plant lectins: targeting programmed cell death pathways as antitumor agents. Int J Biochem Cell Biol ; 43 : — Rabinovich GA. Galectins: an evolutionarily conserved family of animal lectins with multifunctional properties; a trip from the gene to clinical therapy. Cell Death Differ ; 6 : — Regulatory circuits mediated by lectin—glycan interactions in autoimmunity and cancer. Immunity ; 36 : — Galectins in acute and chronic inflammation.

    Ann N Y Acad Sci ; : 80— Clusters, bundles, arrays and lattices: novel mechanisms for lectin—saccharide-mediated cellular interactions. Curr Opin Struct Biol ; 12 : — Vasta GR. Galectins as pattern recognition receptors: structure, function, and evolution. Adv Exp Med Biol ; : 21— Mammalian glycosylation in immunity.

    Bullet Points

    Nat Rev Immunol ; 8 : — Ah, sweet mystery of death! Galectins and control of cell fate. Glycobiology ; 12 : R—R. The sweet and sour of cancer: glycans as novel therapeutic targets.

    a family of sialic-acid binding lectins.

    Nat Rev Cancer ; 5 : — Nat Med ; 13 : — Gastroenterology ; : — J Biol Chem ; : — PLoS One ; 6 : e Leukemia ; 24 : — Sialyltransferases in cancer. Glycoconj J ; 18 : — Cell surface sialylation plays a role in modulating sensitivity towards APOmediated apoptotic cell death. Cell Death Differ ; 2 : — Glycobiology ; 9 : — Sialylation of the Fas death receptor by ST6Gal-I provides protection against Fas-mediated apoptosis in colon carcinoma cells.

    Epithelial ovarian cancer cells secrete functional Fas ligand. Cancer Res ; 63 : — Conveying glycan information into T-cell homeostatic programs: a challenging role for galectin-1 in inflammatory and tumor microenvironments. Immunol Rev ; : — Galectin-1 sensitizes resting human T lymphocytes to Fas CD95 -mediated cell death via mitochondrial hyperpolarization, budding, and fission.

    Endogenous galectin-3 determines the routing of CD95 apoptotic signaling pathways. Cancer Res ; 64 : — Galectin-3 inhibits tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by activating Akt in human bladder carcinoma cells. Cancer Res ; 65 : — Reconstitution of galectin-3 alters glutathione content and potentiates TRAIL-induced cytotoxicity by dephosphorylation of Akt. Exp Cell Res ; : 21— Wells V, Mallucci L. Phosphoinositide 3-kinase targeting by the beta galactoside binding protein cytokine negates akt gene expression and leads aggressive breast cancer cells to apoptotic death.

    Breast Cancer Res ; 11 : R2. Cell-surface galectin-3 confers resistance to TRAIL by impeding trafficking of death receptors in metastatic colon adenocarcinoma cells. Cell Death Differ ; 19 : — Phosphorylation of the beta-galactoside-binding protein galectin-3 modulates binding to its ligands. Phosphorylated galectin-3 mediates tumor necrosis factor-related apoptosis-inducing ligand signaling by regulating phosphatase and tensin homologue deleted on chromosome 10 in human breast carcinoma cells. Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin J Immunol ; : — Apoptosis ; 13 : — Induction of allogenic T-cell hyporesponsiveness by galectinmediated apoptotic and non-apoptotic mechanisms.

    Cell Death Differ ; 9 : — Galectin-1 induces nuclear translocation of endonuclease G in caspase- and cytochrome c -independent T cell death. Cell Death Differ ; 11 : — Role of p56lck and ZAPmediated tyrosine phosphorylation in galectininduced cell death. Cell Death Differ ; 12 : — Molecular mechanisms implicated in galectininduced apoptosis: activation of the AP-1 transcription factor and downregulation of Bcl Cell Death Differ ; 7 : — Cell Death Dis ; 1 : e CD45 modulates galectininduced T cell death: regulation by expression of core 2 O -glycans.

    N - and O -glycans modulate galectin-1 binding, CD45 signaling, and T cell death. Nat Immunol ; 8 : — Galectin-1 deactivates classically activated microglia and protects from inflammation-induced neurodegeneration.


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    Immunity ; 37 : — Mol Cell Biol ; 27 : — Nat Immunol ; 7 : — Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death. Galectin-3 translocates to the perinuclear membranes and inhibits cytochrome c release from the mitochondria. A role for synexin in galectin-3 translocation. Sialylation of beta1 integrins blocks cell adhesion to galectin-3 and protects cells against galectininduced apoptosis.

    A bite so sweet: the glycobiology interface of tick-host-pathogen interactions

    Sialylation of 3-methylcholanthrene-induced fibrosarcoma determines antitumor immune responses during immunoediting. The involvement of CD44 and its novel ligand galectin-8 in apoptotic regulation of autoimmune inflammation. Nat Rev Immunol ; 9 : — The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity. Nat Immunol ; 6 : — Galectin-9 induces apoptosis through the calcium-calpain-caspase-1 pathway.

    Characterization of galectininduced death of Jurkat T cells. J Biochem ; : — Bat3 promotes T cell responses and autoimmunity by repressing Timmediated cell death and exhaustion. Nat Med ; 18 : — T cell immunoglobulin mucin-3 crystal structure reveals a galectinindependent ligand-binding surface. Immunity ; 26 : — J Clin Invest ; : — Human galectin novel inducer of T cell apoptosis with distinct profile of caspase activation. Galectin-4 controls intestinal inflammation by selective regulation of peripheral and mucosal T cell apoptosis and cell cycle.

    In the group of carbohydrate-binding proteins, lec- tins are distinguished from antibodies or ligand-affecting enzymes, according to the most recent definition. The thorough analysis of their structure and function is considered as a focus to collect a critical mass of information for delineating details of a further array of biochemical processes with pivotal physiological im- pact.

    Laboratory of Glycoimmunology

    Following an already century-long history of scientific description, reflected by subjectively chosen highlights see the Brief History of Lectin Research at page VI , the excitement in glycobiological research that prevails today can easily be ex- plained by our growing awareness of the multifarious significance of a sugar-code system of biological information. This present notion unmistakably has an im- pact on lines of research in diverse disciplines like cell and molecular biology, histochemistry, or clinical sciences.

    It also prompts inherent practical questions such as how to obtain lectins, or how to employ them as instruments in various assay systems with the best possible results. Included are methods for the preparation of synthetic carbohydrate ligands, the determination of physico-chemical properties of lectin-oligosaccharide interactions, the isolation and chemical modification of lectins, and assays to detect and quantitate lectins.

    Several chapters focus on the study of signal transduction and cellular responses induced by lectins as well as on cellular adhesion and cell recognition involving lectin-glycoprotein interaction.

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