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Overview of Animal Galectins: Proto-Type Subfamily

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Animal Lectins: Form, Function and Clinical Applications

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Abstract

Lectins recognize and bind carbohydrates covalently linked to proteins and lipids on the cell surface and within the extracellular matrix, and they mediate many cellular functions ranging from cell adhesion to pathogen recognition. Phylogenetically conserved family of Galectins was defined in 1994 as a shared consensus of amino-acid-sequences of about 130 amino acids and the CRD responsible for ß-galactoside binding (Barondes et al. 1994). The galectin (Gal) CRDs bind small β-galactosides/poly-N-acetyllactosamine-enriched glycoconjugates. But the overall binding affinity for more complex glycoconjugates varies substantially. To date, 15 members of the mammalian galectin family have been identified. Some, such as galectin-1, are isolated as dimers and have a single CRD in each monomer, whereas others, such as galectin-4, are isolated as monomers and have two CRDs in a single polypeptide chain. While CRDs of all galectins share an affinity for minimum saccharide ligand N-acetyllactosamine—a common disaccharide found on many cellular glycoproteins—individual galectins can also recognize different modifications to this minimum saccharide ligand and so demonstrate the fine specificity of certain galectins for tissue- or developmentally-specific ligands (Ahmad et al. 2004a). Location studies of galectins have established that these proteins can segregate into multiple cell compartments in function of the status of the cells in question (Danguy et al. 2002; Liu and Rabinovich 2005). Although galectins as a whole do not have the signal sequence required for protein secretion through usual secretory pathway, some galectins are secreted and are found in the extracellular space. While the intracellular activity of galectin-1 is mainly independent on its lectin activity, its extracellular activity is mainly dependent on it. The functions and distribution of Gal-1 and Gal-3 are well characterized.

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Authors and Affiliations

  1. Department of Biomedical Engineering, Rayat and Bahra Institute of Engineering and Biotechnology, Kharar (Mohali), Punjab, India

    Anita Gupta (Assistant Professor)

  2. Department of Biophysics, Punjab University, Chandigarh, India

    G. S. Gupta (Former Professor and Chairman)

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  1. Anita Gupta
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Gupta, A., Gupta, G.S. (2012). Overview of Animal Galectins: Proto-Type Subfamily. In: Animal Lectins: Form, Function and Clinical Applications. Springer, Vienna. https://doi.org/10.1007/978-3-7091-1065-2_9

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