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      Galectin-3: an open-ended story.

      1 , ,
      Biochimica et biophysica acta
      Elsevier BV

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          Abstract

          Galectins, an ancient lectin family, are characterized by specific binding of beta-galactosides through evolutionary conserved sequence elements of carbohydrate-recognition domain (CRD). A structurally unique member of the family is galectin-3; in addition to the CRD it contains a proline- and glycine-rich N-terminal domain (ND) through which is able to form oligomers. Galectin-3 is widely spread among different types of cells and tissues, found intracellularly in nucleus and cytoplasm or secreted via non-classical pathway outside of cell, thus being found on the cell surface or in the extracellular space. Through specific interactions with a variety of intra- and extracellular proteins galectin-3 affects numerous biological processes and seems to be involved in different physiological and pathophysiological conditions, such as development, immune reactions, and neoplastic transformation and metastasis. The review attempts to summarize the existing information on structural, biochemical and intriguing functional properties of galectin-3.

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          Author and article information

          Journal
          Biochim Biophys Acta
          Biochimica et biophysica acta
          Elsevier BV
          0006-3002
          0006-3002
          Apr 2006
          : 1760
          : 4
          Affiliations
          [1 ] Department of Biochemistry and Molecular Biology, Faculty of Pharmacy and Biochemistry, University of Zagreb, Croatia. jdumic@pharma.hr
          Article
          S0304-4165(05)00408-3
          10.1016/j.bbagen.2005.12.020
          16478649
          ad7d73b2-fe84-42f8-a669-48557e44e2a3
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