Galectin-3: An open-ended story

• Published in: Biochimica et biophysica acta Vol. 1760; no. 4; pp. 616 - 635
• Main Authors: Dumic, Jerka, Dabelic, Sanja, Flögel, Mirna
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2006
• Subjects: Animals; Cancer; Carbohydrates - chemistry; Expression; Functional properties; Galectin 3 - chemistry; Galectin 3 - genetics; Galectin 3 - metabolism; Galectin 3 - physiology; Galectin-3; Gene Expression Regulation; Humans; Immune reaction; LGALS3; Structure; Tissue Distribution; LGALS3; Functional properties; Expression; Immune reaction; Galectin-3; Tissue distribution; Structure; Cancer
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2005.12.020

Galectins, an ancient lectin family, are characterized by specific binding of β-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.