The INDIVIDUALIST

A Wiki about biochemical individuality

Lectinology

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Description

Elevated levels of Galectin 3, hGal-3 are found in a wide range of neoplasms, and expression was shown to be associated in some tumor cell systems with metastases.

Galectin-3 has been shown to be involved in cell adhesion and activation of immune cells and plays a significant role in cell to extracellular matrix interactions. High levels of galectin-3 in metastatic cancer cells suggest an impact on metastasis formation.

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Galectin 3

Galectin 3 and the blood group precursor and tumor associated carbohydrate T antigen play a leading role in docking breast and prostate cancer cells onto endothelium. Importantly, T antigen-bearing glycoproteins are also capable of mobilizing galectin-3 to the surface of endothelial cells, thus priming them for harboring metastatic cancer cells.

Galectin 3 mediates genistein-induced G(2)/M arrest and inhibits apoptosis. It has a binding capacity for various glycoconjugates including IgE.

Abstracts

The role of galectin-3 in endocytosis of advanced glycation end products and modified low density lipoproteins

Biochem Biophys Res Commun. 2001 Feb 2;280(4):1183-8.

Zhu W, Sano H, Nagai R, Fukuhara K, Miyazaki A, Horiuchi S.

  • Galectin-3, a member of beta-galactoside-binding lectin family, is suggested to be an AGE-receptor. To examine this possibility, we prepared CHO cells overexpressing human galectin-3 (galectin-3-CHO cells). Galectin-3-CHO cells showed a specific and saturable binding to (125)I-AGE-BSA with Kd of 3.1 microg/ml. (125)I-AGE-BSA was endocytosed by galectin-3-CHO cells and underwent lysosomal degradation. The endocytosis of (125)I-AGE-BSA was inhibited not only by unlabeled AGE-BSA but also by acetylated LDL and oxidized LDL, ligands for the scavenger receptor family. Furthermore, (125)I-oxidized LDL and (125)I-acetylated LDL were actively endocytosed by galectin-3-CHO cells and the incubation with acetyl-LDL led to intracellular accumulation of cholesteryl esters, indicating the role of galectin-3 in endocytosis of AGE-proteins and modified LDLs. Since galectin-3 was localized and up-regulated in foam cells at human atherosclerotic lesions, the present results suggest that galectin-3 plays an important role in formation of atherosclerotic lesions in vivo, by modulating endocytic uptake of AGE-proteins and modified LDLs.

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