Journal
GLYCOCONJUGATE JOURNAL
Volume 19, Issue 7-9, Pages 527-535Publisher
SPRINGER
DOI: 10.1023/B:GLYC.0000014082.99675.2f
Keywords
extracellular-matrix; galectin-3; endocytosis; carbohydrate-recognition-domain; collagen-like-domain
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Funding
- NCI NIH HHS [U54 CA91408-02] Funding Source: Medline
- NIGMS NIH HHS [GM 08037] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [U54CA091408] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T34GM008037] Funding Source: NIH RePORTER
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Galectin-3 has been suspected of modulating cell to extracellular matrix interactions in a novel fashion ever since it was first described. However, the rapid accumulation of research data in just the last 8 years alone has completely changed our perspective of this multifunctional protein. Its chimeric nature (consists of carbohydrate recognition and collagen like domains) somehow makes it suited to interact with a plethora of interesting extracellular matrix proteins some of which might enable it to cross the plasma membrane despite its lack of appropriate signal peptides. It is now becoming established as a mediator of signal transduction events on the cell surface as well as a mediator of a variety of extra-cellular processes such as kidney development, angiogenesis, neuronal functions, tumor metastasis, autoimmune disorders, endocytosis and possibly exocytosis. Nevertheless, it still retains its unique position as a mediator/modulator of cell to extracellular matrix adhesive interactions. Cells, particularly epithelial cells which lack galectin-3 expression, interact poorly with their extracellular matrices. In some of these processes, it functions as a matricellular protein, displaying both pro- and anti-adhesive properties.
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