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Galectin-4 in normal tissues and cancer

Huflejt, ME and Leffler, Hakon LU (2003) In Glycoconjugate Journal 20(4). p.247-255
Abstract
Galectin-4 belongs to a subfamily of galectins composed of two carbohydrate recognition domains within the same peptide chain. The two domains have all the conserved galectin signature amino acids, but their overall sequences are only approximately 40% identical. Both domains bind lactose with a similar affinity as other galectins, but their respective preferences for other disaccharides, and larger saccharides, are distinctly different. Thus galectin-4 has a property of a natural cross-linker, but in a modified sense since each domain prefers a different subset of ligands. Similarly to other galectins, galectin-4 is synthesized as a cytosolic protein, but can be externalized. During development and in adult normal tissues, galectin-4 is... (More)
Galectin-4 belongs to a subfamily of galectins composed of two carbohydrate recognition domains within the same peptide chain. The two domains have all the conserved galectin signature amino acids, but their overall sequences are only approximately 40% identical. Both domains bind lactose with a similar affinity as other galectins, but their respective preferences for other disaccharides, and larger saccharides, are distinctly different. Thus galectin-4 has a property of a natural cross-linker, but in a modified sense since each domain prefers a different subset of ligands. Similarly to other galectins, galectin-4 is synthesized as a cytosolic protein, but can be externalized. During development and in adult normal tissues, galectin-4 is expressed only in the alimentary tract, from the tongue to the large intestine. It is often found in relatively insoluble complexes, as a component of either adherens junctions or lipid rafts in the microvillus membrane, and it has been proposed to stabilize these structures. Strong expression of galectin-4 can be induced, however, in cancers from other tissues including breast and liver. Within a collection of human epithelial cancer cell lines, galectin-4 is overexpressed and soluble in those forming highly differentiated polarized monolayers, but absent in less differentiated ones. In cultured cells, intracellular galectin-4 may promote resistance to nutrient starvation, whereas-as an extracellular protein-it can mediate cell adhesion. Because of its distinct induction in breast and other cancers, it may be a valuable diagnostic marker and target for the development of inhibitory carbohydrate-based drugs. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
breast, promoter, carbohydrate specificity, galectin-4, galectins, cancer, epithelial cells
in
Glycoconjugate Journal
volume
20
issue
4
pages
247 - 255
publisher
Springer
external identifiers
  • wos:000221101200003
  • scopus:4143128862
ISSN
1573-4986
DOI
language
English
LU publication?
yes
id
4f1df190-4fac-47ea-81ee-01244fa24709 (old id 280458)
date added to LUP
2007-09-13 12:07:05
date last changed
2018-05-29 09:42:40
@article{4f1df190-4fac-47ea-81ee-01244fa24709,
  abstract     = {Galectin-4 belongs to a subfamily of galectins composed of two carbohydrate recognition domains within the same peptide chain. The two domains have all the conserved galectin signature amino acids, but their overall sequences are only approximately 40% identical. Both domains bind lactose with a similar affinity as other galectins, but their respective preferences for other disaccharides, and larger saccharides, are distinctly different. Thus galectin-4 has a property of a natural cross-linker, but in a modified sense since each domain prefers a different subset of ligands. Similarly to other galectins, galectin-4 is synthesized as a cytosolic protein, but can be externalized. During development and in adult normal tissues, galectin-4 is expressed only in the alimentary tract, from the tongue to the large intestine. It is often found in relatively insoluble complexes, as a component of either adherens junctions or lipid rafts in the microvillus membrane, and it has been proposed to stabilize these structures. Strong expression of galectin-4 can be induced, however, in cancers from other tissues including breast and liver. Within a collection of human epithelial cancer cell lines, galectin-4 is overexpressed and soluble in those forming highly differentiated polarized monolayers, but absent in less differentiated ones. In cultured cells, intracellular galectin-4 may promote resistance to nutrient starvation, whereas-as an extracellular protein-it can mediate cell adhesion. Because of its distinct induction in breast and other cancers, it may be a valuable diagnostic marker and target for the development of inhibitory carbohydrate-based drugs.},
  author       = {Huflejt, ME and Leffler, Hakon},
  issn         = {1573-4986},
  keyword      = {breast,promoter,carbohydrate specificity,galectin-4,galectins,cancer,epithelial cells},
  language     = {eng},
  number       = {4},
  pages        = {247--255},
  publisher    = {Springer},
  series       = {Glycoconjugate Journal},
  title        = {Galectin-4 in normal tissues and cancer},
  url          = {http://dx.doi.org/},
  volume       = {20},
  year         = {2003},
}