描述：
The galectins constitute a large family of carbohydratebinding proteins with specificity for
N-acetyl-lactosamine-containing glycoproteins. At least 14 mammalian galectins, which share
structural similarities in their carbohydrate recognition domains (CRD), have been identified
to date. The galectins have been classified into the prototype galectins (-1, -2, -5, -7, -10, -11,
-13, -14), which contain one CRD and exist either as a monomer or a noncovalent homodimer.
The chimera galectins (Galectin3) containing one CRD linked to a nonlectin domain, and the
tandem-repeat Galectins (-4, -6, -8, -9, -12) consisting of two CRDs joined by a linker peptide.
Galectins lack a classical signal peptide and can be localized to the cytosolic compartments
where they have intracellular functions. However, via one or more as yet unidentified non
classical secretory pathways, galectins can also be secreted to function extracellularly.
Individual members of the galectin family have different tissue distribution profiles and exhibit
subtle differences in their carbohydrate-binding specificities. Each family member may
preferentially bind to a unique subset of cellsurface glycoproteins.Galectin-8, also known as
prostate carcinoma tumor antigen 1 (PCTA1) in human, is a tandem repeat-type galectin.
Prototype (single CRD) isoforms arising through alternate gene splicing have also been
identified. Galectin-8 is highly expressed in lung carcinomas, certain forms of prostate
carcinomas, as well as other tumor cells. It binds to a subset of cell surface integrins to
modulate ECM-integrin interactions. As a soluble ligand, Galectin-8 can inhibit cell adhesion.
Immobilized Galectin8, however, has also been shown to promote cell adhesion.Human
and mouse Galectin8 share approximately 80% amino acid homology.
原厂资料：
The galectins constitute a large family of carbohydratebinding proteins with specificity for
N-acetyl-lactosamine-containing glycoproteins. At least 14 mammalian galectins, which share
structural similarities in their carbohydrate recognition domains (CRD), have been identified
to date. The galectins have been classified into the prototype galectins (-1, -2, -5, -7, -10, -11,
-13, -14), which contain one CRD and exist either as a monomer or a noncovalent homodimer.
The chimera galectins (Galectin3) containing one CRD linked to a nonlectin domain, and the
tandem-repeat Galectins (-4, -6, -8, -9, -12) consisting of two CRDs joined by a linker peptide.
Galectins lack a classical signal peptide and can be localized to the cytosolic compartments
where they have intracellular functions. However, via one or more as yet unidentified non
classical secretory pathways, galectins can also be secreted to function extracellularly.
Individual members of the galectin family have different tissue distribution profiles and exhibit
subtle differences in their carbohydrate-binding specificities. Each family member may
preferentially bind to a unique subset of cellsurface glycoproteins.Galectin-8, also known as
prostate carcinoma tumor antigen 1 (PCTA1) in human, is a tandem repeat-type galectin.
Prototype (single CRD) isoforms arising through alternate gene splicing have also been
identified. Galectin-8 is highly expressed in lung carcinomas, certain forms of prostate
carcinomas, as well as other tumor cells. It binds to a subset of cell surface integrins to
modulate ECM-integrin interactions. As a soluble ligand, Galectin-8 can inhibit cell adhesion.
Immobilized Galectin8, however, has also been shown to promote cell adhesion.Human
and mouse Galectin8 share approximately 80% amino acid homology.
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