描述：
The galectins constitute a large family of carbohydratebinding proteins with specificity
for Nacetyllactosaminecontaining glycoproteins. At least 14 mammalian galectins,
which share structural similarities in their carbohydrate recognition domains (CRD), have
been identified. The galectins have been classified into the prototype galectins, 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 galectinsconsisting 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 nonclassical 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 carbohydratebinding specificities. Each family member may preferentially bind to
a unique subset of cellsurface glycoproteins.Galectin-3, also known as Mac2, L29, CBP35
and εBP, is a chimera galectin that has a tendency to dimerize. Besides the soluble protein,
alternatively spliced forms of chicken Galectin3 containing a transmembranespanning
domain and a leucine zipper motif have been reported. Galectin-3 is expressed in tumor
cells, macrophages, activated T cells, osteoclasts, epithelial cells, and fibroblasts. It binds
various matrix glycoproteins including laminin, fibronectin, LAMPS, 90K/Mac2BP,MP20
and CEA. Galectin-3 promotes cell growth and proliferation for many cell types. Galectin-3
acts intracellularly to prevent apoptosis. Depending on the cell types,Galectin-3 exhibits
proor antiadhesive properties. Galectin-3 has proinflammatory activities in vitro and in vivo.
It induces proinflammatory and inhibits Th2 type cytokine production. Galectin-3
chemoattracts monocytes and macrophages. It activates and degranulates basophils
and mast cells. Elevated circulating levels of Galectin-3 has been show to correlate with
the malignant potential of several types of cancer, suggesting that Galectin-3 is also involved
in tumor growth and metastasis. Human and mouse Galectin-3 shares approximately 80%
amino acid sequence similarity.
原厂资料：
The galectins constitute a large family of carbohydratebinding proteins with specificity
for Nacetyllactosaminecontaining glycoproteins. At least 14 mammalian galectins,
which share structural similarities in their carbohydrate recognition domains (CRD), have
been identified. The galectins have been classified into the prototype galectins, 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 galectinsconsisting 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 nonclassical 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 carbohydratebinding specificities. Each family member may preferentially bind to
a unique subset of cellsurface glycoproteins.Galectin-3, also known as Mac2, L29, CBP35
and εBP, is a chimera galectin that has a tendency to dimerize. Besides the soluble protein,
alternatively spliced forms of chicken Galectin3 containing a transmembranespanning
domain and a leucine zipper motif have been reported. Galectin-3 is expressed in tumor
cells, macrophages, activated T cells, osteoclasts, epithelial cells, and fibroblasts. It binds
various matrix glycoproteins including laminin, fibronectin, LAMPS, 90K/Mac2BP,MP20
and CEA. Galectin-3 promotes cell growth and proliferation for many cell types. Galectin-3
acts intracellularly to prevent apoptosis. Depending on the cell types,Galectin-3 exhibits
proor antiadhesive properties. Galectin-3 has proinflammatory activities in vitro and in vivo.
It induces proinflammatory and inhibits Th2 type cytokine production. Galectin-3
chemoattracts monocytes and macrophages. It activates and degranulates basophils
and mast cells. Elevated circulating levels of Galectin-3 has been show to correlate with
the malignant potential of several types of cancer, suggesting that Galectin-3 is also involved
in tumor growth and metastasis. Human and mouse Galectin-3 shares approximately 80%
amino acid sequence similarity.
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