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.
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
tandemrepeat 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 carbohydratebinding specificities. Each family member may
preferentially bind to a unique subset of cell-surface glycoproteins.Human Galectin-7 is a
prototype monomeric galectin. It is specifically expressed in stratified epithelia, notably in
epidermis, but is barely detectable in epidermal tumors and significantly down regulated or
absent from squamous carconima cell lines. The Galectin-7 gene is induced by tumor
suppressor protein p53 transcriptional activity following genotoxic events. A proapoptotic
protein, Galectin-7 functions intracellularly upstream of JNK activation and cytochromec
release. This protein has been shown to increase the susceptibility of keratinocytes to UVB
induced apoptosis, an essential processss in the maintenance of epidermal homeostasis.
Cell lines transfected with the Galectin-7 gene localized the protein in the nucleus and
intracellularly. Human and mouse Galectin7 share 79% 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.
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
tandemrepeat 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 carbohydratebinding specificities. Each family member may
preferentially bind to a unique subset of cell-surface glycoproteins.Human Galectin-7 is a
prototype monomeric galectin. It is specifically expressed in stratified epithelia, notably in
epidermis, but is barely detectable in epidermal tumors and significantly down regulated or
absent from squamous carconima cell lines. The Galectin-7 gene is induced by tumor
suppressor protein p53 transcriptional activity following genotoxic events. A proapoptotic
protein, Galectin-7 functions intracellularly upstream of JNK activation and cytochromec
release. This protein has been shown to increase the susceptibility of keratinocytes to UVB
induced apoptosis, an essential processss in the maintenance of epidermal homeostasis.
Cell lines transfected with the Galectin-7 gene localized the protein in the nucleus and
intracellularly. Human and mouse Galectin7 share 79% amino acid homology.
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