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 (-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 (Galectin-3) 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.Mouse Galectin-7
is a prototype monomeric galectin. It is expressed in stratified epithelia and is significantly
downregulated in squamous cell carcinomas. Galectin-7 is a proapoptotic protein that is
highly induced by the tumor suppressor protein p53. It functions intracellularly upstream of
JNK activation to enhance cytochrome c release during apoptosis.Galectin-7 may also be
involved in cellcell and cell-matrix interactions and exogenous galectin has been found to
accelerate the reepithelialization of wounds.
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 (-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 (Galectin-3) 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.Mouse Galectin-7
is a prototype monomeric galectin. It is expressed in stratified epithelia and is significantly
downregulated in squamous cell carcinomas. Galectin-7 is a proapoptotic protein that is
highly induced by the tumor suppressor protein p53. It functions intracellularly upstream of
JNK activation to enhance cytochrome c release during apoptosis.Galectin-7 may also be
involved in cellcell and cell-matrix interactions and exogenous galectin has been found to
accelerate the reepithelialization of wounds.
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