描述：
Galectins are a family of carbohydratebinding proteins with specificity for
Nacetyllactosaminecontaining glycoproteins. At least 14 mammalian galectins
share structural similarities in their carbohydrate recognition domains (CRD),
forming three groups often termed prototype (one CRD), tandem-repeat (two CRDs)
and chimeric (one CRD, unique N-terminus). All lack classical signal peptides, but are
present and active both within and outside of the cell. Galectins are involved in cell
adhesion, migration, survival and apoptosis, and are often upor down-regulated in cancer.
Galectin-4 is a 36 kDa tandem-repeat galectin found throughout the gastrointestinal tract,
but also present in welldifferentiated breast and liver carcinomas. Each CRD binds a
different set of carbohydrate groups, including those found on red cell blood group antigens.
CRD1 also binds cholesterol 3-sulfate and other sulfatides, which are concentrated within
lipid raft membrane microdomains. Endocytosed Galectin-4 is thought to play a role in
forming the rafts, delivering them to the intestinal apical membrane, and stabilizing highly detergentresistant "superrafts". Human Galectin-4 shares 76%, 77%, 78% and 80%
aa identity with mouse, rat, bovine and porcine Galectin4, respectively, with the highest
identity occurring within the CRDs. A potential splice variant begins at aa 132 and lacks
most of the first CRD. Galectin-4 expression is concentrated within microvilli in the
gastrointestinal epithelium, where it can interact with CD3 and bind activated T cells
in the lamina propria during intestinal inflammation. Either proor anti-inflammatory
activity has been shown, depending on the mouse model used. Galectin-4 can also bind
lung, spleen and kidney macrophages, although its expression is normally low in these
tissues.
原厂资料：
Galectins are a family of carbohydratebinding proteins with specificity for
Nacetyllactosaminecontaining glycoproteins. At least 14 mammalian galectins
share structural similarities in their carbohydrate recognition domains (CRD),
forming three groups often termed prototype (one CRD), tandem-repeat (two CRDs)
and chimeric (one CRD, unique N-terminus). All lack classical signal peptides, but are
present and active both within and outside of the cell. Galectins are involved in cell
adhesion, migration, survival and apoptosis, and are often upor down-regulated in cancer.
Galectin-4 is a 36 kDa tandem-repeat galectin found throughout the gastrointestinal tract,
but also present in welldifferentiated breast and liver carcinomas. Each CRD binds a
different set of carbohydrate groups, including those found on red cell blood group antigens.
CRD1 also binds cholesterol 3-sulfate and other sulfatides, which are concentrated within
lipid raft membrane microdomains. Endocytosed Galectin-4 is thought to play a role in
forming the rafts, delivering them to the intestinal apical membrane, and stabilizing highly detergentresistant "superrafts". Human Galectin-4 shares 76%, 77%, 78% and 80%
aa identity with mouse, rat, bovine and porcine Galectin4, respectively, with the highest
identity occurring within the CRDs. A potential splice variant begins at aa 132 and lacks
most of the first CRD. Galectin-4 expression is concentrated within microvilli in the
gastrointestinal epithelium, where it can interact with CD3 and bind activated T cells
in the lamina propria during intestinal inflammation. Either proor anti-inflammatory
activity has been shown, depending on the mouse model used. Galectin-4 can also bind
lung, spleen and kidney macrophages, although its expression is normally low in these
tissues.
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