Tissue- and cell-specific localization of galectins, β-galactose-binding animal lectins, and their potential functions in health and disease

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• 作者：Junko Nio-Kobayashi
• 关键词：Galectin ; Epithelium ; Macrophage ; Reproduction ; Fibrosis
• 刊名：Anatomical Science International
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：92
• 期：1
• 页码：25-36
• 全文大小：
• 刊物主题：Anatomy; Human Physiology; Neurosciences; Cell Biology; Animal Anatomy / Morphology / Histology; Animal Physiology;
• 出版者：Springer Japan
• ISSN：1447-073X
• 卷排序：92

文摘

Fifteen galectins, β-galactose-binding animal lectins, are known to be distributed throughout the body. We herein summarize current knowledge on the tissue- and cell-specific localization of galectins and their potential functions in health and disease. Galectin-3 is widely distributed in epithelia, including the simple columnar epithelium in the gut, stratified squamous epithelium in the gut and skin, and transitional epithelium and several regions in nephrons in the urinary tract. Galectin-2 and galectin-4/6 are gut-specific, while galectin-7 is found in the stratified squamous epithelium in the gut and skin. The reproductive tract mainly contains galectin-1 and galectin-3, and their expression markedly changes during the estrous/menstrual cycle. The galectin subtype expressed in the corpus luteum (CL) changes in association with luteal function. The CL of women and cows displays a “galectin switch” with coordinated changes in the major galectin subtype and its ligand glycoconjugate structure. Macrophages express galectin-3, which may be involved in phagocytotic activity. Lymphoid tissues contain galectin-3-positive macrophages, which are not always stained with the macrophage marker, F4/80. Subsets of neurons in the brain and dorsal root ganglion express galectin-1 and galectin-3, which may contribute to the regeneration of damaged axons, stem cell differentiation, and pain control. The subtype-specific contribution of galectins to implantation, fibrosis, and diabetes are also discussed. The function of galectins may differ depending on the tissues or cells in which they act. The ligand glycoconjugate structures mediated by glycosyltransferases including MGAT5, ST6GAL1, and C2GnT are important for revealing the functions of galectins in healthy and disease states.