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

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,...

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Veröffentlicht in:Anatomical science international 2017, Vol.92 (1), p.25-36
1. Verfasser: Nio-Kobayashi, Junko
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description 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.
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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.</description><subject>Anatomy</subject><subject>Animal Anatomy</subject><subject>Animal Physiology</subject><subject>Animals</subject><subject>Axonogenesis</subject><subject>Axons - physiology</subject><subject>Brain - metabolism</subject><subject>Cattle</subject><subject>Cell Biology</subject><subject>Corpus luteum</subject><subject>Corpus Luteum - metabolism</subject><subject>Diabetes mellitus</subject><subject>Dorsal root ganglia</subject><subject>Epithelium</subject><subject>Epithelium - metabolism</subject><subject>Estrous Cycle - metabolism</subject><subject>Estrus</subject><subject>Female</subject><subject>Fibrosis</subject><subject>Galactose</subject><subject>Galectin-1</subject><subject>Galectin-3</subject><subject>Galectins - chemistry</subject><subject>Galectins - classification</subject><subject>Galectins - metabolism</subject><subject>Galectins - physiology</subject><subject>Ganglia, Spinal - metabolism</subject><subject>Glycoconjugates</subject><subject>Glycosyltransferases</subject><subject>Histology</subject><subject>Human Physiology</subject><subject>Humans</subject><subject>Intestines - metabolism</subject><subject>Lectins</subject><subject>Ligands</subject><subject>Localization</subject><subject>Lymphoid tissue</subject><subject>Macrophages</subject><subject>Macrophages - metabolism</subject><subject>Medicine</subject><subject>Medicine &amp; Public Health</subject><subject>Menstrual cycle</subject><subject>Menstrual Cycle - metabolism</subject><subject>Morphology</subject><subject>Nephrons</subject><subject>Nephrons - metabolism</subject><subject>Nerve Regeneration</subject><subject>Neurosciences</subject><subject>Organ Specificity</subject><subject>Pain</subject><subject>Phagocytosis</subject><subject>Regeneration</subject><subject>Reproductive system</subject><subject>Review Article</subject><subject>Skin</subject><subject>Skin - metabolism</subject><subject>Stem cells</subject><subject>Urinary tract</subject><issn>1447-6959</issn><issn>1447-073X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kcuKVDEQhoMozjj6AG4k4MaF0VxObksZvMGAmxHchXROpTvD6aQ9yVmM7-DL-CA-kzl2O4LgqlLUV3-q6kfoKaOvGKX6dWVcKkkoU4QKpYi6h87ZMGhCtfhy__RWVtoz9KjWG0qZlUw8RGdcS0uN1efo-3WqdQGCfR5xgGki9QAhxRTwVIKf0jffUsm4RLz1E4SWcn2Jf_4gPfOhlQpkk_KY8rYrpL2f8B20KrYdpBkfSoPcUi_GJYdVr-KU8Q781Ha_uTFV8BUeowfRTxWenOIF-vzu7fXlB3L16f3HyzdXJAirGuE-SCYHo72CQXG2YdZEIcbotdW67xaAmqCZ0Mz4fh3NuI-R28i04UM04gK9OOoe5vJ1gdrcPtV1e5-hLNUxMyihpDS6o8__QW_KMuc-neOcaSm5FivFjlSYS60zRHeY-zXmW8eoW71yR69cn8atXjnVe56dlJfNHsa7jj_mdIAfgdpLeQvz36__r_oL22egMw</recordid><startdate>2017</startdate><enddate>2017</enddate><creator>Nio-Kobayashi, Junko</creator><general>Springer Japan</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>K9.</scope><scope>7X8</scope></search><sort><creationdate>2017</creationdate><title>Tissue- and cell-specific localization of galectins, β-galactose-binding animal lectins, and their potential functions in health and disease</title><author>Nio-Kobayashi, Junko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c396t-2ac515487a6e4621b198f33dfa7977759ce08c713718a016712aff29f17824f83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Anatomy</topic><topic>Animal Anatomy</topic><topic>Animal Physiology</topic><topic>Animals</topic><topic>Axonogenesis</topic><topic>Axons - physiology</topic><topic>Brain - metabolism</topic><topic>Cattle</topic><topic>Cell Biology</topic><topic>Corpus luteum</topic><topic>Corpus Luteum - metabolism</topic><topic>Diabetes mellitus</topic><topic>Dorsal root ganglia</topic><topic>Epithelium</topic><topic>Epithelium - metabolism</topic><topic>Estrous Cycle - metabolism</topic><topic>Estrus</topic><topic>Female</topic><topic>Fibrosis</topic><topic>Galactose</topic><topic>Galectin-1</topic><topic>Galectin-3</topic><topic>Galectins - chemistry</topic><topic>Galectins - classification</topic><topic>Galectins - metabolism</topic><topic>Galectins - physiology</topic><topic>Ganglia, Spinal - metabolism</topic><topic>Glycoconjugates</topic><topic>Glycosyltransferases</topic><topic>Histology</topic><topic>Human Physiology</topic><topic>Humans</topic><topic>Intestines - metabolism</topic><topic>Lectins</topic><topic>Ligands</topic><topic>Localization</topic><topic>Lymphoid tissue</topic><topic>Macrophages</topic><topic>Macrophages - metabolism</topic><topic>Medicine</topic><topic>Medicine &amp; Public Health</topic><topic>Menstrual cycle</topic><topic>Menstrual Cycle - metabolism</topic><topic>Morphology</topic><topic>Nephrons</topic><topic>Nephrons - metabolism</topic><topic>Nerve Regeneration</topic><topic>Neurosciences</topic><topic>Organ Specificity</topic><topic>Pain</topic><topic>Phagocytosis</topic><topic>Regeneration</topic><topic>Reproductive system</topic><topic>Review Article</topic><topic>Skin</topic><topic>Skin - metabolism</topic><topic>Stem cells</topic><topic>Urinary tract</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nio-Kobayashi, Junko</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Anatomical science international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nio-Kobayashi, Junko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tissue- and cell-specific localization of galectins, β-galactose-binding animal lectins, and their potential functions in health and disease</atitle><jtitle>Anatomical science international</jtitle><stitle>Anat Sci Int</stitle><addtitle>Anat Sci Int</addtitle><date>2017</date><risdate>2017</risdate><volume>92</volume><issue>1</issue><spage>25</spage><epage>36</epage><pages>25-36</pages><issn>1447-6959</issn><eissn>1447-073X</eissn><abstract>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.</abstract><cop>Tokyo</cop><pub>Springer Japan</pub><pmid>27590897</pmid><doi>10.1007/s12565-016-0366-6</doi><tpages>12</tpages></addata></record>
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subjects Anatomy
Animal Anatomy
Animal Physiology
Animals
Axonogenesis
Axons - physiology
Brain - metabolism
Cattle
Cell Biology
Corpus luteum
Corpus Luteum - metabolism
Diabetes mellitus
Dorsal root ganglia
Epithelium
Epithelium - metabolism
Estrous Cycle - metabolism
Estrus
Female
Fibrosis
Galactose
Galectin-1
Galectin-3
Galectins - chemistry
Galectins - classification
Galectins - metabolism
Galectins - physiology
Ganglia, Spinal - metabolism
Glycoconjugates
Glycosyltransferases
Histology
Human Physiology
Humans
Intestines - metabolism
Lectins
Ligands
Localization
Lymphoid tissue
Macrophages
Macrophages - metabolism
Medicine
Medicine & Public Health
Menstrual cycle
Menstrual Cycle - metabolism
Morphology
Nephrons
Nephrons - metabolism
Nerve Regeneration
Neurosciences
Organ Specificity
Pain
Phagocytosis
Regeneration
Reproductive system
Review Article
Skin
Skin - metabolism
Stem cells
Urinary tract
title Tissue- and cell-specific localization of galectins, β-galactose-binding animal lectins, and their potential functions in health and disease
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