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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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. |
doi_str_mv | 10.1007/s12565-016-0366-6 |
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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><identifier>ISSN: 1447-6959</identifier><identifier>EISSN: 1447-073X</identifier><identifier>DOI: 10.1007/s12565-016-0366-6</identifier><identifier>PMID: 27590897</identifier><language>eng</language><publisher>Tokyo: Springer Japan</publisher><subject>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</subject><ispartof>Anatomical science international, 2017, Vol.92 (1), p.25-36</ispartof><rights>Japanese Association of Anatomists 2016</rights><rights>Copyright Springer Nature B.V. 2017</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c396t-2ac515487a6e4621b198f33dfa7977759ce08c713718a016712aff29f17824f83</citedby><cites>FETCH-LOGICAL-c396t-2ac515487a6e4621b198f33dfa7977759ce08c713718a016712aff29f17824f83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12565-016-0366-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12565-016-0366-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27590897$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nio-Kobayashi, Junko</creatorcontrib><title>Tissue- and cell-specific localization of galectins, β-galactose-binding animal lectins, and their potential functions in health and disease</title><title>Anatomical science international</title><addtitle>Anat Sci Int</addtitle><addtitle>Anat Sci Int</addtitle><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.</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 & 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 & 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 & 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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