Localization of the Human Gene for Advanced Glycosylation End Product-Specific Receptor (AGER) to Chromosome 6p21.3
Advanced glycosylation end products (AGEs), which are the result of nonenzymatic glycosylation and oxidation of proteins exposed to aldoses, are present in plasma and accumulate in the tissues during aging and at an accelerated rate in diabetes as a result of hyperglycemia. A cell surface receptor f...
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| Veröffentlicht in: | Genomics 1994-12, Vol.24 (3), p.606-608 |
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| creator | Vissing, Henrik Aagaard, Lissi Tommerup, Niels Boel, Esper |
| description | Advanced glycosylation end products (AGEs), which are the result of nonenzymatic glycosylation and oxidation of proteins exposed to aldoses, are present in plasma and accumulate in the tissues during aging and at an accelerated rate in diabetes as a result of hyperglycemia. A cell surface receptor for AGE (RAGE) with homology to the immunoglobulin superfamily of receptors has been isolated, and both RAGE antigen and mRNA have been identified in the endothelium, vascular smooth muscle cells, cardiac myocytes, monocyte-derived macrophages, and neural tissue. AGEs modulate a variety of biological reactions in tissues, such as monocyte/macrophage migration and production of cytokine-growth factors in mononuclear cells, as well as permeability, growth, and thrombogenicity of endothelia cells. Although AGEs interact specifically with RAGE, it has been suggested that AGEs are accidental and potentially pathogenic ligands for this receptor. In this study, we have used fluorescence in situ hybridization (FISH) to assign the human RAGE (AGER) gene to chromosome 6p21.3. 9 refs., 1 fig. |
| doi_str_mv | 10.1006/geno.1994.1676 |
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A cell surface receptor for AGE (RAGE) with homology to the immunoglobulin superfamily of receptors has been isolated, and both RAGE antigen and mRNA have been identified in the endothelium, vascular smooth muscle cells, cardiac myocytes, monocyte-derived macrophages, and neural tissue. AGEs modulate a variety of biological reactions in tissues, such as monocyte/macrophage migration and production of cytokine-growth factors in mononuclear cells, as well as permeability, growth, and thrombogenicity of endothelia cells. Although AGEs interact specifically with RAGE, it has been suggested that AGEs are accidental and potentially pathogenic ligands for this receptor. 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A cell surface receptor for AGE (RAGE) with homology to the immunoglobulin superfamily of receptors has been isolated, and both RAGE antigen and mRNA have been identified in the endothelium, vascular smooth muscle cells, cardiac myocytes, monocyte-derived macrophages, and neural tissue. AGEs modulate a variety of biological reactions in tissues, such as monocyte/macrophage migration and production of cytokine-growth factors in mononuclear cells, as well as permeability, growth, and thrombogenicity of endothelia cells. Although AGEs interact specifically with RAGE, it has been suggested that AGEs are accidental and potentially pathogenic ligands for this receptor. In this study, we have used fluorescence in situ hybridization (FISH) to assign the human RAGE (AGER) gene to chromosome 6p21.3. 9 refs., 1 fig.</description><subject>AGE DEPENDENCE</subject><subject>Base Sequence</subject><subject>BIOLOGICAL MARKERS</subject><subject>BIOLOGY AND MEDICINE, BASIC STUDIES</subject><subject>Chromosome Mapping</subject><subject>Chromosomes, Human, Pair 6 - ultrastructure</subject><subject>Cloning, Molecular</subject><subject>DIABETES MELLITUS</subject><subject>DNA HYBRIDIZATION</subject><subject>DNA Primers - genetics</subject><subject>DNA, Complementary - genetics</subject><subject>FLUORESCENCE</subject><subject>GENES</subject><subject>GENETIC MAPPING</subject><subject>GLYCOLYSIS</subject><subject>HUMAN CHROMOSOME 6</subject><subject>Humans</subject><subject>IMMUNOGLOBULINS</subject><subject>In Situ Hybridization, Fluorescence</subject><subject>Molecular Sequence Data</subject><subject>Polymerase Chain Reaction</subject><subject>PROTEINS</subject><subject>Receptor for Advanced Glycation End Products</subject><subject>RECEPTORS</subject><subject>Receptors, Immunologic - genetics</subject><issn>0888-7543</issn><issn>1089-8646</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kc2r1DAUxYMoz3lPt-6EuBFdtCZN89HlMIzzhAHlqevQSW6cSNvUJH0w_vW2dHg7V_fC_Z3D5RyE3lBSUkLEp18whJI2TV1SIcUztKFENYUStXiONkQpVUhes5foNqXfhJCGqeoG3UhJGadqg9IxmLbzf9vsw4CDw_kM-H7q2wEfYADsQsRb-9gOBiw-dBcT0qVb4f1g8bcY7GRy8X0E4503-AEMjHkWfdge9g8fcQ54d46hDyn0gMVY0ZK9Qi9c2yV4fZ136Ofn_Y_dfXH8eviy2x4LUzOaC3dqneDcKkpPTc2ZqB2bJxDKT0JV82pc04AwrGKVtNZJzoh1RBolHW8Fu0PvVt-QstfJ-AzmbMIwgMm6qinh1cy8X5kxhj8TpKx7nwx0XTtAmJKWUpGKKzaD5QqaGFKK4PQYfd_Gi6ZEL03opQm9NKGXJmbB26vzdOrBPuHX6Oe7Wu8wR_DoIS4fwpKzj8uDNvj_Wf8DqDiWGg</recordid><startdate>19941201</startdate><enddate>19941201</enddate><creator>Vissing, Henrik</creator><creator>Aagaard, Lissi</creator><creator>Tommerup, Niels</creator><creator>Boel, Esper</creator><general>Elsevier Inc</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>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19941201</creationdate><title>Localization of the Human Gene for Advanced Glycosylation End Product-Specific Receptor (AGER) to Chromosome 6p21.3</title><author>Vissing, Henrik ; Aagaard, Lissi ; Tommerup, Niels ; Boel, Esper</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c431t-fbaf655d811b945364f3945e015b682945cf99e6c32327ddf7530df07c87f5a63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>AGE DEPENDENCE</topic><topic>Base Sequence</topic><topic>BIOLOGICAL MARKERS</topic><topic>BIOLOGY AND MEDICINE, BASIC STUDIES</topic><topic>Chromosome Mapping</topic><topic>Chromosomes, Human, Pair 6 - ultrastructure</topic><topic>Cloning, Molecular</topic><topic>DIABETES MELLITUS</topic><topic>DNA HYBRIDIZATION</topic><topic>DNA Primers - genetics</topic><topic>DNA, Complementary - genetics</topic><topic>FLUORESCENCE</topic><topic>GENES</topic><topic>GENETIC MAPPING</topic><topic>GLYCOLYSIS</topic><topic>HUMAN CHROMOSOME 6</topic><topic>Humans</topic><topic>IMMUNOGLOBULINS</topic><topic>In Situ Hybridization, Fluorescence</topic><topic>Molecular Sequence Data</topic><topic>Polymerase Chain Reaction</topic><topic>PROTEINS</topic><topic>Receptor for Advanced Glycation End Products</topic><topic>RECEPTORS</topic><topic>Receptors, Immunologic - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vissing, Henrik</creatorcontrib><creatorcontrib>Aagaard, Lissi</creatorcontrib><creatorcontrib>Tommerup, Niels</creatorcontrib><creatorcontrib>Boel, Esper</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Genomics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vissing, Henrik</au><au>Aagaard, Lissi</au><au>Tommerup, Niels</au><au>Boel, Esper</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Localization of the Human Gene for Advanced Glycosylation End Product-Specific Receptor (AGER) to Chromosome 6p21.3</atitle><jtitle>Genomics</jtitle><addtitle>Genomics</addtitle><date>1994-12-01</date><risdate>1994</risdate><volume>24</volume><issue>3</issue><spage>606</spage><epage>608</epage><pages>606-608</pages><issn>0888-7543</issn><eissn>1089-8646</eissn><abstract>Advanced glycosylation end products (AGEs), which are the result of nonenzymatic glycosylation and oxidation of proteins exposed to aldoses, are present in plasma and accumulate in the tissues during aging and at an accelerated rate in diabetes as a result of hyperglycemia. A cell surface receptor for AGE (RAGE) with homology to the immunoglobulin superfamily of receptors has been isolated, and both RAGE antigen and mRNA have been identified in the endothelium, vascular smooth muscle cells, cardiac myocytes, monocyte-derived macrophages, and neural tissue. AGEs modulate a variety of biological reactions in tissues, such as monocyte/macrophage migration and production of cytokine-growth factors in mononuclear cells, as well as permeability, growth, and thrombogenicity of endothelia cells. Although AGEs interact specifically with RAGE, it has been suggested that AGEs are accidental and potentially pathogenic ligands for this receptor. In this study, we have used fluorescence in situ hybridization (FISH) to assign the human RAGE (AGER) gene to chromosome 6p21.3. 9 refs., 1 fig.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7713518</pmid><doi>10.1006/geno.1994.1676</doi><tpages>3</tpages></addata></record> |
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| subjects | AGE DEPENDENCE Base Sequence BIOLOGICAL MARKERS BIOLOGY AND MEDICINE, BASIC STUDIES Chromosome Mapping Chromosomes, Human, Pair 6 - ultrastructure Cloning, Molecular DIABETES MELLITUS DNA HYBRIDIZATION DNA Primers - genetics DNA, Complementary - genetics FLUORESCENCE GENES GENETIC MAPPING GLYCOLYSIS HUMAN CHROMOSOME 6 Humans IMMUNOGLOBULINS In Situ Hybridization, Fluorescence Molecular Sequence Data Polymerase Chain Reaction PROTEINS Receptor for Advanced Glycation End Products RECEPTORS Receptors, Immunologic - genetics |
| title | Localization of the Human Gene for Advanced Glycosylation End Product-Specific Receptor (AGER) to Chromosome 6p21.3 |
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