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rdf:type |
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lifeskim:mentions |
umls-concept:C0019878,
umls-concept:C0024264,
umls-concept:C0205263,
umls-concept:C0271510,
umls-concept:C0282554,
umls-concept:C1167322,
umls-concept:C1332824,
umls-concept:C1424460,
umls-concept:C1515655,
umls-concept:C1533691,
umls-concept:C1801960,
umls-concept:C2752508
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pubmed:issue |
5A
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pubmed:dateCreated |
2008-11-17
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pubmed:abstractText |
Hyperhomocysteinemia induces endothelial dysfunction and promotes atherosclerotic vascular disease. Infiltrates of activated macrophages and lymphocytes are observed in human and experimental atherosclerotic lesions, their emigration being guided by endothelial-leukocyte adhesion molecules and chemoattractants. The CXC-chemokine CXCL16 functions as an adhesion molecule by interacting with its receptor (CXCR6) and also as a scavenger for oxidized low density lipoprotein (oxLDL). We investigated the modulation of CXCL16 on cultured endothelial cells (EC) and the recruitment of CXCR6(+) lymphocytes in response to homocysteine (Hcy), in vitro and in vivo.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/CXCR6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CXCL6,
http://linkedlifedata.com/resource/pubmed/chemical/Cxcr6 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Homocysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/PPAR gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, CXCR,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Chemokine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus,
http://linkedlifedata.com/resource/pubmed/chemical/oxidized low density lipoprotein
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pubmed:status |
MEDLINE
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pubmed:issn |
1582-1838
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1700-9
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pubmed:meshHeading |
pubmed-meshheading:18194461-Animals,
pubmed-meshheading:18194461-Antioxidants,
pubmed-meshheading:18194461-Blood Vessels,
pubmed-meshheading:18194461-Cell Adhesion,
pubmed-meshheading:18194461-Cell Membrane,
pubmed-meshheading:18194461-Cell Movement,
pubmed-meshheading:18194461-Cells, Cultured,
pubmed-meshheading:18194461-Chemokine CXCL6,
pubmed-meshheading:18194461-Endothelial Cells,
pubmed-meshheading:18194461-Homocysteine,
pubmed-meshheading:18194461-Humans,
pubmed-meshheading:18194461-Lipoproteins, LDL,
pubmed-meshheading:18194461-Lymphocytes,
pubmed-meshheading:18194461-Mice,
pubmed-meshheading:18194461-PPAR gamma,
pubmed-meshheading:18194461-Receptors, CXCR,
pubmed-meshheading:18194461-Receptors, Chemokine,
pubmed-meshheading:18194461-Receptors, Virus,
pubmed-meshheading:18194461-Up-Regulation
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pubmed:articleTitle |
Homocysteine up-regulates vascular transmembrane chemokine CXCL16 and induces CXCR6+ lymphocyte recruitment in vitro and in vivo.
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pubmed:affiliation |
Institute for Molecular Cardiovascular Research, University Hospital, Aachen, Germany. potilia@gmx.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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