Source:http://linkedlifedata.com/resource/pubmed/id/17357979
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
2007-4-2
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| pubmed:abstractText |
High mobility group box protein 1 (HMGB1) is a ubiquitous nuclear protein that can be actively released from the cell in certain conditions thereby mediating cytokine-like function. While nuclear HMGB1 modulates the transcriptional activity of cells, extracellular HMGB1 partially acts via binding to the receptor for advanced glycation end products (RAGE), which is highly expressed in lung tissue. Therefore, we studied the impact of food-derived advanced glycation end products (AGEs), the Maillard reaction products, on the lung expression of HMGB1. Feeding rats with AGE-rich diet, containing either bread crust or coffee beverage, resulted in an upregulation of HMGB1 mRNA and protein especially in those animals receiving bread crust diet. The expression of RAGE was not influenced. Moreover, we revealed a positive correlation between an increased lung AGE level and HMGB1 protein expression in both animal groups receiving either bread crust or coffee extract but not in the control group. In contrast, the ageing-related AGE accumulation was not associated with an increased level of HMGB1 protein in lung tissue from senescent (100 wk) compared to young-adult (24 wk) rats. Our data suggest a physiological role of food- but not ageing-associated AGEs in the regulation of the HMGB1 expression in lung.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Coffee,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylation End Products, Advanced,
http://linkedlifedata.com/resource/pubmed/chemical/HMGB1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/advanced glycosylation end-product...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
1613-4125
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
51
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
479-87
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:17357979-Aging,
pubmed-meshheading:17357979-Animals,
pubmed-meshheading:17357979-Bread,
pubmed-meshheading:17357979-Cell Line,
pubmed-meshheading:17357979-Coffee,
pubmed-meshheading:17357979-Diet,
pubmed-meshheading:17357979-Epithelial Cells,
pubmed-meshheading:17357979-Food,
pubmed-meshheading:17357979-Glycosylation End Products, Advanced,
pubmed-meshheading:17357979-HMGB1 Protein,
pubmed-meshheading:17357979-Humans,
pubmed-meshheading:17357979-Immunohistochemistry,
pubmed-meshheading:17357979-Lung,
pubmed-meshheading:17357979-Maillard Reaction,
pubmed-meshheading:17357979-Male,
pubmed-meshheading:17357979-Models, Animal,
pubmed-meshheading:17357979-RNA, Messenger,
pubmed-meshheading:17357979-Rats,
pubmed-meshheading:17357979-Rats, Wistar,
pubmed-meshheading:17357979-Receptors, Immunologic,
pubmed-meshheading:17357979-Up-Regulation
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| pubmed:year |
2007
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| pubmed:articleTitle |
Lung level of HMBG1 is elevated in response to advanced glycation end product-enriched food in vivo.
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| pubmed:affiliation |
Cardio-thoracic Surgery, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany. babett.bartling@medizin.uni-halle.de
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|