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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0040648,
umls-concept:C0062505,
umls-concept:C0162574,
umls-concept:C0185117,
umls-concept:C0205179,
umls-concept:C0205263,
umls-concept:C0225336,
umls-concept:C0597357,
umls-concept:C0598528,
umls-concept:C1334518,
umls-concept:C1879547,
umls-concept:C2911684
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pubmed:issue |
1-2
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pubmed:dateCreated |
2011-6-29
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pubmed:abstractText |
As an endo-? (1-4)-D: -glucuronidase, heparanase can specifically cleave carbohydrate chains of heparan sulfate (HS) and has been implicated in development of endothelial cells dsyfunction. The advanced glycation end products (AGEs) play a pivotal role in the pathology of diabetic complications. In the present study, we investigated the effect of AGE-bovine serum albumin (AGE-BSA) on heparanase expression in human microvascular endothelial cells (HMVECs) and the underlying molecular mechanisms. The results indicated that in vitro direct exposure of HMVECs to AGE-BSA (300, 1000, and 3000 ?g/ml) could increase heparanase mRNA and protein expression in a dose and time-dependent manner. The effect of 1000 ?g/ml AGE-BSA could be abolished by neutralization with antibody of the receptor for advanced glycation end products (RAGE). Moreover, pretreatment with inhibitors of nuclear factor-?B (NF-?B) or PI3-kinase did not affect heparanase expression induced by AGE-BSA. Nevertheless, small interference RNA (siRNA) for transcriptional factor FOXO4 could reduce the increase of heparanase expression in HMVECs induced by 1000 ?g/ml AGE-BSA. These results suggest that AGEs could induce heparanase expression in HMVECs by RAGE and predominantly through activation of the FOXO4 transcription factor.
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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/FOXO4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronidase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylation End Products, Advanced,
http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/advanced glycosylation end-product...,
http://linkedlifedata.com/resource/pubmed/chemical/heparanase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1573-4919
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
354
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
47-55
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pubmed:meshHeading |
pubmed-meshheading:21461610-Animals,
pubmed-meshheading:21461610-Cattle,
pubmed-meshheading:21461610-Diabetic Nephropathies,
pubmed-meshheading:21461610-Endothelial Cells,
pubmed-meshheading:21461610-Endothelium, Vascular,
pubmed-meshheading:21461610-Glucuronidase,
pubmed-meshheading:21461610-Glycosylation End Products, Advanced,
pubmed-meshheading:21461610-Humans,
pubmed-meshheading:21461610-L-Lactate Dehydrogenase,
pubmed-meshheading:21461610-Microvessels,
pubmed-meshheading:21461610-NF-kappa B,
pubmed-meshheading:21461610-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:21461610-Receptors, Immunologic,
pubmed-meshheading:21461610-Serum Albumin, Bovine,
pubmed-meshheading:21461610-Transcription, Genetic,
pubmed-meshheading:21461610-Transcription Factors
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pubmed:year |
2011
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pubmed:articleTitle |
Advanced glycation end-products induce heparanase expression in endothelial cells by the receptor for advanced glycation end products and through activation of the FOXO4 transcription factor.
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pubmed:affiliation |
Department of Endocrinology, Jiangsu Province Hospital of Chinese Medicine, 155 Han-Zhong Road, Nanjing 210029, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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