| pubmed-article:1905847 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1905847 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
| pubmed-article:1905847 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
| pubmed-article:1905847 | lifeskim:mentions | umls-concept:C0017973 | lld:lifeskim |
| pubmed-article:1905847 | lifeskim:mentions | umls-concept:C0040018 | lld:lifeskim |
| pubmed-article:1905847 | lifeskim:mentions | umls-concept:C0547047 | lld:lifeskim |
| pubmed-article:1905847 | lifeskim:mentions | umls-concept:C1550605 | lld:lifeskim |
| pubmed-article:1905847 | lifeskim:mentions | umls-concept:C0456205 | lld:lifeskim |
| pubmed-article:1905847 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1905847 | pubmed:dateCreated | 1991-8-8 | lld:pubmed |
| pubmed-article:1905847 | pubmed:abstractText | The effect of thrombin on the metabolism of glycosaminoglycans (GAG) in cultured bovine aortic endothelial cells was investigated. Incubation of confluent endothelial cell cultures with thrombin at 1.0 NIH U/ml for 8 h and above caused a significant decrease in the accumulation of [35S]sulfate-labeled GAG (35S-GAG) in the cell layer. After a 24 h incubation, thrombin at 0.5 U/ml and above decreased the accumulation of 35S-GAG in both cell layer and medium. The percentage of 35S-GAG released into the medium during the last 3 h of 24 h incubation was significantly increased by thrombin. In thrombin-treated cell layer, both heparan sulfate and the other GAG was significantly decreased at the same degree. The incorporation of both [3H]thymidine and [14C]leucine was significantly increased by thrombin. Gabexate mesilate, a serine protease inhibitor, suppressed the thrombin inhibition. From these results, it was suggested that thrombin decreased 35S-GAG in the endothelial cell layer without a nonspecific damage of the cells through mainly an inhibition of GAG production and additionally a stimulation of GAG release. | lld:pubmed |
| pubmed-article:1905847 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1905847 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1905847 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1905847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1905847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1905847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1905847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1905847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1905847 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1905847 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1905847 | pubmed:issn | 0049-3848 | lld:pubmed |
| pubmed-article:1905847 | pubmed:author | pubmed-author:HayashiTT | lld:pubmed |
| pubmed-article:1905847 | pubmed:author | pubmed-author:SakuragawaNN | lld:pubmed |
| pubmed-article:1905847 | pubmed:author | pubmed-author:KajiTT | lld:pubmed |
| pubmed-article:1905847 | pubmed:author | pubmed-author:AkaiTT | lld:pubmed |
| pubmed-article:1905847 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1905847 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1905847 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:1905847 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1905847 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1905847 | pubmed:pagination | 375-84 | lld:pubmed |
| pubmed-article:1905847 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:meshHeading | pubmed-meshheading:1905847-... | lld:pubmed |
| pubmed-article:1905847 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1905847 | pubmed:articleTitle | Thrombin decreases glycosaminoglycans content of endothelial cells in culture. | lld:pubmed |
| pubmed-article:1905847 | pubmed:affiliation | Department of Environmental Science, Faculty of Pharmaceutical Sciences, Hokuriku University, Kanazawa, Japan. | lld:pubmed |
| pubmed-article:1905847 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1905847 | lld:pubmed |
