| pubmed-article:19345232 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19345232 | lifeskim:mentions | umls-concept:C0014257 | lld:lifeskim |
| pubmed-article:19345232 | lifeskim:mentions | umls-concept:C1522318 | lld:lifeskim |
| pubmed-article:19345232 | lifeskim:mentions | umls-concept:C0007428 | lld:lifeskim |
| pubmed-article:19345232 | lifeskim:mentions | umls-concept:C0068355 | lld:lifeskim |
| pubmed-article:19345232 | lifeskim:mentions | umls-concept:C0277785 | lld:lifeskim |
| pubmed-article:19345232 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
| pubmed-article:19345232 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:19345232 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19345232 | pubmed:dateCreated | 2009-6-15 | lld:pubmed |
| pubmed-article:19345232 | pubmed:abstractText | Cathepsin L is a cysteine protease that can generate endogenous endostatin in vascular and epithelial basement membranes and importantly participates in a variety of pathophysiological processes. The present study was designed to determine whether this cathepsin L-derived endogenous endostatin alters endothelium-dependent vasodilator responses in coronary arteries via NAD(P)H oxidase activation. In isolated and perfused small bovine coronary arteries, administration of cathepsin L (200 ng/ml) markedly attenuated endothelium-dependent vasodilator responses to bradykinin or A23187 by 56.16+/-9.58% and 68.95+/-10.32%, respectively. This inhibitory effect of cathepsin L on endothelium-dependent vasodilator responses could be significantly reversed by pre-incubation of the arteries with O(2)(-) scavenger, Tiron, or neutralizing anti-endostatin antibody. By fluorescent ELISA assay, cathepsin L dose-dependently increased endostatin production in coronary arteries. In situ high-speed dual wavelength switching fluorescent microscopic imaging showed that cathepsin L decreased bradykinin- and A23187-induced NO levels in the intact endothelium, but it had no effect on Ca(2+) response to these vasodilators. This cathepsin L-induced reduction of NO was restored by the pretreatment of an anti-endostatin antibody. Electron spin resonance (ESR) analysis demonstrated that cathepsin L increased O(2)(-) production which could be markedly attenuated by the NAD(P)H oxidase inhibitors, apocynin or anti-endostatin antibody. It is concluded that endostatin could be endogenously produced in coronary arteries when cathepsin L is increased and that this cathepsin L-derived endostatin, if excessive, may result in endothelial dysfunction through enhanced production of O(2)(-) due to NAD(P)H oxidase activation. | lld:pubmed |
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| pubmed-article:19345232 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19345232 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19345232 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19345232 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19345232 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:19345232 | pubmed:issn | 1095-9319 | lld:pubmed |
| pubmed-article:19345232 | pubmed:author | pubmed-author:ZhangFanF | lld:pubmed |
| pubmed-article:19345232 | pubmed:author | pubmed-author:ZhangYangY | lld:pubmed |
| pubmed-article:19345232 | pubmed:author | pubmed-author:LiPin-LanPL | lld:pubmed |
| pubmed-article:19345232 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19345232 | pubmed:volume | 78 | lld:pubmed |
| pubmed-article:19345232 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19345232 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19345232 | pubmed:pagination | 45-50 | lld:pubmed |
| pubmed-article:19345232 | pubmed:dateRevised | 2010-12-28 | lld:pubmed |
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| pubmed-article:19345232 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19345232 | pubmed:articleTitle | Dependence of cathepsin L-induced coronary endothelial dysfunction upon activation of NAD(P)H oxidase. | lld:pubmed |
| pubmed-article:19345232 | pubmed:affiliation | Department of Pharmacology and Toxicology, Medical College of Virginia, Virginia Commonwealth University, 410 N 12th, Richmond, VA 23298, USA. | lld:pubmed |
| pubmed-article:19345232 | pubmed:publicationType | Journal Article | lld:pubmed |
