pubmed-article:12051729 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C0022713 | lld:lifeskim |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C0064833 | lld:lifeskim |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C0162337 | lld:lifeskim |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C1999177 | lld:lifeskim |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
pubmed-article:12051729 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
pubmed-article:12051729 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:12051729 | pubmed:dateCreated | 2002-6-7 | lld:pubmed |
pubmed-article:12051729 | pubmed:abstractText | Stimulated neutrophils produced vascular permeability enhancing (VPE) activity in the presence of high molecular weight kininogen (HMWK), which was inhibited mainly by a neutrophil elastase (NE) inhibitor or a bradykinin (BK) B(2)-receptor antagonist. NE (>3 nM) generated VPE activity from kininogens at normal plasma concentrations with the smaller protein being several fold more responsive than the larger protein, through releasing a new VPE peptide (E-kinin), SLMKRPPGFSPFRSSRI. Synthetic E-kinin, SLMKRPPGFSPFRSS and SLMKRPPGFSPFR had VPE and blood pressure lowering activities, which were comparable to the activities of BK and completely inhibited by B(2)-receptor antagonists. Interestingly, E-kinin and SLMKRPPGFSPFRSS did not induce smooth muscle contraction. These results suggest that E-kinin formed in vivo may be processed at the carboxy-terminus to give a peptide that can bind to the B(2)-receptor. The molecular mechanism for neutrophil-associated VPE may be explained by excision of E-kinin from kininogens by NE, followed by further processing of the peptide. | lld:pubmed |
pubmed-article:12051729 | pubmed:language | eng | lld:pubmed |
pubmed-article:12051729 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051729 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12051729 | pubmed:month | Jun | lld:pubmed |
pubmed-article:12051729 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:12051729 | pubmed:author | pubmed-author:TravisJamesJ | lld:pubmed |
pubmed-article:12051729 | pubmed:author | pubmed-author:HayashiIzumiI | lld:pubmed |
pubmed-article:12051729 | pubmed:author | pubmed-author:PotempaJanJ | lld:pubmed |
pubmed-article:12051729 | pubmed:author | pubmed-author:ImamuraTakahi... | lld:pubmed |
pubmed-article:12051729 | pubmed:author | pubmed-author:TanaseSumioS | lld:pubmed |
pubmed-article:12051729 | pubmed:author | pubmed-author:KozikAndrzejA | lld:pubmed |
pubmed-article:12051729 | pubmed:copyrightInfo | (c) 2002 Elsevier Science (USA). | lld:pubmed |
pubmed-article:12051729 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12051729 | pubmed:day | 7 | lld:pubmed |
pubmed-article:12051729 | pubmed:volume | 294 | lld:pubmed |
pubmed-article:12051729 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12051729 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12051729 | pubmed:pagination | 423-8 | lld:pubmed |
pubmed-article:12051729 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:12051729 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12051729 | pubmed:articleTitle | Release of a new vascular permeability enhancing peptide from kininogens by human neutrophil elastase. | lld:pubmed |
pubmed-article:12051729 | pubmed:affiliation | Division of Molecular Pathology, Department of Neuroscience and Immunology, Kumamoto University Graduate School of Medical Sciences, 2-2-1, Honjo, Kumamoto 860-0811, Japan. taka@kaiju.medic.kumamoto-u.ac.jp | lld:pubmed |
pubmed-article:12051729 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12051729 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:3827 | entrezgene:pubmed | pubmed-article:12051729 | lld:entrezgene |
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