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rdf:type |
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lifeskim:mentions |
umls-concept:C0022713,
umls-concept:C0030685,
umls-concept:C0030956,
umls-concept:C0064833,
umls-concept:C0086418,
umls-concept:C0162337,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1963578,
umls-concept:C1999177
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pubmed:issue |
2
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pubmed:dateCreated |
2002-6-7
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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.
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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/Bradykinin,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Kininogen, High-Molecular-Weight,
http://linkedlifedata.com/resource/pubmed/chemical/Kininogen, Low-Molecular-Weight,
http://linkedlifedata.com/resource/pubmed/chemical/Kininogens,
http://linkedlifedata.com/resource/pubmed/chemical/Kinins,
http://linkedlifedata.com/resource/pubmed/chemical/Leukocyte Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/N-Formylmethionine...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Bradykinin B2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Bradykinin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:copyrightInfo |
(c) 2002 Elsevier Science (USA).
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
294
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
423-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12051729-Amino Acid Sequence,
pubmed-meshheading:12051729-Animals,
pubmed-meshheading:12051729-Blood Pressure,
pubmed-meshheading:12051729-Bradykinin,
pubmed-meshheading:12051729-Capillary Permeability,
pubmed-meshheading:12051729-Dose-Response Relationship, Drug,
pubmed-meshheading:12051729-Enzyme Inhibitors,
pubmed-meshheading:12051729-Female,
pubmed-meshheading:12051729-Guinea Pigs,
pubmed-meshheading:12051729-Humans,
pubmed-meshheading:12051729-Kininogen, High-Molecular-Weight,
pubmed-meshheading:12051729-Kininogen, Low-Molecular-Weight,
pubmed-meshheading:12051729-Kininogens,
pubmed-meshheading:12051729-Kinins,
pubmed-meshheading:12051729-Leukocyte Elastase,
pubmed-meshheading:12051729-Male,
pubmed-meshheading:12051729-Molecular Sequence Data,
pubmed-meshheading:12051729-Muscle, Smooth,
pubmed-meshheading:12051729-Muscle Contraction,
pubmed-meshheading:12051729-N-Formylmethionine Leucyl-Phenylalanine,
pubmed-meshheading:12051729-Neutrophils,
pubmed-meshheading:12051729-Peptides,
pubmed-meshheading:12051729-Rats,
pubmed-meshheading:12051729-Rats, Sprague-Dawley,
pubmed-meshheading:12051729-Receptor, Bradykinin B2,
pubmed-meshheading:12051729-Receptors, Bradykinin
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pubmed:year |
2002
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pubmed:articleTitle |
Release of a new vascular permeability enhancing peptide from kininogens by human neutrophil elastase.
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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
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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