| pubmed-article:12071855 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C0015879 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C0006100 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C0023693 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
| pubmed-article:12071855 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
| pubmed-article:12071855 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:12071855 | pubmed:dateCreated | 2002-6-19 | lld:pubmed |
| pubmed-article:12071855 | pubmed:abstractText | Ferritin is an iron-storage protein that exists in both intracellular and extracellular compartments. We have previously identified H-kininogen (high-molecular-weight kininogen) as a ferritin-binding protein [Torti and Torti (1998) J. Biol. Chem. 273, 13630-13635]. H-Kininogen is a precursor of the potent pro-inflammatory peptide bradykinin, which is released from H-kininogen following cleavage of H-kininogen by the serine protease kallikrein. In this report, we demonstrate that binding of ferritin to H-kininogen occurs via the modified light chain of H-kininogen, and that ferritin binds preferentially to activated H-kininogen. We further demonstrate that binding of ferritin to H-kininogen retards the proteolytic cleavage of H-kininogen by kallikrein and its subsequent release of bradykinin from H-kininogen. Ferritin does not interfere with the ability of kallikrein to digest a synthetic substrate, suggesting that ferritin specifically impedes the ability of kallikrein to digest H-kininogen, perhaps by steric hindrance. Based on these results, we propose a model of sequential H-kininogen cleavage and ferritin binding. These results are consistent with the hypothesis that the binding of ferritin to H-kininogen may serve to modulate bradykinin release. | lld:pubmed |
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| pubmed-article:12071855 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12071855 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12071855 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12071855 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12071855 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12071855 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:12071855 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:12071855 | pubmed:author | pubmed-author:TortiSuzy VSV | lld:pubmed |
| pubmed-article:12071855 | pubmed:author | pubmed-author:TortiFrank... | lld:pubmed |
| pubmed-article:12071855 | pubmed:author | pubmed-author:Parthasarathy... | lld:pubmed |
| pubmed-article:12071855 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12071855 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12071855 | pubmed:volume | 365 | lld:pubmed |
| pubmed-article:12071855 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12071855 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12071855 | pubmed:pagination | 279-86 | lld:pubmed |
| pubmed-article:12071855 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12071855 | pubmed:meshHeading | pubmed-meshheading:12071855... | lld:pubmed |
| pubmed-article:12071855 | pubmed:meshHeading | pubmed-meshheading:12071855... | lld:pubmed |
| pubmed-article:12071855 | pubmed:meshHeading | pubmed-meshheading:12071855... | lld:pubmed |
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| pubmed-article:12071855 | pubmed:meshHeading | pubmed-meshheading:12071855... | lld:pubmed |
