{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T06:47:35Z","timestamp":1791096455305,"version":"4.1.0"},"reference-count":89,"publisher":"Georg Thieme Verlag KG","issue":"09","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Thromb Haemost"],"published-print":{"date-parts":[[2013]]},"abstract":"<jats:title>Summary<\/jats:title>\n                  <jats:p>Plasma prekallikrein is the liver-derived precursor of the trypsin-like serine protease plasma kallikrein (PK) and circulates in plasma bound to high molecular weight kininogen. The zymogen is converted to PK by activated factor XII. PK drives multiple proteolytic reaction cascades in the cardiovascular system such as the intrinsic pathway of coagulation, the kallikrein-kinin system, the fibrinolytic system, the renin-angiotensin system and the alternative complement pathway. Here, we review the biochemistry and cell biology of PK and focus on recent in vivo studies that have established important functions of the protease in procoagulant and proinflammatory disease states. Targeting PK offers novel strategies not previously appreciated to interfere with thrombosis and vascular inflammation in a broad variety of diseases.<\/jats:p>","DOI":"10.1160\/th13-03-0258","type":"journal-article","created":{"date-parts":[[2013,7,12]],"date-time":"2013-07-12T01:39:43Z","timestamp":1373593183000},"page":"399-407","source":"Crossref","is-referenced-by-count":128,"title":["Plasma kallikrein: the bradykinin-producing enzyme"],"prefix":"10.1160","volume":"110","author":[{"given":"Jenny","family":"Bj\u00f6rkqvist","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne","family":"J\u00e4ms\u00e4","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Renn\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"194","published-online":{"date-parts":[[2017,11,22]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/s00281-011-0288-2","article-title":"The procoagulant and proinflammatory plasma contact system","volume":"34","author":"T Renne","year":"2012","journal-title":"Semin Immunopathol"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"4296","DOI":"10.1182\/blood-2012-07-292094","article-title":"In vivo roles of factor XII","volume":"22","author":"T Renne","year":"2012","journal-title":"Blood"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"3819","DOI":"10.1182\/blood.V90.10.3819","article-title":"Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes","volume":"90","author":"RW Colman","year":"1997","journal-title":"Blood"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"2410","DOI":"10.1021\/bi00357a017","article-title":"Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats","volume":"25","author":"DW Chung","year":"1986","journal-title":"Biochemistry"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"4892","DOI":"10.1074\/jbc.M105221200","article-title":"Characterisation of the H-kininogen-binding site on factor XI: a comparison of factor XI and plasma prekallikrein","volume":"277","author":"T Renne","year":"2002","journal-title":"J Biol Chem"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"14527","DOI":"10.1016\/S0021-9258(19)85270-5","article-title":"Mapping of the high molecular weight kininogen binding site of prekallikrein. 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