{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T22:23:07Z","timestamp":1768342987451,"version":"3.49.0"},"reference-count":0,"publisher":"American Physiological Society","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[1993,5,1]]},"abstract":"<jats:p> The role of thrombin in angiogenesis was investigated in the chick chorioallantoic membrane (CAM) system. alpha-Thrombin promoted angiogenesis in a dose-dependent fashion and at 8.4 pmol\/disk reached a maximum of 78% above the control. At a higher dose of alpha-thrombin (25 pmol\/disk) the angiogenic effect declines and this can be explained by desensitization of the thrombin receptor. The promotion of angiogenesis by alpha-thrombin is specific as evidenced by the reversal of this effect by hirudin, which binds both the catalytic and the anion-binding exosite of thrombin or by heparin, which binds thrombin and accelerates its inactivation by antithrombin III. gamma-Thrombin, which is catalytically active but lacks the anion-binding exosite required for clotting activity, promotes angiogenesis in the CAM in the same fashion and to the same extent as alpha-thrombin, at doses up to 130 pmol\/disk. Phenylalanyl-propyl-arginine chloromethyl ketone (P-PACK)-thrombin, the catalytically inactive analogue of alpha-thrombin that retains the anion-binding exosite, had no significant effect on angiogenesis in the CAM. When combined with alpha-thrombin, P-PACK-thrombin abolished the angiogenesis-promoting effect of alpha-thrombin. These results suggest that alpha-thrombin can promote angiogenesis in the CAM through interaction with its catalytic site without the requirement for fibrin formation. <\/jats:p>","DOI":"10.1152\/ajpcell.1993.264.5.c1302","type":"journal-article","created":{"date-parts":[[2017,12,24]],"date-time":"2017-12-24T14:53:56Z","timestamp":1514127236000},"page":"C1302-C1307","source":"Crossref","is-referenced-by-count":91,"title":["Thrombin promotes angiogenesis by a mechanism independent of fibrin formation"],"prefix":"10.1152","volume":"264","author":[{"given":"N. E.","family":"Tsopanoglou","sequence":"first","affiliation":[{"name":"Department of Pharmacology, University of Patras Medical School,Greece."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E.","family":"Pipili-Synetos","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, University of Patras Medical School,Greece."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M. E.","family":"Maragoudakis","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, University of Patras Medical School,Greece."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"24","container-title":["American Journal of Physiology-Cell Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.physiology.org\/doi\/pdf\/10.1152\/ajpcell.1993.264.5.C1302","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T19:41:50Z","timestamp":1718653310000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.physiology.org\/doi\/10.1152\/ajpcell.1993.264.5.C1302"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1993,5,1]]},"references-count":0,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1993,5,1]]}},"alternative-id":["10.1152\/ajpcell.1993.264.5.C1302"],"URL":"https:\/\/doi.org\/10.1152\/ajpcell.1993.264.5.c1302","relation":{},"ISSN":["0363-6143","1522-1563"],"issn-type":[{"value":"0363-6143","type":"print"},{"value":"1522-1563","type":"electronic"}],"subject":[],"published":{"date-parts":[[1993,5,1]]}}}