Literature DB >> 8807716

Hirudins: from leeches to man.

R B Wallis1.   

Abstract

Hirudins are a group of highly homologous polypeptides from the medicinal leech, Hirudo medicinalis. They have an extremely high and specific affinity for thrombin and are consequently potent anticoagulants. They inhibit platelet aggregation induced by thrombin and efficiently inhibit thrombin when it is bound to a fibrin clot. Recombinant hirudins have now been produced and have been used to show a wide range of effects on thrombosis in animal models. They are particularly effective against venous-type thrombi and have greater effects than heparins on the platelet-rich thrombi in arteries. Recombinant hirudins are currently undergoing clinical trails in deep venous thrombosis and acute coronary syndrome and as an adjunct to thrombolysis in myocardial infarction. Results from pilot trials indicate promising advantages over the currently used antithrombotic agents. Larger clinical trails have been initiated and we await with great interest their imminent publication.

Entities:  

Mesh:

Substances:

Year:  1996        PMID: 8807716     DOI: 10.1055/s-2007-999007

Source DB:  PubMed          Journal:  Semin Thromb Hemost        ISSN: 0094-6176            Impact factor:   4.180


  9 in total

Review 1.  Laboratory diagnosis of heparin-induced thrombocytopenia and monitoring of alternative anticoagulants.

Authors:  Albrecht Leo; Susanne Winteroll
Journal:  Clin Diagn Lab Immunol       Date:  2003-09

Review 2.  Parenteral anticoagulants: Antithrombotic Therapy and Prevention of Thrombosis, 9th ed: American College of Chest Physicians Evidence-Based Clinical Practice Guidelines.

Authors:  David A Garcia; Trevor P Baglin; Jeffrey I Weitz; Meyer Michel Samama
Journal:  Chest       Date:  2012-02       Impact factor: 9.410

3.  Poly(lactic-co-glycolic) acid microspheres encapsulated in Pluronic F-127 prolong hirudin delivery and improve functional recovery from a demyelination lesion.

Authors:  Drew L Sellers; Tae Hee Kim; Christopher W Mount; Suzie H Pun; Philip J Horner
Journal:  Biomaterials       Date:  2014-07-23       Impact factor: 12.479

4.  Thrombin-induced glucose transport via Src-p38 MAPK pathway in vascular smooth muscle cells.

Authors:  Yasunari Kanda; Yasuhiro Watanabe
Journal:  Br J Pharmacol       Date:  2005-09       Impact factor: 8.739

Review 5.  Pharmacologic reperfusion therapy for acute myocardial infarction.

Authors:  Harry C Lowe; Briain D Mac Neill; Frans Van de Werf; Ik-Kyung Jang
Journal:  J Thromb Thrombolysis       Date:  2002-12       Impact factor: 2.300

6.  Clinician update: direct thrombin inhibitors in acute coronary syndromes.

Authors:  Joanna J Wykrzykowska; Sekar Kathiresan; Ik-Kyung Jang
Journal:  J Thromb Thrombolysis       Date:  2003-02       Impact factor: 2.300

Review 7.  Management of patients with acute coronary syndromes: what is the clinical role of direct thrombin inhibitors?

Authors:  John W Eikelboom; John French
Journal:  Drugs       Date:  2002       Impact factor: 9.546

8.  Expression, purification, and mass spectrometric analysis of 15N, 13C-labeled RGD-hirudin, expressed in Pichia pastoris, for NMR studies.

Authors:  Yinong Huang; Yanling Zhang; Yi Wu; Jue Wang; Xingang Liu; Linsen Dai; Longsheng Wang; Min Yu; Wei Mo
Journal:  PLoS One       Date:  2012-08-07       Impact factor: 3.240

9.  Structural basis of RGD-hirudin binding to thrombin: Tyr3 and five C-terminal residues are crucial for inhibiting thrombin activity.

Authors:  Yinong Huang; Yanling Zhang; Bing Zhao; Qiping Xu; Xiushi Zhou; Houyan Song; Min Yu; Wei Mo
Journal:  BMC Struct Biol       Date:  2014-12-20
  9 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.