Elafin is an endogenous human protein composed of an N-terminal transglutaminase substrate motif and a C-terminal WAP (whey acidic protein)-domain with antiproteolytic properties. Elafin is expressed predominantly in epithelial tissue and potently inhibits the neutrophil-derived serine proteases elastase and proteinase-3 by a competitive tight-binding mechanism. Furthermore, it inhibits EVE (endogenous vascular elastase). Studies on several animal models show that antiprotease augmentation with human elafin is an effective strategy in the treatment of inflammatory vascular, systemic and pulmonary diseases and of inflammation triggered by reperfusion injury. This raises the possibility that elafin might be effective in the treatment of a variety of human inflammatory diseases. In a Phase I clinical trial, elafin was well tolerated. Phase II trials are underway to investigate the therapeutic effects of elafin on post-operative inflammation and the clinical consequences of major surgery. Of particular interest is the reduction of post-operative morbidity after oesophagus cancer surgery, coronary artery bypass surgery and kidney transplantation.
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October 2011
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Conference Article|
September 21 2011
Therapeutic potential of human elafin
Lee Shaw;
Lee Shaw
*Proteo Biotech AG, Am-Kiel-Kanal 44, 24106 Kiel, Germany
†Institute of Biochemistry, University of Kiel, Olshausenstrasse 40, 24098 Kiel, Germany
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Oliver Wiedow
Oliver Wiedow
1
*Proteo Biotech AG, Am-Kiel-Kanal 44, 24106 Kiel, Germany
‡Department of Dermatology, University of Kiel, Schittenhelmstrasse 7, 24105 Kiel, Germany
1To whom correspondence should be addressed (email wiedow@proteo.de).
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Publisher: Portland Press Ltd
Received:
June 21 2011
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (5): 1450–1454.
Article history
Received:
June 21 2011
Citation
Lee Shaw, Oliver Wiedow; Therapeutic potential of human elafin. Biochem Soc Trans 1 October 2011; 39 (5): 1450–1454. doi: https://doi.org/10.1042/BST0391450
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