Biochemical Features, Molecular Biology and Clinical Relevance of the Human 15-Domain Serine Proteinase Inhibitor LEKTI

M. Walden; P. Kreutzmann; K. Drögemüller; H. John; W.-G. Forssmann; H.-J. Mägert

doi:10.1515/BC.2002.124

Published by De Gruyter June 1, 2005

Biochemical Features, Molecular Biology and Clinical Relevance of the Human 15-Domain Serine Proteinase Inhibitor LEKTI

M. Walden , P. Kreutzmann , K. Drögemüller , H. John , W.-G. Forssmann and H.-J. Mägert

From the journal Biological Chemistry

https://doi.org/10.1515/BC.2002.124

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Abstract

Based on the isolation of a 55 amino acid peptide from human hemofiltrate, we cloned the cDNA for a novel human 15-domain serine proteinase inhibitor termed LEKTI. A trypsininhibiting activity was demonstrated for three different domains. High levels of expression of the corresponding gene were detected in oral mucosa, followed by the tonsils, parathyroid glands, thymus, and trachea. Hovnanian and coworkers recently found that certain mutations within the LEKTI gene are linked to the severe congenital disease Netherton syndrome and atopic manifestations (including asthma). Thus, a future therapeutic use of LEKTI is conceivable.

Published Online: 2005-06-01

Published in Print: 2002-08-27

Biochemical Features, Molecular Biology and Clinical Relevance of the Human 15-Domain Serine Proteinase Inhibitor LEKTI

Abstract

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