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  • Title: The 15-domain serine proteinase inhibitor LEKTI: biochemical properties, genomic organization, and pathophysiological role.
    Author: Mägert HJ, Kreutzmann P, Drögemüller K, Ständker L, Adermann K, Walden M, John H, Korting HC, Forssmann WG.
    Journal: Eur J Med Res; 2002 Feb 21; 7(2):49-56. PubMed ID: 11891144.
    Abstract:
    Proteinases are involved in specific and non-specific proteolytic reactions, and participate in many pathophysiological processes. Normally, they are regulated by endogenously produced proteinase inhibitors which, thus, represent lead structures for the development of therapeutics. We succeeded in partially isolating and cloning a novel human serine proteinase inhibitor which, according to its structure and the expression pattern of the corresponding gene, was termed lympho-epithelial Kazal-type-related inhibitor (LEKTI). This inhibitor is of special interest because it exhibits an extraordinarily large number of 15 potentially inhibitory domains and is of pathophysiological importance for the severe congenital disease Netherton syndrome. Here, we review the as yet known data on protein structure, biochemical properties, genomic organization and gene expression. Furthermore, the relevance of LEKTI for several disorders pointing out its possible future therapeutic value, is discussed.
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