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J Biol Chem, Vol. 274, Issue 31, 21499-21502, July 30, 1999
From the Lower Saxony Institute for Peptide Research,
Feodor-Lynen-Strasse 31, D-30 625 Hannover, Germany the
¶ Department of Anatomy, University of Zürich,
Wintherthurerstrasse 190, CH-8057 Zürich, Switzerland, and the
§ Department of Clinical Chemistry and Clinical
Biochemistry, Klinikum Innenstadt,
Ludwig-Maximilians-Universität, Nu Proteinase inhibitors are important negative
regulators of proteinase action in vivo. We have succeeded
in isolating two previously unknown polypeptides (HF6478 and HF7665)
from human blood filtrate that are parts of a larger precursor protein
containing two typical Kazal-type serine proteinase inhibitor motifs.
The entire precursor protein, as deduced from the nucleotide sequence
of the cloned cDNA, exhibits 15 potential inhibitory domains,
including the Kazal-type domains, HF6478, HF7665, and 11 additional
similar domains. An inhibitory effect of HF7665 on trypsin activity is demonstrated. Because all of the 13 HF6478- and HF7665-related domains
share partial homology to the typical Kazal-type domain but lack one of
the three conserved disulfide bonds, they may represent a novel type of
serine proteinase inhibitor. The gene encoding the
multidomain proteinase inhibitor, which we have termed LEKTI, was localized on human chromosome 5q31-32. As shown by reverse transcriptase-polymerase chain reaction and Northern blot analysis, it is expressed in the thymus, vaginal epithelium,
Bartholin's glands, oral mucosa, tonsils, and the parathyroid glands.
From these results, we assume that LEKTI may play a role in
anti-inflammatory and/or antimicrobial protection of mucous epithelia.
baumstrasse 20, D-80 336 Munich, Germany
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