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Biochim Biophys Acta. 2001 Mar 19;1518(1-2):204-9.

Cloning and expression of novel mosaic serine proteases with and without a transmembrane domain from human lung.

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  • 1Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, 770-8503, Tokushima, Japan.


Two cDNAs encoding novel mosaic proteins with a serine protease domain and potential regulatory modules, consisting of a protein kinase substrate and a low-density lipoprotein receptor, were cloned from a human lung cDNA library by PCR. One with a transmembrane domain (MSPL) and the other without one (MSPS) comprise 581 and 537 amino acids, respectively. Except for the C-terminal ends, the two isoforms had an identical serine protease domain exhibiting 42, 39 and 43% identity with those of plasma kallikrein, hepsin and transmembrane protease serine 2, respectively. Both genes were predominantly expressed in human lung, placenta, pancreas and prostate.

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