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Submitted on July 24, 2003
Accepted on December 17, 2003
1 Endocrinology & Diabetes Unit, Department of Medicine, University of Wuerzburg, Josef-Schneider-Strasse 2, D-97080 Wuerzburg, Germany, School of Animal and Microbial Sciences, The University of Reading, Whiteknights, PO Box 228, Reading, Berkshire, RG6 6AJ, United Kingdom
* To whom correspondence should be addressed.
To further elucidate the role of proteases capable of cleaving N terminal proopiomelanocortin (N-POMC) derived peptides, we have cloned two cDNAs encoding isoforms of the airway trypsin-like protease (AT) from mouse and rat, respectively. The open reading frames comprise 417 amino acids (aa), and 279 aa. The mouse AT-gene was located at chromosome 5E1 and contains 10 exons. The longer isoform, which we designated MAT1 and RAT1, has a simple type II transmembrane protein structure, consisting of a short cytoplasmic domain, a transmembrane domain, a "SEA" module, and a serine protease domain. The human homolog of MAT1 and RAT1 is the human airway trypsin-like protease (HAT). The shorter isoform, designated MAT2 and RAT2, which contains an alternative N terminus, was formerly described in the rat as adrenal secretory serine protease (AsP) and has been shown to be involved in the processing of N-POMC derived peptides. In contrast to the long isoform, neither MAT2 and RAT2 (AsP) contain a transmembrane domain nor a "SEA" domain but a N terminal signal peptide to direct the enzyme to the secretory pathway. The C-terminus, covering the catalytic triad, is identical in both isoforms. Immunohistochemicaly, MAT/RAT was predominantly expressed in tissues of the upper gastrointestinal and the respiratory tract - but also in the adrenal gland. Moreover, isoform-specific RT-PCR and quantitative PCR analysis revealed a complex expression pattern of the two isoforms with differences between mice and rats. These findings indicate a multifunctional role of these proteases beyond adrenal proliferation.
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