Molecular Cloning, Chromosomal Localization, and Expression of Murine Dipeptidyl Peptidase I
Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine protease that catalyzes the sequential removal of dipeptides from the amino termini of various protein substrates. We have isolated a cDNA coding for murine DPPI from mouse thymus and spleen cDNA libraries. The deduced amino acid sequence codes f...
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Veröffentlicht in: | The Journal of biological chemistry 1997-04, Vol.272 (16), p.10695-10703 |
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Zusammenfassung: | Dipeptidyl peptidase I (DPPI) is a lysosomal cysteine protease that catalyzes the sequential removal of dipeptides from the
amino termini of various protein substrates. We have isolated a cDNA coding for murine DPPI from mouse thymus and spleen cDNA
libraries. The deduced amino acid sequence codes for a protein of 462 amino acid residues; comparison of this deduced sequence
with that of rat and human DPPI revealed 90.1% and 77.8% identity, respectively. Using DPPI cDNA, we obtained two BAC (Bacterial
Artificial Chromosome) clones that contained the murine DPPI locus. The DPPI gene consists of seven exons and 6 introns, and
spans approximately 20 kilobases. Using fluorescence in situ chromosome hybridization, we localized murine DPPI to chromosome 7D3-E1.1. We determined that DPPI protein is widely distributed
in mouse tissues, although its relative abundance varies from tissue to tissue. In contrast to previous reports, we show here
that DPPI mRNA and protein levels and enzymatic activity are unchanged during in vitro T cell activation, implying that this enzyme is not rate-limiting for granzyme processing. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.272.16.10695 |