Molecular cloning, chromosomal localization, and expression of murine Dipeptidyl peptidase I

Christine T.N. Pham, Randall J. Armstrong, Drazen B. Zimonjie, Nicholas C. Popescu, Donald G. Payan, Timothy J. Ley

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)10695-10703
Number of pages9
JournalJournal of Biological Chemistry
Volume272
Issue number16
DOIs
StatePublished - Apr 18 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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