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|Title:||Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DDP) IV homolog, DPP8|
|Citation:||FEBS Journal, 2000; 267(20):6140-6150|
|Publisher:||Blackwell Science Ltd|
|Abstract:||Dipeptidyl peptidase (DPP) IV has roles in T-cell costimulation, chemokine biology, type-II diabetes and tumor biology. Fibroblast activation protein (FAP) has been implicated in tumor growth and cirrhosis. Here we describe DPP8, a novel human postproline dipeptidyl aminopeptidase that is homologous to DPPIV and FAP. Northern-blot hybridization showed that the tissue expression of DPP8 mRNA is ubiquitous, similar to that of DPPIV. The DPP8 gene was localized to chromosome 15q22, distinct from a closely related gene at 19p13.3 which we named DPP9. The full-length DPP8 cDNA codes for an 882-amino-acid protein that has about 27% identity and 51% similarity to DPPIV and FAP, but no transmembrane domain and no N-linked or O-linked glycosylation. Western blots and confocal microscopy of transfected COS-7 cells showed DPP8 to be a 100-kDa monomeric protein expressed in the cytoplasm. Purified recombinant DPP8 hydrolyzed the DPPIV substrates Ala-Pro, Arg-Pro and Gly-Pro. Thus recombinant DPP8 shares a postproline dipeptidyl aminopeptidase activity with DPPIV and FAP. DPP8 enzyme activity had a neutral pH optimum consistent with it being nonlysosomal. The similarities between DPP8 and DPPIV in tissue expression pattern and substrates suggests a potential role for DPP8 in T-cell activation and immune function.|
|Keywords:||Lymphocytes; Monocytes; Cell Line; Chromosomes, Human, Pair 15; Chromosomes, Human, Pair 19; Humans; Gelatinases; Serine Endopeptidases; Growth Substances; Membrane Proteins; Recombinant Proteins; Antigens, Neoplasm; Chromosome Mapping; Cloning, Molecular; Sequence Alignment; Amino Acid Sequence; Sequence Homology, Amino Acid; Molecular Sequence Data; Dipeptidyl Peptidase 4; Biomarkers, Tumor|
|Appears in Collections:||Paediatrics publications|
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