Premium
Identification of a dipeptidyl peptidase from Trypanosoma brucei
Author(s) -
GIRARD D.,
BASTOS I. M. D.,
GRELLIER P.
Publication year - 2005
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.2005.05202003_3_18.x
Subject(s) - dipeptidyl peptidase , biology , trypanosoma brucei , oligopeptidase , biochemistry , serine protease , peptide , dipeptidyl peptidase 4 , microbiology and biotechnology , enzyme , protease , gene , diabetes mellitus , type 2 diabetes , endocrinology
Dipeptidyl peptidases (DPP) are ubiquitous enzymes. Several DPPs have been described and the most known among them is dipeptidyl peptidase IV, a type II multifunctional cell surface protein that belong to the prolyl oligopeptidase family of serine proteases. DPP IV specifically cleaves dipeptides from the N‐terminus of peptides with a Pro, Hyp or Ala in the penultimate position. DPP IV substrates include certain chemokines, growth factors (e.g. growth hormone, growth hormone‐releasing factor, glucagon‐like peptides 1 and 2) and neuro‐ and vasoactive peptides including neuropeptide Y, peptide YY and substance P. In this work, we present the identification of a dipeptidyl peptidase from Trypanosoma brucei (DPPTb). Its gene was isolated by PCR using primers designed from T. brucei ESTs sequences that matched with human DPP IV. However, the cloned and sequenced insert obtained displays similarity mainly with human DPP8 and DPP9. Active recombinant DPP Tb was expressed in insect cells using the baculovirus system. We observed by immunofluorescence, using anti‐DPPTb antibodies, that native DPPTb is localized in vesicles in the cytoplasm from procyclic forms of T. brucei .