Title:Research Progress on Dipeptidyl Peptidase Family: Structure, Function
and Xenobiotic Metabolism
Volume: 29
Issue: 12
Author(s): Xing-Kai Qian, Jing Zhang, Xiao-Dong Li, Pei-Fang Song and Li-Wei Zou*
Affiliation:
- Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese
Medicine, Shanghai, China
Keywords:
Dipeptidyl peptidase family, metabolism, detection methods, inhibitor, prolyl carboxypeptidase, FAP.
Abstract: Prolyl-specific peptidases or proteases, including Dipeptidyl Peptidase 2, 4, 6,
8, 9, 10, Fibroblast Activation Protein, prolyl endopeptidase, and prolyl carboxypeptidase,
belong to the dipeptidyl peptidase family. In human physiology and anatomy, they have
homology amino acid sequences and similarities in the structure; however, they have distinct
functions and play different roles. Some of them also play important roles in the metabolism
of drugs containing endogenous peptides, xenobiotics containing peptides, and
exogenous peptides. The major functions of these peptidases in both the metabolism of
human health and bioactive peptides are of significant importance in the development of
effective inhibitors to control the metabolism of endogenous bioactive peptides. The
structural characteristics, distribution of tissue, endogenous substrates, and biological
functions were summarized in this review. Furthermore, the xenobiotics metabolism of
the dipeptidyl peptidase family is illustrated. All the evidence and information summarized
in this review would be very useful for researchers to extend the understanding of
the proteins of these families and offer advice and assistance in physiology and pathology
studies.
