期刊
CURRENT MEDICINAL CHEMISTRY
卷 29, 期 12, 页码 2167-2188出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/0929867328666210915103431
关键词
Dipeptidyl peptidase family; metabolism; detection methods; inhibitor; prolyl carboxypeptidase; FAP
资金
- NSF of China [82073813, 81973393]
- National Science and Technology Major Project of China [2018ZX 09731016]
- National Key Research and Development Program of China [2017YFC1702000]
This article summarizes the structural characteristics, functions, and metabolism of the prolyl-specific peptidases or proteases family, as well as their importance in human physiology and drug metabolism.
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.
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