Research Progress on Dipeptidyl Peptidase Family : Structure, Function and Xenobiotic Metabolism
Copyright© Bentham Science Publishers; For any queries, please email at epubbenthamscience.net..
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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2022 |
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| Erschienen: |
2022 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:29 |
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| Enthalten in: |
Current medicinal chemistry - 29(2022), 12 vom: 16., Seite 2167-2188 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Qian, Xing-Kai [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 17.05.2022 Date Revised 17.05.2022 published: Print Citation Status MEDLINE |
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| doi: |
10.2174/0929867328666210915103431 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 500 | |a published: Print | ||
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| 520 | |a Copyright© Bentham Science Publishers; For any queries, please email at epubbenthamscience.net. | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
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| 650 | 4 | |a Dipeptidyl peptidase family | |
| 650 | 4 | |a FAP | |
| 650 | 4 | |a detection methods | |
| 650 | 4 | |a inhibitor | |
| 650 | 4 | |a metabolism | |
| 650 | 4 | |a prolyl carboxypeptidase | |
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| 650 | 7 | |a Xenobiotics |2 NLM | |
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| 700 | 1 | |a Li, Xiao-Dong |e verfasserin |4 aut | |
| 700 | 1 | |a Song, Pei-Fang |e verfasserin |4 aut | |
| 700 | 1 | |a Zou, Li-Wei |e verfasserin |4 aut | |
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