| 词条 | Dipeptidyl peptidase-4 |
| 释义 |
Dipeptidyl peptidase-4 (DPP4), also known as adenosine deaminase complexing protein 2 or CD26 (cluster of differentiation 26) is a protein that, in humans, is encoded by the DPP4 gene.[1] DPP4 is related to FAP, DPP8, and DPP9. The enzyme was discovered in 1966 by Hopsu-Havu and Glenner,[2] and as a result of various studies on chemism, was called dipeptidyl peptidase IV [DP IV]. FunctionThe protein encoded by the DPP4 gene is an enzyme expressed on the surface of most cell types and is associated with immune regulation, signal transduction, and apoptosis. It is a type II transmembrane glycoprotein, but a soluble form, which lacks the intracellular and transmembrane part, is present in blood plasma and various body fluids. DPP-4 is a serine exopeptidase that cleaves X-proline or X-alanine dipeptides from the N-terminus of polypeptides. Peptide bonds involving the cyclic amino acid proline cannot be cleaved by the majority of proteases and an N-terminal X-proline "shields" various biopeptides.[3] Extracellular proline-specific proteases therefore play an important role in the regulation of these biopeptides. DPP-4 is known to cleave a broad range of substrates including growth factors, chemokines, neuropeptides, and vasoactive peptides.[4][5][6] The cleaved substrates loose their biological activity in the majority of cases, but in the case of the chemokine RANTES and neuropeptide Y, DPP-4 mediated cleavage leads to a shift in the receptor subtype binding.[4] DPP4 plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1.[7] Furthermore, it appears to work as a suppressor in the development of some tumors.[8][9][10][11] DPP-4 also binds the enzyme adenosine deaminase specifically and with high affinity. The significance of this interaction has yet to be established. Animal studiesAnimal studies suggest its pathogenetic role in development of fibrosis of various organs, such as liver and kidney.[12][13] Clinical significanceCD26/DPPIV plays an important role in tumor biology, and is useful as a marker for various cancers, with its levels either on the cell surface or in the serum increased in some neoplasms and decreased in others.[14] A class of oral hypoglycemics called dipeptidyl peptidase-4 inhibitors works by inhibiting the action of this enzyme, thereby prolonging incretin effect in vivo.[15] Middle East respiratory syndrome coronavirus has been found to bind to DPP4. It is found on the surface of cells in the airways (such as the lungs) and kidneys. Scientists may be able to use this to their advantage by blocking the virus's entry into the cell.[16]See also
References1. ^{{cite journal | vauthors = Kameoka J, Tanaka T, Nojima Y, Schlossman SF, Morimoto C | title = Direct association of adenosine deaminase with a T cell activation antigen, CD26 | journal = Science | volume = 261 | issue = 5120 | pages = 466–9 | date = July 1993 | pmid = 8101391 | doi = 10.1126/science.8101391 }} 2. ^{{cite journal | vauthors = Hopsu-Havu VK, Glenner GG | title = A new dipeptide naphthylamidase hydrolyzing glycyl-prolyl-beta-naphthylamide | journal = Histochemie. Histochemistry. Histochimie | volume = 7 | issue = 3 | pages = 197–201 | date = 1966 | pmid = 5959122 }} 3. ^{{cite journal | vauthors = Vanhoof G, Goossens F, De Meester I, Hendriks D, Scharpé S | title = Proline motifs in peptides and their biological processing | journal = FASEB Journal | volume = 9 | issue = 9 | pages = 736–44 | date = June 1995 | pmid = 7601338 }} 4. ^1 {{cite journal | vauthors = Mentlein R | title = Dipeptidyl-peptidase IV (CD26)--role in the inactivation of regulatory peptides | journal = Regulatory Peptides | volume = 85 | issue = 1 | pages = 9–24 | date = November 1999 | pmid = 10588446 }} 5. ^{{Cite journal|last=Busek|first=Petr|last2=Sedo|first2=Aleksi|date=2013-02-27|title=Dipeptidyl Peptidase-IV and Related Proteases in Brain Tumors|url=https://www.intechopen.com/books/evolution-of-the-molecular-biology-of-brain-tumors-and-the-therapeutic-implications/dipeptidyl-peptidase-iv-and-related-proteases-in-brain-tumors|journal=Evolution of the Molecular Biology of Brain Tumors and the Therapeutic Implications|language=en|volume=|pages=|doi=10.5772/53888|via=}} 6. ^{{cite journal | vauthors = Chen X | title = Biochemical properties of recombinant prolyl dipeptidases DPP-IV and DPP8 | journal = Advances in Experimental Medicine and Biology | volume = 575 | issue = | pages = 27–32 | year = 2006 | pmid = 16700505 | doi = 10.1007/0-387-32824-6_3 | isbn = 978-0-387-29058-4 | series = Advances in Experimental Medicine and Biology }} 7. ^{{cite journal | vauthors = Barnett A | title = DPP-4 inhibitors and their potential role in the management of type 2 diabetes | journal = International Journal of Clinical Practice | volume = 60 | issue = 11 | pages = 1454–70 | date = November 2006 | pmid = 17073841 | doi = 10.1111/j.1742-1241.2006.01178.x }} 8. ^{{cite journal | vauthors = Pro B, Dang NH | title = CD26/dipeptidyl peptidase IV and its role in cancer | journal = Histology and Histopathology | volume = 19 | issue = 4 | pages = 1345–51 | date = October 2004 | pmid = 15375776 | doi = 10.14670/HH-19.1345 }} 9. ^{{cite journal | vauthors = Masur K, Schwartz F, Entschladen F, Niggemann B, Zaenker KS | title = DPPIV inhibitors extend GLP-2 mediated tumour promoting effects on intestinal cancer cells | journal = Regulatory Peptides | volume = 137 | issue = 3 | pages = 147–55 | date = December 2006 | pmid = 16908079 | doi = 10.1016/j.regpep.2006.07.003 }} 10. ^{{cite journal | vauthors = Wesley UV, McGroarty M, Homoyouni A | title = Dipeptidyl peptidase inhibits malignant phenotype of prostate cancer cells by blocking basic fibroblast growth factor signaling pathway | journal = Cancer Research | volume = 65 | issue = 4 | pages = 1325–34 | date = February 2005 | pmid = 15735018 | doi = 10.1158/0008-5472.CAN-04-1852 }} 11. ^{{cite journal | vauthors = Busek P, Malík R, Sedo A | title = Dipeptidyl peptidase IV activity and/or structure homologues (DASH) and their substrates in cancer | journal = The International Journal of Biochemistry & Cell Biology | volume = 36 | issue = 3 | pages = 408–21 | date = March 2004 | pmid = 14687920 }} 12. ^{{cite journal | vauthors = Kaji K, Yoshiji H, Ikenaka Y, Noguchi R, Aihara Y, Douhara A, Moriya K, Kawaratani H, Shirai Y, Yoshii J, Yanase K, Kitade M, Namisaki T, Fukui H | title = Dipeptidyl peptidase-4 inhibitor attenuates hepatic fibrosis via suppression of activated hepatic stellate cell in rats | journal = Journal of Gastroenterology | volume = 49 | issue = 3 | pages = 481–91 | date = March 2014 | pmid = 23475323 | doi = 10.1007/s00535-013-0783-4 }} 13. ^{{cite journal | vauthors = Min HS, Kim JE, Lee MH, Song HK, Kang YS, Lee MJ, Lee JE, Kim HW, Cha JJ, Chung YY, Hyun YY, Han JY, Cha DR | title = Dipeptidyl peptidase IV inhibitor protects against renal interstitial fibrosis in a mouse model of ureteral obstruction | journal = Laboratory Investigation; A Journal of Technical Methods and Pathology | volume = 94 | issue = 6 | pages = 598–607 | date = June 2014 | pmid = 24687121 | doi = 10.1038/labinvest.2014.50 }} 14. ^{{cite journal | vauthors = Havre PA, Abe M, Urasaki Y, Ohnuma K, Morimoto C, Dang NH | title = The role of CD26/dipeptidyl peptidase IV in cancer | journal = Frontiers in Bioscience | volume = 13 | issue = 13 | pages = 1634–45 | date = January 2008 | pmid = 17981655 | doi = 10.2741/2787 | url = http://www.bioscience.org/2008/v13/af/2787/fulltext.htm }} 15. ^{{cite journal | vauthors = Rosenstock J, Zinman B | title = Dipeptidyl peptidase-4 inhibitors and the management of type 2 diabetes mellitus | journal = Current Opinion in Endocrinology, Diabetes and Obesity | volume = 14 | issue = 2 | pages = 98–107 | date = April 2007 | pmid = 17940427 | doi = 10.1097/MED.0b013e3280a02f65 }} 16. ^{{cite journal | vauthors = Raj VS, Mou H, Smits SL, Dekkers DH, Müller MA, Dijkman R, Muth D, Demmers JA, Zaki A, Fouchier RA, Thiel V, Drosten C, Rottier PJ, Osterhaus AD, Bosch BJ, Haagmans BL | title = Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC | journal = Nature | volume = 495 | issue = 7440 | pages = 251–4 | date = March 2013 | pmid = 23486063 | doi = 10.1038/nature12005 | laysummary = http://www.sciencenews.org/view/generic/id/348950/description/News_in_Brief_New_virus_uses_protein_handle_to_infect_cells | laysource = ScienceNews | publisher = ScienceNews }} Further reading{{refbegin | 2}}
External links
2 : EC 3.4.14|Peptidase |
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