関: CD26 antigen

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/11/08 17:10:19」(JST)

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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]

Function

The protein encoded by the DPP4 gene is an antigenic enzyme expressed on the surface of most cell types and is associated with immune regulation, signal transduction and apoptosis. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides.

It is a rather indiscriminate enzyme for which a diverse range of substrates are known.^[2] The substrates of CD26/DPPIV are proline(or alanine)-containing peptides and include growth factors, chemokines, neuropeptides, and vasoactive peptides.

DPP4 is related to attractin, FAP, DPP8 and DPP9.

DPP4 plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1.^[3]

Furthermore, it appears to work as a suppressor in the development of cancer and tumours.^[4]^[5]^[6]

CD26/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.^[7]

DPP-4 also binds the enzyme adenosine deaminase specifically and with high affinity. The significance of this interaction has yet to be established.

Animal studies suggest its pathogenetic role in development of fibrosis of various organs, such as liver and kidney.^[8]^[9]

Clinical significance

A new class of oral hypoglycemics called dipeptidyl peptidase-4 inhibitors work by inhibiting the action of this enzyme, thereby prolonging incretin effect in vivo.^[10]

A new coronavirus related to SARS, named Middle East respiratory syndrome coronavirus, has been found to bind to DPP4. DPP4 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.^[11]

References

^ Kameoka J, Tanaka T, Nojima Y, Schlossman SF, Morimoto C (July 1993). "Direct association of adenosine deaminase with a T cell activation antigen, CD26". Science 261 (5120): 466–9. doi:10.1126/science.8101391. PMID 8101391.
^ Chen X (2006). "Biochemical properties of recombinant prolyl dipeptidases DPP-IV and DPP8". Adv. Exp. Med. Biol. Advances in Experimental Medicine and Biology 575: 27–32. doi:10.1007/0-387-32824-6_3. ISBN 978-0-387-29058-4. PMID 16700505.
^ Barnett A (November 2006). "DPP-4 inhibitors and their potential role in the management of type 2 diabetes". Int. J. Clin. Pract. 60 (11): 1454–70. doi:10.1111/j.1742-1241.2006.01178.x. PMID 17073841.
^ Pro B, Dang NH (2004). "CD26/dipeptidyl peptidase IV and its role in cancer". Histol Histopathol 19 (4): 1345–51. PMID 15375776.
^ Masur K, Schwartz F, Entschladen F, Niggemann B, Zaenker KS (2006). "DPPIV inhibitors extend GLP-2 mediated tumour promoting effects on intestinal cancer cells". Regul Pept. 137 (3): 147–55. doi:10.1016/j.regpep.2006.07.003. PMID 16908079.
^ Wesley UV, McGroarty M, Homoyouni A (2005). "Dipeptidyl peptidase inhibits malignant phenotype of prostate cancer cells by blocking basic fibroblast growth factor signaling pathway". Cancer Res. 65 (4): 1325–34. doi:10.1158/0008-5472.CAN-04-1852. PMID 15735018.
^ Havre PA, Abe M, Urasaki Y, Ohnuma K, Morimoto C, Dang NH (2008). "The role of CD26/dipeptidyl peptidase IV in cancer". Front. Biosci. 13 (13): 1634–45. doi:10.2741/2787. PMID 17981655.
^ 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 (2014). "Dipeptidyl peptidase-4 inhibitor attenuates hepatic fibrosis via suppression of activated hepatic stellate cell in rats". J. Gastroenterol. 49 (3): 481–91. doi:10.1007/s00535-013-0783-4. PMID 23475323.
^ 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 (2014). "Dipeptidyl peptidase IV inhibitor protects against renal interstitial fibrosis in a mouse model of ureteral obstruction". Lab. Invest. 94 (6): 598–607. doi:10.1038/labinvest.2014.50. PMID 24687121.
^ Rosenstock J, Zinman B (April 2007). "Dipeptidyl peptidase-4 inhibitors and the management of type 2 diabetes mellitus". Current Opinion in Endocrinology, Diabetes and Obesity 14 (2): 98–107. doi:10.1097/MED.0b013e3280a02f65. PMID 17940427.
^ 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 (March 2013). "Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC". Nature (ScienceNews) 495 (7440): 251–4. doi:10.1038/nature12005. PMID 23486063. Lay summary – ScienceNews.

External links

The MEROPS online database for peptidases and their inhibitors: S09.003
Dipeptidyl-Peptidase IV at the US National Library of Medicine Medical Subject Headings (MeSH)
Banting and Best Diabetes Centre at UT dpp4

UpToDate Contents

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1. 2型糖尿病のGlucagon-like peptide-1をベースとした治療 glucagon like peptide 1 based therapies for the treatment of type 2 diabetes mellitus
2. 透析前慢性腎臓病または末期腎不全を伴う2型糖尿病患者における高血糖のマネージメント management of hyperglycemia in patients with type 2 diabetes and pre dialysis chronic kidney disease or end stage renal disease
3. ACE 阻害薬誘発性血管浮腫 ace inhibitor induced angioedema
4. 高齢患者における2型糖尿病の治療 treatment of type 2 diabetes mellitus in the older patient
5. 成人の2型糖尿病治療におけるメトホルミン metformin in the treatment of adults with type 2 diabetes mellitus

English Journal

Proportion of patients at HbA1c target <7% with eight classes of antidiabetic drugs in type 2 diabetes: systematic review of 218 randomized controlled trials with 78 945 patients.

Esposito K, Chiodini P, Bellastella G, Maiorino MI, Giugliano D.SourceDepartment of Cardio-Thoracic and Respiratory Sciences, Second University of Naples, Naples, Italy Department of Medicine and Public Health, Second University of Naples, Naples, Italy Department of Geriatrics and Metabolic Diseases, Second University of Naples, Naples, Italy.
Diabetes, obesity & metabolism.Diabetes Obes Metab.2012 Mar;14(3):228-33. doi: 10.1111/j.1463-1326.2011.01512.x. Epub 2011 Nov 3.
Aim: We assessed the efficacy of eight classes of diabetes medications used in current clinical practice [metformin, sulphonylureas, α-glucosidase inhibitors, thiazolidinediones, glinides, dipeptidyl peptidase-4 inhibitors, glucagon-like peptide-1 (GLP-1) analogues and insulin analogues] to reach t
PMID 21958121

Do antidiabetic medications play a specific role in differentiated thyroid cancer compared to other cancer types?

Fröhlich E, Wahl R.SourceInternal Medicine, Department of Endocrinology, Metabolism, Nephrology, Angiology and Clinical Chemistry, University of Tuebingen, Tuebingen, Germany Center for Medical Research, Medical University Graz, Graz, Austria.
Diabetes, obesity & metabolism.Diabetes Obes Metab.2012 Mar;14(3):204-13. doi: 10.1111/j.1463-1326.2011.01491.x. Epub 2011 Nov 21.
The risk for differentiated thyroid cancer, like for many other types of cancer, is increased in obese individuals and people with intermediate hyperglycaemia. The incidence of all cancers, with the exception of thyroid cancer, is also increased in type 2 diabetes mellitus patients. The review compa
PMID 21883805

Dipeptidyl peptidase-4 (DPP-4) inhibitors are favourable to Glucagon-Like Peptide-1 (GLP-1) agonists: No.

Madsbad S.AbstractIncretin-based therapies, which include the GLP-1 receptor agonists and DPP-4 inhibitors, use the antidiabetic properties of potentiating the GLP-1 receptor signalling via the regulation of insulin and glucagon secretion, inhibition of gastric emptying and suppression of appetite. Most physicians will start antidiabetic treatment with metformin, but adding a GLP-1 receptor agonist as the second drug seems to be optimal since more patients will reach an HbA1c below 7% than with a DPP-4 inhibitor or another oral antidiabetic agents and with minimal risk of hypoglycaemia. The GLP-1 receptor agonists are also more effective in weight and systolic blood pressure control than DPP-4 inhibitors. The side effects of the GLP-1 receptor agonists are primarily nausea and vomiting, which is less pronounced with the long acting agonists and often transient. A GLP-1 receptor agonist can be recommended before a DPP-4 inhibitor in obese type 2 diabetic patients, who want to lose weight. Furthermore, the GLP-1 receptor agonists cover the whole spectrum of treatment from time of diagnosis with lifestyle treatment to combination treatment with basal insulin.
European journal of internal medicine.Eur J Intern Med.2012 Mar;23(2):132-6. Epub 2011 Nov 29.
Incretin-based therapies, which include the GLP-1 receptor agonists and DPP-4 inhibitors, use the antidiabetic properties of potentiating the GLP-1 receptor signalling via the regulation of insulin and glucagon secretion, inhibition of gastric emptying and suppression of appetite. Most physicians wi
PMID 22284242

Japanese Journal

Identification and characterization of a novel fermented substance produced by edible Aspergillus oryzae AO-1 that inhibits DPP-IV activity(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)

Imamura Kazuhiko,Tsuyama Yoshihito,Hirata Terukage
Journal of bioscience and bioengineering 111(1), 37-40, 2011-01
… We identified a novel fermented substance (FKA) produced by the edible Aspergillus oryzae strain AO-1 that inhibited dipeptidyl peptidase IV (DPP-IV) (IC_<50>=3.41mg・mL^<-1>). … HPLC analysis of FKA showed specific one metabolite (WYK-1), which inhibited DPP-IV (IC_<50>=6.98μM). … This is the first report that an edible A.oryzae strain produces a DPP-IV inhibitor such as WYK-1. …
NAID 110008440346

Proteomic Analysis of Two Types of Exosomes in Human Whole Saliva

Ogawa Yuko,Miura Yuri,Harazono Akira,Kanai-Azuma Masami,Akimoto Yoshihiro,Kawakami Hayato,Yamaguchi Teruhide,Toda Tosifusa,Endo Tamao,Tsubuki Masayoshi,Yanoshita Ryohei
Biological & Pharmaceutical Bulletin 34(1), 13-23, 2011
… Most of dipeptidyl peptidase IV known as CD26 in whole saliva, was present on the exosome II and metabolically active in cleaving chemokines (CXCL11 and CXCL12). …
NAID 130000402256

The expression of dipeptidyl peptidase IV (DPPIV/CD26) is associated with enhanced chemosensitivity to paclitaxel in epithelial ovarian carcinoma cells

KAJIYAMA Hiroaki,SHIBATA Kiyosumi,INO Kazuhiko,MIZUTANI Shigehiko,NAWA Akihiro,KIKKAWA Fumitaka
Cancer science 101(2), 347-354, 2010-02-10
NAID 10026587626

Related Pictures

★リンクテーブル★

リンク元	「ジペプチジルペプチダーゼIV」「CD26 antigen」
拡張検索	「dipeptidyl-peptidase IV inhibitor」
関連記事	「I」「peptidase」「dipeptidyl peptidase」「IV」

「ジペプチジルペプチダーゼIV」

Dipeptidyl-peptidase 4
	; Ribbon diagram of human DPP-4.; From PDB 1PFQ.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1J2E, 1N1M, 1NU6, 1NU8, 1PFQ, 1R9M, 1R9N, 1RWQ, 1TK3, 1TKR, 1U8E, 1W1I, 1WCY, 1X70, 2AJL, 2BGN, 2BGR, 2BUB, 2FJP, 2G5P, 2G5T, 2G63, 2HHA, 2I03, 2I78, 2IIT, 2IIV, 2JID, 2OAG, 2OGZ, 2OLE, 2ONC, 2OPH, 2OQI, 2OQV, 2P8S, 2QJR, 2QKY, 2QOE, 2QT9, 2QTB, 2RGU, 2RIP, 3BJM, 3C43, 3C45, 3CCB, 3CCC, 3D4L, 3EIO, 3F8S, 3G0B, 3G0C, 3G0D, 3G0G, 3H0C, 3HAB, 3HAC, 3KWF, 3KWJ, 3NOX, 3O95, 3O9V, 3OC0, 3OPM, 3Q0T, 3Q8W, 3QBJ, 3SWW, 3SX4, 3VJK, 3VJL, 3VJM, 3W2T, 4A5S, 4DSA, 4DSZ, 4DTC, 4G1F, 4J3J, 4JH0, 4KR0, 4L72, 4LKO, 4N8D, 4N8E, 4PNZ
Identifiers
Symbols	DPP4 ; ADABP; ADCP2; CD26; DPPIV; TP103
External IDs	OMIM: 102720 MGI: 94919 HomoloGene: 3279 ChEMBL: 284 GeneCards: DPP4 Gene
EC number	3.4.14.5
Gene ontology
Molecular function	• protease binding; • serine-type endopeptidase activity; • receptor binding; • protein binding; • serine-type peptidase activity; • dipeptidyl-peptidase activity; • identical protein binding; • protein homodimerization activity;
Cellular component	• lysosomal membrane; • plasma membrane; • cell surface; • membrane; • integral component of membrane; • apical plasma membrane; • lamellipodium; • endocytic vesicle; • lamellipodium membrane; • membrane raft; • intercellular canaliculus; • extracellular vesicular exosome; • invadopodium membrane;
Biological process	• response to hypoxia; • proteolysis; • cell adhesion; • positive regulation of cell proliferation; • negative regulation of extracellular matrix disassembly; • T cell costimulation; • regulation of cell-cell adhesion mediated by integrin; • T cell activation; • endothelial cell migration;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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