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Dipeptidyl peptidase-4

April 27, 2024

Dipeptidyl peptidase-4 (DPP4 or DPPIV), 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.[5] DPP4 is related to FAP, DPP8, and DPP9. The enzyme was discovered in 1966 by Hopsu-Havu and Glenner,[6] and as a result of various studies on chemism, was called dipeptidyl peptidase IV [DP IV].

DPP4
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDPP4, ADABP, ADCP2, CD26, DPPIV, TP103, dipeptidyl peptidase 4
External IDsOMIM: 102720 MGI: 94919 HomoloGene: 3279 GeneCards: DPP4
Orthologs
SpeciesHumanMouse
Entrez

1803

13482

Ensembl

ENSG00000197635

ENSMUSG00000035000

UniProt

P27487

P28843

RefSeq (mRNA)

NM_001935

NM_001159543
NM_010074

RefSeq (protein)

NP_001926
NP_001366533
NP_001366534
NP_001366535

NP_001153015
NP_034204

Location (UCSC)Chr 2: 161.99 – 162.07 MbChr 2: 62.16 – 62.24 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function edit

The 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.[7] 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.[8][9] The cleaved substrates lose 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.[8]

DPP4 plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1.[10] Furthermore, it appears to work as a suppressor in the development of some tumors.[11][12][13][14]

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 edit

Animal studies suggest its pathogenetic role in development of fibrosis of various organs, such as liver and kidney.[15][16]

Clinical significance edit

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.[17]

A class of oral hypoglycemics called dipeptidyl peptidase-4 inhibitors works by inhibiting the action of this enzyme, thereby prolonging incretin effect in vivo.[18]

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.[19]

DPP4,[20] or its Mycobacterial homologue MtDPP,[21] might play a role in the pathogenesis of tuberculosis via cleavage of the chemokine C-X-C motif chemokine ligand 10 (CXCL10).

See also edit

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000197635 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035000 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. Bibcode:1993Sci...261..466K. doi:10.1126/science.8101391. PMID 8101391.
  6. ^ Hopsu-Havu VK, Glenner GG (1966). "A new dipeptide naphthylamidase hydrolyzing glycyl-prolyl-beta-naphthylamide". Histochemie. Histochemistry. Histochimie. 7 (3): 197–201. doi:10.1007/bf00577838. PMID 5959122. S2CID 9674831.
  7. ^ Vanhoof G, Goossens F, De Meester I, Hendriks D, Scharpé S (June 1995). "Proline motifs in peptides and their biological processing". FASEB Journal. 9 (9): 736–44. doi:10.1096/fasebj.9.9.7601338. PMID 7601338. S2CID 37551773.
  8. ^ a b Mentlein R (November 1999). "Dipeptidyl-peptidase IV (CD26)--role in the inactivation of regulatory peptides". Regulatory Peptides. 85 (1): 9–24. doi:10.1016/S0167-0115(99)00089-0. PMID 10588446. S2CID 22354304.
  9. ^ Chen X (2006). "Biochemical properties of recombinant prolyl dipeptidases DPP-IV and DPP8". Dipeptidyl Aminopeptidases. Advances in Experimental Medicine and Biology. Vol. 575. pp. 27–32. doi:10.1007/0-387-32824-6_3. ISBN 978-0-387-29058-4. PMID 16700505.
  10. ^ Barnett A (November 2006). "DPP-4 inhibitors and their potential role in the management of type 2 diabetes". International Journal of Clinical Practice. 60 (11): 1454–70. doi:10.1111/j.1742-1241.2006.01178.x. PMID 17073841. S2CID 2645092.
  11. ^ Pro B, Dang NH (October 2004). "CD26/dipeptidyl peptidase IV and its role in cancer". Histology and Histopathology. 19 (4): 1345–51. doi:10.14670/HH-19.1345. PMID 15375776.
  12. ^ Masur K, Schwartz F, Entschladen F, Niggemann B, Zaenker KS (December 2006). "DPPIV inhibitors extend GLP-2 mediated tumour promoting effects on intestinal cancer cells". Regulatory Peptides. 137 (3): 147–55. doi:10.1016/j.regpep.2006.07.003. PMID 16908079. S2CID 2857735.
  13. ^ Wesley UV, McGroarty M, Homoyouni A (February 2005). "Dipeptidyl peptidase inhibits malignant phenotype of prostate cancer cells by blocking basic fibroblast growth factor signaling pathway". Cancer Research. 65 (4): 1325–34. doi:10.1158/0008-5472.CAN-04-1852. PMID 15735018.
  14. ^ Busek P, Malík R, Sedo A (March 2004). "Dipeptidyl peptidase IV activity and/or structure homologues (DASH) and their substrates in cancer". The International Journal of Biochemistry & Cell Biology. 36 (3): 408–21. doi:10.1016/S1357-2725(03)00262-0. PMID 14687920.
  15. ^ 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 (March 2014). "Dipeptidyl peptidase-4 inhibitor attenuates hepatic fibrosis via suppression of activated hepatic stellate cell in rats". Journal of Gastroenterology. 49 (3): 481–91. doi:10.1007/s00535-013-0783-4. PMID 23475323. S2CID 2726091.
  16. ^ 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 (June 2014). "Dipeptidyl peptidase IV inhibitor protects against renal interstitial fibrosis in a mouse model of ureteral obstruction". Laboratory Investigation; A Journal of Technical Methods and Pathology. 94 (6): 598–607. doi:10.1038/labinvest.2014.50. PMID 24687121. S2CID 23745972.
  17. ^ Havre PA, Abe M, Urasaki Y, Ohnuma K, Morimoto C, Dang NH (January 2008). "The role of CD26/dipeptidyl peptidase IV in cancer". Frontiers in Bioscience. 13 (13): 1634–45. doi:10.2741/2787. PMID 17981655.
  18. ^ 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. S2CID 25482131.
  19. ^ 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. 495 (7440): 251–4. Bibcode:2013Natur.495..251R. doi:10.1038/nature12005. PMC 7095326. PMID 23486063.
    • Tina Hesman Saey (March 13, 2013). . ScienceNews. Archived from the original on 2013-03-20.
  20. ^ Blauenfeldt T, Petrone L, Del Nonno F, Baiocchini A, Falasca L, Chiacchio T, Bondet V, Vanini V, Palmieri F, Galluccio G, Casrouge A, Eugen-Olsen J, Albert ML, Goletti D, Duffy D, Ruhwald M (Jul 2018). "Interplay of DDP4 and IP-10 as a Potential Mechanism for Cell Recruitment to Tuberculosis Lesions". Front Immunol. 9 (1456): 1456. doi:10.3389/fimmu.2018.01456. PMC 6041415. PMID 30026741.
  21. ^ Lioe TS, Xie Z, Wu J, Li W, Sun L, Feng Q, Raju S, Tefsen B, Ruiz-Carrillo D (Jan 2023). "The Mycobacterium tuberculosis prolyl dipeptidyl peptidase cleaves the N-terminal peptide of the immunoprotein CXCL-10". Biol Chem. 404 (6): 633–43. doi:10.1515/hsz-2022-0265. PMID 36632703. S2CID 255596512.

Further reading edit

  • Ansorge S, Bühling F, Kähne T, Lendeckel U, Reinhold D, Täger M, Wrenger S (1997). "CD26/Dipeptidyl Peptidase IV in Lymphocyte Growth Regulation". Cellular Peptidases in Immune Functions and Diseases. Advances in Experimental Medicine and Biology. Vol. 421. pp. 127–40. doi:10.1007/978-1-4757-9613-1_17. ISBN 978-1-4757-9615-5. PMID 9330689.
  • Reinhold D, Kähne T, Steinbrecher A, Wrenger S, Neubert K, Ansorge S, Brocke S (2003). "The role of dipeptidyl peptidase IV (DP IV) enzymatic activity in T cell activation and autoimmunity". Biological Chemistry. 383 (7–8): 1133–8. doi:10.1515/BC.2002.123. PMID 12437097. S2CID 30027839.
  • Sato K, Dang NH (March 2003). "CD26: a novel treatment target for T-cell lymphoid malignancies? (Review)". International Journal of Oncology. 22 (3): 481–97. doi:10.3892/ijo.22.3.481 (inactive 31 January 2024). PMID 12579300.{{cite journal}}: CS1 maint: DOI inactive as of January 2024 (link)
  • de Meester I, Lambeir AM, Proost P, Scharpé S (2003). "Dipeptidyl Peptidase IV Substrates". Dipeptidyl Aminopeptidases in Health and Disease. Advances in Experimental Medicine and Biology. Vol. 524. pp. 3–17. doi:10.1007/0-306-47920-6_1. ISBN 0-306-47717-3. PMID 12675218.
  • Koch S, Anthonsen D, Skovbjerg H, Sjöström H (2003). "On the role of dipeptidyl peptidase IV in the digestion of an immunodominant epitope in celiac disease". Dipeptidyl Aminopeptidases in Health and Disease. Advances in Experimental Medicine and Biology. Vol. 524. pp. 181–7. doi:10.1007/0-306-47920-6_22. ISBN 0-306-47717-3. PMID 12675238.
  • Pro B, Dang NH (October 2004). "CD26/dipeptidyl peptidase IV and its role in cancer". Histology and Histopathology. 19 (4): 1345–51. doi:10.14670/HH-19.1345. PMID 15375776.

External links edit

April 27, 2024
dipeptidyl, peptidase, dpp4, dppiv, also, known, adenosine, deaminase, complexing, protein, cd26, cluster, differentiation, protein, that, humans, encoded, dpp4, gene, dpp4, related, dpp8, dpp9, enzyme, discovered, 1966, hopsu, havu, glenner, result, various, . Dipeptidyl peptidase 4 DPP4 or DPPIV 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 5 DPP4 is related to FAP DPP8 and DPP9 The enzyme was discovered in 1966 by Hopsu Havu and Glenner 6 and as a result of various studies on chemism was called dipeptidyl peptidase IV DP IV DPP4Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1J2E 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 4JH0 4KR0 4L72 4LKO 4J3J 4N8D 4N8E 4PNZ 4PV7 4QZV 3WQH 5KBY 5ISM 5I7UIdentifiersAliasesDPP4 ADABP ADCP2 CD26 DPPIV TP103 dipeptidyl peptidase 4External IDsOMIM 102720 MGI 94919 HomoloGene 3279 GeneCards DPP4Gene location Human Chr Chromosome 2 human 1 Band2q24 2Start161 992 245 bp 1 End162 074 215 bp 1 Gene location Mouse Chr Chromosome 2 mouse 2 Band2 C1 3 2 35 85 cMStart62 160 417 bp 2 End62 242 575 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inAchilles tendonjejunal mucosaparotid glandduodenumkidney tubuleplacentastromal cell of endometriumparietal pleuraseminal vesiculaglomerulusTop expressed injejunumseminal vesiculasacculeileumlacrimal glandparotid glandleft lobe of liverrenal corpuscleintestinal epitheliumintestinal villusMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functiondipeptidyl peptidase activity signaling receptor binding identical protein binding peptidase activity hydrolase activity virus receptor activity protein homodimerization activity serine type peptidase activity protease binding aminopeptidase activity protein binding serine type endopeptidase activityCellular componentlamellipodium membrane extracellular exosome lysosomal membrane endocytic vesicle integral component of membrane cell projection cell junction lamellipodium apical plasma membrane membrane focal adhesion cell surface intercellular canaliculus membrane raft extracellular region plasma membraneBiological processresponse to hypoxia T cell costimulation psychomotor behavior behavioral fear response negative regulation of extracellular matrix disassembly regulation of cell cell adhesion mediated by integrin locomotory exploration behavior endothelial cell migration positive regulation of cell population proliferation T cell activation cell adhesion viral entry into host cell regulation of insulin secretion proteolysisSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez180313482EnsemblENSG00000197635ENSMUSG00000035000UniProtP27487P28843RefSeq mRNA NM 001935NM 001159543NM 010074RefSeq protein NP 001926NP 001366533NP 001366534NP 001366535NP 001153015NP 034204Location UCSC Chr 2 161 99 162 07 MbChr 2 62 16 62 24 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Animal studies 3 Clinical significance 4 See also 5 References 6 Further reading 7 External linksFunction editThe 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 7 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 8 9 The cleaved substrates lose 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 8 DPP4 plays a major role in glucose metabolism It is responsible for the degradation of incretins such as GLP 1 10 Furthermore it appears to work as a suppressor in the development of some tumors 11 12 13 14 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 editAnimal studies suggest its pathogenetic role in development of fibrosis of various organs such as liver and kidney 15 16 Clinical significance editCD26 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 17 A class of oral hypoglycemics called dipeptidyl peptidase 4 inhibitors works by inhibiting the action of this enzyme thereby prolonging incretin effect in vivo 18 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 19 DPP4 20 or its Mycobacterial homologue MtDPP 21 might play a role in the pathogenesis of tuberculosis via cleavage of the chemokine C X C motif chemokine ligand 10 CXCL10 See also editDevelopment of dipeptidyl peptidase 4 inhibitors BerberineReferences edit a b c GRCh38 Ensembl release 89 ENSG00000197635 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000035000 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine 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 Bibcode 1993Sci 261 466K doi 10 1126 science 8101391 PMID 8101391 Hopsu Havu VK Glenner GG 1966 A new dipeptide naphthylamidase hydrolyzing glycyl prolyl beta naphthylamide Histochemie Histochemistry Histochimie 7 3 197 201 doi 10 1007 bf00577838 PMID 5959122 S2CID 9674831 Vanhoof G Goossens F De Meester I Hendriks D Scharpe S June 1995 Proline motifs in peptides and their biological processing FASEB Journal 9 9 736 44 doi 10 1096 fasebj 9 9 7601338 PMID 7601338 S2CID 37551773 a b Mentlein R November 1999 Dipeptidyl peptidase IV CD26 role in the inactivation of regulatory peptides Regulatory Peptides 85 1 9 24 doi 10 1016 S0167 0115 99 00089 0 PMID 10588446 S2CID 22354304 Chen X 2006 Biochemical properties of recombinant prolyl dipeptidases DPP IV and DPP8 Dipeptidyl Aminopeptidases Advances in Experimental Medicine and Biology Vol 575 pp 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 International Journal of Clinical Practice 60 11 1454 70 doi 10 1111 j 1742 1241 2006 01178 x PMID 17073841 S2CID 2645092 Pro B Dang NH October 2004 CD26 dipeptidyl peptidase IV and its role in cancer Histology and Histopathology 19 4 1345 51 doi 10 14670 HH 19 1345 PMID 15375776 Masur K Schwartz F Entschladen F Niggemann B Zaenker KS December 2006 DPPIV inhibitors extend GLP 2 mediated tumour promoting effects on intestinal cancer cells Regulatory Peptides 137 3 147 55 doi 10 1016 j regpep 2006 07 003 PMID 16908079 S2CID 2857735 Wesley UV McGroarty M Homoyouni A February 2005 Dipeptidyl peptidase inhibits malignant phenotype of prostate cancer cells by blocking basic fibroblast growth factor signaling pathway Cancer Research 65 4 1325 34 doi 10 1158 0008 5472 CAN 04 1852 PMID 15735018 Busek P Malik R Sedo A March 2004 Dipeptidyl peptidase IV activity and or structure homologues DASH and their substrates in cancer The International Journal of Biochemistry amp Cell Biology 36 3 408 21 doi 10 1016 S1357 2725 03 00262 0 PMID 14687920 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 March 2014 Dipeptidyl peptidase 4 inhibitor attenuates hepatic fibrosis via suppression of activated hepatic stellate cell in rats Journal of Gastroenterology 49 3 481 91 doi 10 1007 s00535 013 0783 4 PMID 23475323 S2CID 2726091 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 June 2014 Dipeptidyl peptidase IV inhibitor protects against renal interstitial fibrosis in a mouse model of ureteral obstruction Laboratory Investigation A Journal of Technical Methods and Pathology 94 6 598 607 doi 10 1038 labinvest 2014 50 PMID 24687121 S2CID 23745972 Havre PA Abe M Urasaki Y Ohnuma K Morimoto C Dang NH January 2008 The role of CD26 dipeptidyl peptidase IV in cancer Frontiers in Bioscience 13 13 1634 45 doi 10 2741 2787 PMID 17981655 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 S2CID 25482131 Raj VS Mou H Smits SL Dekkers DH Muller 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 495 7440 251 4 Bibcode 2013Natur 495 251R doi 10 1038 nature12005 PMC 7095326 PMID 23486063 Tina Hesman Saey March 13 2013 News in Brief New virus uses protein handle to infect cells ScienceNews Archived from the original on 2013 03 20 Blauenfeldt T Petrone L Del Nonno F Baiocchini A Falasca L Chiacchio T Bondet V Vanini V Palmieri F Galluccio G Casrouge A Eugen Olsen J Albert ML Goletti D Duffy D Ruhwald M Jul 2018 Interplay of DDP4 and IP 10 as a Potential Mechanism for Cell Recruitment to Tuberculosis Lesions Front Immunol 9 1456 1456 doi 10 3389 fimmu 2018 01456 PMC 6041415 PMID 30026741 Lioe TS Xie Z Wu J Li W Sun L Feng Q Raju S Tefsen B Ruiz Carrillo D Jan 2023 The Mycobacterium tuberculosis prolyl dipeptidyl peptidase cleaves the N terminal peptide of the immunoprotein CXCL 10 Biol Chem 404 6 633 43 doi 10 1515 hsz 2022 0265 PMID 36632703 S2CID 255596512 Further reading editAnsorge S Buhling F Kahne T Lendeckel U Reinhold D Tager M Wrenger S 1997 CD26 Dipeptidyl Peptidase IV in Lymphocyte Growth Regulation Cellular Peptidases in Immune Functions and Diseases Advances in Experimental Medicine and Biology Vol 421 pp 127 40 doi 10 1007 978 1 4757 9613 1 17 ISBN 978 1 4757 9615 5 PMID 9330689 Reinhold D Kahne T Steinbrecher A Wrenger S Neubert K Ansorge S Brocke S 2003 The role of dipeptidyl peptidase IV DP IV enzymatic activity in T cell activation and autoimmunity Biological Chemistry 383 7 8 1133 8 doi 10 1515 BC 2002 123 PMID 12437097 S2CID 30027839 Sato K Dang NH March 2003 CD26 a novel treatment target for T cell lymphoid malignancies Review International Journal of Oncology 22 3 481 97 doi 10 3892 ijo 22 3 481 inactive 31 January 2024 PMID 12579300 a href Template Cite journal html title Template Cite journal cite journal a CS1 maint DOI inactive as of January 2024 link de Meester I Lambeir AM Proost P Scharpe S 2003 Dipeptidyl Peptidase IV Substrates Dipeptidyl Aminopeptidases in Health and Disease Advances in Experimental Medicine and Biology Vol 524 pp 3 17 doi 10 1007 0 306 47920 6 1 ISBN 0 306 47717 3 PMID 12675218 Koch S Anthonsen D Skovbjerg H Sjostrom H 2003 On the role of dipeptidyl peptidase IV in the digestion of an immunodominant epitope in celiac disease Dipeptidyl Aminopeptidases in Health and Disease Advances in Experimental Medicine and Biology Vol 524 pp 181 7 doi 10 1007 0 306 47920 6 22 ISBN 0 306 47717 3 PMID 12675238 Pro B Dang NH October 2004 CD26 dipeptidyl peptidase IV and its role in cancer Histology and Histopathology 19 4 1345 51 doi 10 14670 HH 19 1345 PMID 15375776 External links editThe MEROPS online database for peptidases and their inhibitors S09 003 Dipeptidyl Peptidase IV at the U S National Library of Medicine Medical Subject Headings MeSH Banting and Best Diabetes Centre at UT dpp4 Portal nbsp Biology Retrieved from https en wikipedia org w index php title Dipeptidyl peptidase 4 amp oldid 1212639353, wikipedia, wiki, book, books, library,

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