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The cytoplasmic peptidase DPP9 is rate-limiting for degradation of proline-containing peptides

Bibliographic reference Geiss-Friedlander, Ruth ; Parmentier, Nicolas ; Möller, Ulrike ; Urlaub, Henning ; Van den Eynde, Benoît ; et. al. The cytoplasmic peptidase DPP9 is rate-limiting for degradation of proline-containing peptides. In: The Journal of Biological Chemistry, Vol. 284, no. 40, p. 27211-27219 (2009)
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  1. Glickman Michael H., Ciechanover Aaron, The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction, 10.1152/physrev.00027.2001
  2. Rosenblum Jonathan S, Kozarich John W, Prolyl peptidases: a serine protease subfamily with high potential for drug discovery, 10.1016/s1367-5931(03)00084-x
  3. Marguet D., Baggio L., Kobayashi T., Bernard A.-M., Pierres M., Nielsen P. F., Ribel U., Watanabe T., Drucker D. J., Wagtmann N., Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26, 10.1073/pnas.120069197
  4. Conarello S. L., Li Z., Ronan J., Roy R. S., Zhu L., Jiang G., Liu F., Woods J., Zycband E., Moller D. E., Thornberry N. A., Zhang B. B., Mice lacking dipeptidyl peptidase IV are protected against obesity and insulin resistance, 10.1073/pnas.0631828100
  5. Drucker D. J., Dipeptidyl Peptidase-4 Inhibition and the Treatment of Type 2 Diabetes: Preclinical biology and mechanisms of action, 10.2337/dc07-0228
  6. De Meester Ingrid, Lambeir Anne-Marie, Proost Paul, Scharpé Simon, Dipeptidyl Peptidase IV Substrates, Dipeptidyl Aminopeptidases in Health and Disease (2004) ISBN:9780306477171 p.3-17, 10.1007/0-306-47920-6_1
  7. McIntosh Christopher, H.S., Dipeptidyl peptidase iv inhibitors and diabetes therapy, 10.2741/2797
  8. Ajami Katerina, Abbott Catherine A, McCaughan Geoffrey W, Gorrell Mark D, Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity, 10.1016/j.bbaexp.2004.03.010
  9. Abbott Catherine A., Yu Denise M. T., Woollatt Erica, Sutherland Grant R., McCaughan Geoffrey W., Gorrell Mark D., Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8 : A novel dipeptidyl peptidase, 10.1046/j.1432-1327.2000.01617.x
  10. Olsen Christina, Wagtmann Nicolai, Identification and characterization of human DPP9 , a novel homologue of dipeptidyl peptidase IV, 10.1016/s0378-1119(02)01059-4
  11. QI Shu Y., RIVIERE Pierre J., TROJNAR Jerzy, JUNIEN Jean-Louis, AKINSANYA Karen O., Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases, 10.1042/bj20021914
  12. Kisselev Alexei F., Akopian Tatos N., Woo Kee Min, Goldberg Alfred L., The Sizes of Peptides Generated from Protein by Mammalian 26 and 20 S Proteasomes : IMPLICATIONS FOR UNDERSTANDING THE DEGRADATIVE MECHANISM AND ANTIGEN PRESENTATION, 10.1074/jbc.274.6.3363
  13. Tang Hung-Kuan, Tang Hsiang-Yun, Hsu Shu-Ching, Chu Yue-Ru, Chien Chia-Hui, Shu Chin-Hang, Chen Xin, Biochemical properties and expression profile of human prolyl dipeptidase DPP9, 10.1016/
  14. Lankas G. R., Leiting B., Roy R. S., Eiermann G. J., Beconi M. G., Biftu T., Chan C.-C., Edmondson S., Feeney W. P., He H., Ippolito D. E., Kim D., Lyons K. A., Ok H. O., Patel R. A., Petrov A. N., Pryor K. A., Qian X., Reigle L., Woods A., Wu J. K., Zaller D., Zhang X., Zhu L., Weber A. E., Thornberry N. A., Dipeptidyl Peptidase IV Inhibition for the Treatment of Type 2 Diabetes: Potential Importance of Selectivity Over Dipeptidyl Peptidases 8 and 9, 10.2337/diabetes.54.10.2988
  15. Wu Jia-Jing, Tang Hung-Kuan, Yeh Teng-Kuang, Chen Chi-Min, Shy Hrong-Shing, Chu Yue-Ru, Chien Chia-Hui, Tsai Ting-Yueh, Huang Yu-Chen, Huang Yu-Lin, Huang Chih-Hsiang, Tseng Huan-Yi, Jiaang Weir-Torn, Chao Yu-Sheng, Chen Xin, Biochemistry, pharmacokinetics, and toxicology of a potent and selective DPP8/9 inhibitor, 10.1016/j.bcp.2009.03.032
  16. Morel Sandra, Lévy Frédéric, Burlet-Schiltz Odile, Brasseur Francis, Probst-Kepper Michaël, Peitrequin Anne-Lise, Monsarrat Bernard, Van Velthoven Robert, Cerottini Jean-Charles, Boon Thierry, Gairin Jean Edouard, Van den Eynde Benoît J., Processing of Some Antigens by the Standard Proteasome but Not by the Immunoproteasome Results in Poor Presentation by Dendritic Cells, 10.1016/s1074-7613(00)80163-6
  17. Mørtz Ejvind, Vorm Ole, Mann Matthias, Roepstorff Peter, Identification of proteins in polyacrylamide gels by mass spectrometric peptide mapping combined with database search, 10.1002/bms.1200230503
  18. Craiu A., Akopian T., Goldberg A., Rock K. L., Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide, 10.1073/pnas.94.20.10850
  19. Serwold Thomas, Gonzalez Federico, Kim Jennifer, Jacob Richard, Shastri Nilabh, ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum, 10.1038/nature01074
  20. York Ian A., Chang Shih-Chung, Saric Tomo, Keys Jennifer A., Favreau Janice M., Goldberg Alfred L., Rock Kenneth L., The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8–9 residues, 10.1038/ni860
  21. Saric Tomo, Chang Shih-Chung, Hattori Akira, York Ian A., Markant Shirley, Rock Kenneth L., Tsujimoto Masafumi, Goldberg Alfred L., An IFN-γ–induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I–presented peptides, 10.1038/ni859
  22. Beninga Jochen, Rock Kenneth L., Goldberg Alfred L., Interferon-γ Can Stimulate Post-proteasomal Trimming of the N Terminus of an Antigenic Peptide by Inducing Leucine Aminopeptidase, 10.1074/jbc.273.30.18734
  23. Cascio P., 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide, 10.1093/emboj/20.10.2357
  24. Stoltze Lars, Schirle Markus, Schwarz Gerold, Schröter Christian, Thompson Michael W., Hersh Louis B., Kalbacher Hubert, Stevanovic Stefan, Rammensee Hans-Georg, Schild Hansjörg, 10.1038/80852
  25. Silva Celio L., Portaro Fernanda C.V., Bonato Vânia L.D., de Camargo Antonio C.M., Ferro Emer S., Thimet Oligopeptidase (EC, a Novel Protein on the Route of MHC Class I Antigen Presentation, 10.1006/bbrc.1999.0250
  26. Saric Tomo, Beninga Jochen, Graef Claudia I., Akopian Tatos N., Rock Kenneth L., Goldberg Alfred L., Major Histocompatibility Complex Class I-presented Antigenic Peptides Are Degraded in Cytosolic Extracts Primarily by Thimet Oligopeptidase, 10.1074/jbc.m105517200
  27. York Ian A., Mo Annie X.Y., Lemerise Kristen, Zeng Wanyong, Shen Yuelei, Abraham Carmela R., Saric Tomo, Goldberg Alfred L., Rock Kenneth L., The Cytosolic Endopeptidase, Thimet Oligopeptidase, Destroys Antigenic Peptides and Limits the Extent of MHC Class I Antigen Presentation, 10.1016/s1074-7613(03)00058-x
  28. Seifert Ulrike, Marañón Concepción, Shmueli Ayelet, Desoutter Jean-François, Wesoloski Lisa, Janek Katharina, Henklein Peter, Diescher Susanne, Andrieu Muriel, de la Salle Henri, Weinschenk Toni, Schild Hansjörg, Laderach Diego, Galy Anne, Haas Gaby, Kloetzel Peter-M., Reiss Yuval, Hosmalin Anne, An essential role for tripeptidyl peptidase in the generation of an MHC class I epitope, 10.1038/ni905
  29. Reits Eric, Neijssen Joost, Herberts Carla, Benckhuijsen Willemien, Janssen Lennert, Drijfhout Jan Wouter, Neefjes Jacques, A Major Role for TPPII in Trimming Proteasomal Degradation Products for MHC Class I Antigen Presentation, 10.1016/s1074-7613(04)00074-3
  30. Rammensee H. -G., Bachmann J., Emmerich N. P. N., Bachor O. A., Stevanović S., SYFPEITHI: database for MHC ligands and peptide motifs, 10.1007/s002510050595
  31. Levy F., Burri L., Morel S., Peitrequin A.-L., Levy N., Bachi A., Hellman U., Van den Eynde B. J., Servis C., The Final N-Terminal Trimming of a Subaminoterminal Proline-Containing HLA Class I-Restricted Antigenic Peptide in the Cytosol Is Mediated by Two Peptidases, 10.4049/jimmunol.169.8.4161
  32. Connolly Beth A., Sanford David G., Chiluwal Amrita K., Healey Sarah E., Peters Diane E., Dimare Matthew T., Wu Wengen, Liu Yuxin, Maw Hlaing, Zhou Yuhong, Li Youhua, Jin Zhiping, Sudmeier James L., Lai Jack H., Bachovchin William W., Dipeptide Boronic Acid Inhibitors of Dipeptidyl Peptidase IV: Determinants of Potency and in Vivo Efficacy and Safety, 10.1021/jm800390n
  33. van Endert P. M., The peptide-binding motif for the human transporter associated with antigen processing, 10.1084/jem.182.6.1883
  34. Reits Eric, Griekspoor Alexander, Neijssen Joost, Groothuis Tom, Jalink Kees, van Veelen Peter, Janssen Hans, Calafat Jero, Drijfhout Jan Wouter, Neefjes Jacques, Peptide Diffusion, Protection, and Degradation in Nuclear and Cytoplasmic Compartments before Antigen Presentation by MHC Class I, 10.1016/s1074-7613(02)00511-3
  35. Neisig, J. Immunol., 154, 1273 (1995)
  36. Uebel S., Kraas W., Kienle S., Wiesmuller K.-H., Jung G., Tampe R., Recognition principle of the TAP transporter disclosed by combinatorial peptide libraries, 10.1073/pnas.94.17.8976
  37. Daniel, J. Immunol., 161, 617 (1998)
  38. Saveanu Loredana, Carroll Oliver, Lindo Vivian, Del Val Margarita, Lopez Daniel, Lepelletier Yves, Greer Fiona, Schomburg Lutz, Fruci Doriana, Niedermann Gabriele, van Endert Peter M, Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum, 10.1038/ni1208
  39. Van der Veken Pieter, Haemers Achiel, Augustyns Koen, Prolyl Peptidases Related to Dipeptidyl Peptidase IV: Potential of Specific Inhibitors in Drug Discovery., 10.2174/156802607780091046
  40. Rock Kenneth L, York Ian A, Goldberg Alfred L, Post-proteasomal antigen processing for major histocompatibility complex class I presentation, 10.1038/ni1089
  41. Kloetzel Peter M, Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII, 10.1038/ni1090
  42. Saveanu Loredana, Carroll Oliver, Hassainya Yousra, van Endert Peter, Complexity, contradictions, and conundrums: studying post-proteasomal proteolysis in HLA class I antigen presentation, 10.1111/j.0105-2896.2005.00313.x
  43. Yewdell Jonathan W., Reits Eric, Neefjes Jacques, Making sense of mass destruction: quantitating MHC class I antigen presentation, 10.1038/nri1250
  44. Polgár L., The prolyl oligopeptidase family, 10.1007/s00018-002-8427-5