메뉴 건너뛰기




Volumn 39, Issue 1, 2016, Pages 413-424

The Dipeptidyl Peptidases 4, 8, and 9 in Mouse Monocytes and Macrophages: DPP8/9 Inhibition Attenuates M1 Macrophage Activation in Mice

Author keywords

atherosclerosis; dipeptidyl peptidase; DPP4; macrophages; monocytes

Indexed keywords

DIPEPTIDYL PEPTIDASE; DIPEPTIDYL PEPTIDASE 8, MOUSE; DIPEPTIDYL PEPTIDASE 9, MOUSE; DIPEPTIDYL PEPTIDASE IV; DPP4 PROTEIN, MOUSE; INTERLEUKIN 6;

EID: 84958058029     PISSN: 03603997     EISSN: 15732576     Source Type: Journal    
DOI: 10.1007/s10753-015-0263-5     Document Type: Article
Times cited : (27)

References (53)
  • 1
    • 85060128593 scopus 로고    scopus 로고
    • The top 10 causes of death
    • WHO. 2014. The top 10 causes of death. World Health Organization.
    • (2014) World Health Organization
  • 2
    • 84892935256 scopus 로고    scopus 로고
    • Atherosclerotic plaque destabilization: mechanisms, models, and therapeutic strategies
    • PID: 24385514
    • Silvestre-Roig, C., M.P. de Winther, C. Weber, M.J. Daemen, E. Lutgens, and O. Soehnlein. 2014. Atherosclerotic plaque destabilization: mechanisms, models, and therapeutic strategies. Circulation Research 114: 214–226. doi:10.1161/CIRCRESAHA.114.302355.
    • (2014) Circulation Research , vol.114 , pp. 214-226
    • Silvestre-Roig, C.1    de Winther, M.P.2    Weber, C.3    Daemen, M.J.4    Lutgens, E.5    Soehnlein, O.6
  • 3
    • 84869491455 scopus 로고    scopus 로고
    • Distribution of macrophage polarization markers in human atherosclerosis
    • PID: 23078881
    • Stöger, J., M. Gijbels, and S. Van der Velden. 2012. Distribution of macrophage polarization markers in human atherosclerosis. Atherosclerosis 225: 461–468.
    • (2012) Atherosclerosis , vol.225 , pp. 461-468
    • Stöger, J.1    Gijbels, M.2    Van der Velden, S.3
  • 5
    • 33846006173 scopus 로고    scopus 로고
    • The incretin system: glucagon-like peptide-1 receptor agonists and dipeptidyl peptidase-4 inhibitors in type 2 diabetes
    • Drucker, D., and M. Nauck. 2006. The incretin system: glucagon-like peptide-1 receptor agonists and dipeptidyl peptidase-4 inhibitors in type 2 diabetes. The Lancet 368: 1696–1705. doi:10.1016/S0140-6736(06)69705-5.
    • (2006) The Lancet , vol.368 , pp. 1696-1705
    • Drucker, D.1    Nauck, M.2
  • 6
    • 78649686908 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitors in the treatment of type 2 diabetes: a comparative review
    • Deacon, C.F. 2011. Dipeptidyl peptidase-4 inhibitors in the treatment of type 2 diabetes: a comparative review. Diabetes, Obesity & Metabolism 13: 7–18. doi:10.1111/j.1463-1326.2010.01306.x.
    • (2011) Diabetes, Obesity & Metabolism , vol.13 , pp. 7-18
    • Deacon, C.F.1
  • 7
    • 0029118049 scopus 로고
    • Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV
    • PID: 7628397
    • Kieffer, T.J., C.H. McIntosh, and R.A. Pederson. 1995. Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology 136: 3585–3596. doi:10.1210/endo.136.8.7628397.
    • (1995) Endocrinology , vol.136 , pp. 3585-3596
    • Kieffer, T.J.1    McIntosh, C.H.2    Pederson, R.A.3
  • 9
    • 0026755628 scopus 로고
    • Dipeptidyl(amino)peptidase IV and aminopeptidase M metabolize circulating substance P in vivo
    • PID: 1372050
    • Ahmad, S., L. Wang, and P.E. Ward. 1992. Dipeptidyl(amino)peptidase IV and aminopeptidase M metabolize circulating substance P in vivo. The Journal of Pharmacology and Experimental Therapeutics 260: 1257–1261.
    • (1992) The Journal of Pharmacology and Experimental Therapeutics , vol.260 , pp. 1257-1261
    • Ahmad, S.1    Wang, L.2    Ward, P.E.3
  • 10
    • 29744462729 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV converts intact B-type natriuretic peptide into its des-SerPro form
    • PID: 16254193
    • Brandt, I., A.-M. Lambeir, J.-M. Ketelslegers, M. Vanderheyden, S. Scharpé, and I. De Meester. 2006. Dipeptidyl-peptidase IV converts intact B-type natriuretic peptide into its des-SerPro form. Clinical Chemistry 52: 82–87. doi:10.1373/clinchem.2005.057638.
    • (2006) Clinical Chemistry , vol.52 , pp. 82-87
    • Brandt, I.1    Lambeir, A.-M.2    Ketelslegers, J.-M.3    Vanderheyden, M.4    Scharpé, S.5    De Meester, I.6
  • 16
    • 0031908130 scopus 로고    scopus 로고
    • The structure and function of CD26 in the T-cell immune response
    • PID: 9553764
    • Morimoto, C., and S.F. Schlossman. 1998. The structure and function of CD26 in the T-cell immune response. Immunological Reviews 161: 55–70.
    • (1998) Immunological Reviews , vol.161 , pp. 55-70
    • Morimoto, C.1    Schlossman, S.F.2
  • 18
    • 33646706075 scopus 로고    scopus 로고
    • Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis
    • PID: 16704418
    • Yu, D.M.T., X.M. Wang, G.W. McCaughan, and M.D. Gorrell. 2006. Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis. The FEBS Journal 273: 2447–2460. doi:10.1111/j.1742-4658.2006.05253.x.
    • (2006) The FEBS Journal , vol.273 , pp. 2447-2460
    • Yu, D.M.T.1    Wang, X.M.2    McCaughan, G.W.3    Gorrell, M.D.4
  • 19
    • 79960661852 scopus 로고    scopus 로고
    • A novel role of dipeptidyl peptidase 9 in epidermal growth factor signaling. Molecular Cancer Research 9
    • Yao, T.W., W.S. Kim, D.M.T. Yu, G. Sharbeen, G.W. McCaughan, K.Y. Choi, P. Xia, and M.D. Gorrell. 2011. A novel role of dipeptidyl peptidase 9 in epidermal growth factor signaling. Molecular Cancer Research 9. AACR: 948–59.
    • (2011) AACR , pp. 948-959
    • Yao, T.W.1    Kim, W.S.2    Yu, D.M.T.3    Sharbeen, G.4    McCaughan, G.W.5    Choi, K.Y.6    Xia, P.7    Gorrell, M.D.8
  • 23
    • 84871782137 scopus 로고    scopus 로고
    • A novel SUMO1-specific interacting motif in dipeptidyl peptidase 9 (DPP9) that is important for enzymatic regulation
    • PID: 23152501
    • Pilla, E., U. Möller, G. Sauer, F. Mattiroli, F. Melchior, and R. Geiss-Friedlander. 2012. A novel SUMO1-specific interacting motif in dipeptidyl peptidase 9 (DPP9) that is important for enzymatic regulation. The Journal of Biological Chemistry 287: 44320–44329. doi:10.1074/jbc.M112.397224.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 44320-44329
    • Pilla, E.1    Möller, U.2    Sauer, G.3    Mattiroli, F.4    Melchior, F.5    Geiss-Friedlander, R.6
  • 31
    • 84901926135 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitors and heart failure: a meta-analysis of randomized clinical trials
    • PID: 24793580
    • Monami, M., I. Dicembrini, and E. Mannucci. 2014. Dipeptidyl peptidase-4 inhibitors and heart failure: a meta-analysis of randomized clinical trials. Nutrition, Metabolism, and Cardiovascular Diseases 24: 689–697. doi:10.1016/j.numecd.2014.01.017.
    • (2014) Nutrition, Metabolism, and Cardiovascular Diseases , vol.24 , pp. 689-697
    • Monami, M.1    Dicembrini, I.2    Mannucci, E.3
  • 36
    • 84355166409 scopus 로고    scopus 로고
    • Method comparison of dipeptidyl peptidase IV activity assays and their application in biological samples containing reversible inhibitors. Clinica chimica acta; international journal of clinical chemistry 413: 456–62
    • Matheeussen, V., A.-M. Lambeir, W. Jungraithmayr, N. Gomez, K. Mc Entee, P. Van der Veken, S. Scharpé, and I. De Meester. 2011. Method comparison of dipeptidyl peptidase IV activity assays and their application in biological samples containing reversible inhibitors. Clinica chimica acta; international journal of clinical chemistry 413: 456–62. doi:10.1016/j.cca.2011.10.031 Elsevier B.V.
    • (2011) doi:10.1016/j.cca.2011.10.031 Elsevier B.V
    • Matheeussen, V.1    Lambeir, A.-M.2    Jungraithmayr, W.3    Gomez, N.4    Mc Entee, K.5    Van der Veken, P.6    Scharpé, S.7    De Meester, I.8
  • 37
    • 33744814340 scopus 로고    scopus 로고
    • Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV
    • PID: 16475979
    • Bjelke, J.R., J. Christensen, P.F. Nielsen, S. Branner, A.B. Kanstrup, N. Wagtmann, and H.B. Rasmussen. 2006. Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV. The Biochemical Journal 396: 391–399. doi:10.1042/BJ20060079.
    • (2006) The Biochemical Journal , vol.396 , pp. 391-399
    • Bjelke, J.R.1    Christensen, J.2    Nielsen, P.F.3    Branner, S.4    Kanstrup, A.B.5    Wagtmann, N.6    Rasmussen, H.B.7
  • 38
    • 34547093890 scopus 로고    scopus 로고
    • Methods to detect nitric oxide and its metabolites in biological samples
    • Bryan, N.S., and M.B. Grisham. 2008. Methods to detect nitric oxide and its metabolites in biological samples. Free Radical Biology and Medicine 43: 645–657.
    • (2008) Free Radical Biology and Medicine , vol.43 , pp. 645-657
    • Bryan, N.S.1    Grisham, M.B.2
  • 39
    • 80051785333 scopus 로고    scopus 로고
    • DPP-4 (CD26) inhibitor alogliptin inhibits atherosclerosis in diabetic apolipoprotein E-deficient mice
    • PID: 21558879
    • Ta, N.N., C.A. Schuyler, Y. Li, M.F. Lopes-Virella, and Y. Huang. 2011. DPP-4 (CD26) inhibitor alogliptin inhibits atherosclerosis in diabetic apolipoprotein E-deficient mice. Journal of Cardiovascular Pharmacology 58: 157–166. doi:10.1097/FJC.0b013e31821e5626.
    • (2011) Journal of Cardiovascular Pharmacology , vol.58 , pp. 157-166
    • Ta, N.N.1    Schuyler, C.A.2    Li, Y.3    Lopes-Virella, M.F.4    Huang, Y.5
  • 41
    • 84862128306 scopus 로고    scopus 로고
    • Effects of p KF275–055, a dipeptidyl peptidase-4 inhibitor, on the development of atherosclerotic lesions in apolipoprotein E-null mice
    • PID: 22225957
    • Terasaki, M., M. Nagashima, T. Watanabe, K. Nohtomi, Y. Mori, A. Miyazaki, and T. Hirano. 2012. Effects of p KF275–055, a dipeptidyl peptidase-4 inhibitor, on the development of atherosclerotic lesions in apolipoprotein E-null mice. Metabolism 61: 974–977. doi:10.1016/j.metabol.2011.11.011.
    • (2012) Metabolism , vol.61 , pp. 974-977
    • Terasaki, M.1    Nagashima, M.2    Watanabe, T.3    Nohtomi, K.4    Mori, Y.5    Miyazaki, A.6    Hirano, T.7
  • 42
    • 84881507403 scopus 로고    scopus 로고
    • Preventive effect of dipeptidyl peptidase-4 inhibitor on atherosclerosis is mainly attributable to incretin’s actions in nondiabetic and diabetic apolipoprotein E-null mice
    • PID: 23967137
    • Terasaki, M., M. Nagashima, K. Nohtomi, K. Kohashi, M. Tomoyasu, K. Sinmura, Y. Nogi, Y. Katayama, K. Sato, F. Itoh, T. Watanabe, and T. Hirano. 2013. Preventive effect of dipeptidyl peptidase-4 inhibitor on atherosclerosis is mainly attributable to incretin’s actions in nondiabetic and diabetic apolipoprotein E-null mice. PLoS One 8, e70933. doi:10.1371/journal.pone.0070933.
    • (2013) PLoS One , vol.8
    • Terasaki, M.1    Nagashima, M.2    Nohtomi, K.3    Kohashi, K.4    Tomoyasu, M.5    Sinmura, K.6    Nogi, Y.7    Katayama, Y.8    Sato, K.9    Itoh, F.10    Watanabe, T.11    Hirano, T.12
  • 43
    • 84874597960 scopus 로고    scopus 로고
    • Anagliptin, a DPP-4 inhibitor, suppresses proliferation of vascular smooth muscles and monocyte inflammatory reaction and attenuates atherosclerosis in male apo E-deficient mice
    • PID: 23337530
    • Ervinna, N., T. Mita, E. Yasunari, K. Azuma, R. Tanaka, S. Fujimura, D. Sukmawati, T. Nomiyama, A. Kanazawa, R. Kawamori, Y. Fujitani, and H. Watada. 2013. Anagliptin, a DPP-4 inhibitor, suppresses proliferation of vascular smooth muscles and monocyte inflammatory reaction and attenuates atherosclerosis in male apo E-deficient mice. Endocrinology 154: 1260–1270. doi:10.1210/en.2012-1855.
    • (2013) Endocrinology , vol.154 , pp. 1260-1270
    • Ervinna, N.1    Mita, T.2    Yasunari, E.3    Azuma, K.4    Tanaka, R.5    Fujimura, S.6    Sukmawati, D.7    Nomiyama, T.8    Kanazawa, A.9    Kawamori, R.10    Fujitani, Y.11    Watada, H.12
  • 48
    • 16844363378 scopus 로고    scopus 로고
    • The sesquiterpene lactone parthenolide induces apoptosis of human acute myelogenous leukemia stem and progenitor cells
    • PID: 15687234
    • Guzman, M.L., R.M. Rossi, L. Karnischky, X. Li, D.R. Peterson, D.S. Howard, and C.T. Jordan. 2005. The sesquiterpene lactone parthenolide induces apoptosis of human acute myelogenous leukemia stem and progenitor cells. Blood 105: 4163–4169. doi:10.1182/blood-2004-10-4135.
    • (2005) Blood , vol.105 , pp. 4163-4169
    • Guzman, M.L.1    Rossi, R.M.2    Karnischky, L.3    Li, X.4    Peterson, D.R.5    Howard, D.S.6    Jordan, C.T.7
  • 49
    • 34447319405 scopus 로고    scopus 로고
    • Parthenolide induces significant apoptosis and production of reactive oxygen species in high-risk pre-B leukemia cells
    • PID: 17470383
    • Zunino, S.J., J.M. Ducore, and D.H. Storms. 2007. Parthenolide induces significant apoptosis and production of reactive oxygen species in high-risk pre-B leukemia cells. Cancer Letters 254: 119–127. doi:10.1016/j.canlet.2007.03.002.
    • (2007) Cancer Letters , vol.254 , pp. 119-127
    • Zunino, S.J.1    Ducore, J.M.2    Storms, D.H.3
  • 50
    • 79952711704 scopus 로고    scopus 로고
    • Parthenolide sensitizes hepatocellular carcinoma cells to TRAIL by inducing the expression of death receptors through inhibition of STAT3 activation
    • PID: 21413021
    • Carlisi, D., A. D’Anneo, L. Angileri, M. Lauricella, S. Emanuele, A. Santulli, R. Vento, and G. Tesoriere. 2011. Parthenolide sensitizes hepatocellular carcinoma cells to TRAIL by inducing the expression of death receptors through inhibition of STAT3 activation. Journal of Cellular Physiology 226: 1632–1641. doi:10.1002/jcp.22494.
    • (2011) Journal of Cellular Physiology , vol.226 , pp. 1632-1641
    • Carlisi, D.1    D’Anneo, A.2    Angileri, L.3    Lauricella, M.4    Emanuele, S.5    Santulli, A.6    Vento, R.7    Tesoriere, G.8
  • 51
    • 66449097674 scopus 로고    scopus 로고
    • Parthenolide promotes the ubiquitination of MDM2 and activates p53 cellular functions
    • PID: 19276167
    • Gopal, Y.N.V., E. Chanchorn, and M.W. Van Dyke. 2009. Parthenolide promotes the ubiquitination of MDM2 and activates p53 cellular functions. Molecular Cancer Therapeutics 8: 552–562. doi:10.1158/1535-7163.MCT-08-0661.
    • (2009) Molecular Cancer Therapeutics , vol.8 , pp. 552-562
    • Gopal, Y.N.V.1    Chanchorn, E.2    Van Dyke, M.W.3
  • 53
    • 84938497115 scopus 로고    scopus 로고
    • The dipeptidyl peptidase family, prolyl oligopeptidase, and prolyl carboxypeptidase in the immune system and inflammatory disease, including atherosclerosis. Frontiers in Immunology 6
    • Waumans, Y., L. Baerts, K. Kehoe, A.-M. Lambeir, and I. De Meester. 2015. The dipeptidyl peptidase family, prolyl oligopeptidase, and prolyl carboxypeptidase in the immune system and inflammatory disease, including atherosclerosis. Frontiers in Immunology 6. doi:10.3389/fimmu.2015.00387 Frontiers.
    • (2015) doi:10.3389/fimmu.2015.00387 Frontiers
    • Waumans, Y.1    Baerts, L.2    Kehoe, K.3    Lambeir, A.-M.4    De Meester, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.