메뉴 건너뛰기




Volumn 9, Issue 1, 2016, Pages

Dipeptidyl peptidase-4 and kidney fibrosis in diabetes

Author keywords

Diabetic nephropathy; Dipeptidyl peptidase 4; Kidney protection

Indexed keywords

ALOGLIPTIN; BETA1 INTEGRIN; DIPEPTIDYL PEPTIDASE IV; DIPEPTIDYL PEPTIDASE IV INHIBITOR; GLITAZONE DERIVATIVE; INSULIN; LC 15 0444; LINAGLIPTIN; MICRORNA; SAXAGLIPTIN; SITAGLIPTIN; SULFONYLUREA DERIVATIVE; UNCLASSIFIED DRUG; VILDAGLIPTIN;

EID: 84957629803     PISSN: None     EISSN: 17551536     Source Type: Journal    
DOI: 10.1186/s13069-016-0038-0     Document Type: Review
Times cited : (47)

References (110)
  • 1
    • 80051986265 scopus 로고    scopus 로고
    • Globalization of diabetes: The role of diet, lifestyle, and genes
    • Hu FB. Globalization of diabetes: the role of diet, lifestyle, and genes. Diabetes care. 2011;34(6):1249-57. doi:10.2337/dc11-0442.
    • (2011) Diabetes care , vol.34 , Issue.6 , pp. 1249-1257
    • Hu, F.B.1
  • 2
    • 84901808296 scopus 로고    scopus 로고
    • The global implications of diabetes and cancer
    • Shi Y, Hu FB. The global implications of diabetes and cancer. Lancet. 2014; 383(9933):1947-8. doi:10.1016/S0140-6736(14)60886-2.
    • (2014) Lancet , vol.383 , Issue.9933 , pp. 1947-1948
    • Shi, Y.1    Hu, F.B.2
  • 3
    • 0034773498 scopus 로고    scopus 로고
    • Diabetic nephropathy: Prevention and treatment
    • Parving HH. Diabetic nephropathy: prevention and treatment. Kidney international. 2001;60(5):2041-55. doi:10.1046/j.1523-1755.2001.00020.x.
    • (2001) Kidney international , vol.60 , Issue.5 , pp. 2041-2055
    • Parving, H.H.1
  • 4
    • 0037061867 scopus 로고    scopus 로고
    • Clinical practice. Nephropathy in patients with type 2 diabetes
    • Remuzzi G, Schieppati A, Ruggenenti P. Clinical practice. Nephropathy in patients with type 2 diabetes. The New England journal of medicine. 2002; 346(15):1145-51. doi:10.1056/NEJMcp01 1 773.
    • (2002) The New England journal of medicine , vol.346 , Issue.15 , pp. 1145-1151
    • Remuzzi, G.1    Schieppati, A.2    Ruggenenti, P.3
  • 5
    • 0028809108 scopus 로고
    • Intensified diabetes management: Lessons from the diabetes control and complications trial
    • Mazze RS, Bergenstal R, Ginsberg B. Intensified diabetes management: lessons from the diabetes control and complications trial. Int J Clin Pharmacol Ther. 199533(1)43-51.
    • (1995) Int J Clin Pharmacol Ther , vol.33 , Issue.1 , pp. 43-51
    • Mazze, R.S.1    Bergenstal, R.2    Ginsberg, B.3
  • 6
    • 0034641568 scopus 로고    scopus 로고
    • Association of glycaemia with macrovascular and microvascular complications of type 2 diabetes (UKPDS 35): Prospective observational study
    • Stratton IM, Adler AI, Neil HA, Matthews DR, Manley SE, Cull CA, et al. Association of glycaemia with macrovascular and microvascular complications of type 2 diabetes (UKPDS 35): prospective observational study. Bmj. 2000;321(7258):405-12.
    • (2000) Bmj , vol.321 , Issue.7258 , pp. 405-412
    • Stratton, I.M.1    Adler, A.I.2    Neil, H.A.3    Matthews, D.R.4    Manley, S.E.5    Cull, C.A.6
  • 7
    • 41849137193 scopus 로고    scopus 로고
    • What is the mechanism of microalbuminuria in diabetes: A role for the glomerular endothelium?
    • Satchell SC, Tooke JE. What is the mechanism of microalbuminuria in diabetes: a role for the glomerular endothelium? Diabetologia. 2008;51(5): 714-25. doi:10.1007/s00125-008-0961-8.
    • (2008) Diabetologia , vol.51 , Issue.5 , pp. 714-725
    • Satchell, S.C.1    Tooke, J.E.2
  • 8
    • 84869238002 scopus 로고    scopus 로고
    • DPP-4 inhibition on top of angiotensin receptor blockade offers a new therapeutic approach for diabetic nephropathy
    • Alter ML, Ott IM, von Websky K, Tsuprykov O, Sharkovska Y, Krause-Relle K, et al. DPP-4 inhibition on top of angiotensin receptor blockade offers a new therapeutic approach for diabetic nephropathy. Kidney & blood pressure research. 2012;36(1):119-30. doi:10.1159/000341487.
    • (2012) Kidney & blood pressure research , vol.36 , Issue.1 , pp. 119-130
    • Alter, M.L.1    Ott, I.M.2    von Websky, K.3    Tsuprykov, O.4    Sharkovska, Y.5    Krause-Relle, K.6
  • 9
    • 84924328397 scopus 로고    scopus 로고
    • Crosstalk between advanced glycation end products (AGEs)-receptor RAGE axis and dipeptidyl peptidase-4-incretin system in diabetic vascular complications
    • Yamagishi S, Fukami K, Matsui T. Crosstalk between advanced glycation end products (AGEs)-receptor RAGE axis and dipeptidyl peptidase-4-incretin system in diabetic vascular complications. Cardiovasc Diabetol. 2015;14:2. doi:10.1186/s12933-015-0176-5.
    • (2015) Cardiovasc Diabetol , vol.14 , pp. 2
    • Yamagishi, S.1    Fukami, K.2    Matsui, T.3
  • 10
    • 84885367853 scopus 로고    scopus 로고
    • Renal effects of DPP-4 inhibitors: A focus on microalbuminuria
    • Haluzik M, Frolik J, Rychlik I. Renal effects of DPP-4 inhibitors: a focus on microalbuminuria. Int J Endocrinol. 2013;2013:895102. doi:10.1155/2013/895102.
    • (2013) Int J Endocrinol , vol.2013 , pp. 895102
    • Haluzik, M.1    Frolik, J.2    Rychlik, I.3
  • 11
    • 0037787851 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV from bench to bedside: An update on structural properties, functions, and clinical aspects of the enzyme DPP IV
    • Lambeir AM, Durinx C, Scharpe S, De Meester I. Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV. Crit Rev Clin Lab Sci. 2003;40(3):209-94. doi:10.1080/713609354.
    • (2003) Crit Rev Clin Lab Sci , vol.40 , Issue.3 , pp. 209-294
    • Lambeir, A.M.1    Durinx, C.2    Scharpe, S.3    De Meester, I.4
  • 12
    • 0027201145 scopus 로고
    • Direct association of adenosine deaminase with a T cell activation antigen, CD26
    • 12 Kameoka J, Tanaka T, Nojima Y, Schlossman SF, Morimoto C Direct association of adenosine deaminase with a T cell activation antigen, CD26. Science. 1993;261(5120):466-9.
    • (1993) Science , vol.261 , Issue.5120 , pp. 466-469
    • Kameoka, J.1    Tanaka, T.2    Nojima, Y.3    Schlossman, S.F.4    Morimoto, C.5
  • 13
    • 34648815810 scopus 로고    scopus 로고
    • Emerging roles ofproteases in tumour suppression
    • Lopez-Otin C, Matrisian LM. Emerging roles ofproteases in tumour suppression. Nat Rev Cancer. 2007;7(10):800-8. doi:10.1038/nrc2228.
    • (2007) Nat Rev Cancer , vol.7 , Issue.10 , pp. 800-808
    • Lopez-Otin, C.1    Matrisian, L.M.2
  • 14
    • 84881479703 scopus 로고    scopus 로고
    • Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26
    • Lu G, Hu Y, Wang Q, Qi J, Gao F, Li Y, et al. Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26. Nature. 2013;500(7461):227-31. doi:10.1038/nature12328.
    • (2013) Nature , vol.500 , Issue.7461 , pp. 227-231
    • Lu, G.1    Hu, Y.2    Wang, Q.3    Qi, J.4    Gao, F.5    Li, Y.6
  • 15
    • 0033159183 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV: A cell surface peptidase involved in regulating T cell growth (review)
    • Kahne T, Lendeckel U, Wrenger S, Neubert K, Ansorge S, Reinhold D. Dipeptidyl peptidase IV: a cell surface peptidase involved in regulating T cell growth (review). Int J Mol Med. 1999;4(1):3-15.
    • (1999) Int J Mol Med , vol.4 , Issue.1 , pp. 3-15
    • Kahne, T.1    Lendeckel, U.2    Wrenger, S.3    Neubert, K.4    Ansorge, S.5    Reinhold, D.6
  • 16
    • 15044341261 scopus 로고    scopus 로고
    • What do we know about the secretion and degradation of incretin hormones?
    • Deacon CF. What do we know about the secretion and degradation of incretin hormones? Regul Pept. 2005;128(2):117-24. doi:10.1016/j. regpep.2004.06.007.
    • (2005) Regul Pept , vol.128 , Issue.2 , pp. 117-124
    • Deacon, C.F.1
  • 17
    • 84920095184 scopus 로고    scopus 로고
    • Pharmacology, physiology, and mechanisms of action of dipeptidyl peptidase-4 inhibitors
    • Mulvihill EE, Drucker DJ. Pharmacology, physiology, and mechanisms of action of dipeptidyl peptidase-4 inhibitors. Endocr Rev. 2014;35(6):992-1019. doi:10.1210/er.2014-1035.
    • (2014) Endocr Rev , vol.35 , Issue.6 , pp. 992-1019
    • Mulvihill, E.E.1    Drucker, D.J.2
  • 19
    • 29744462729 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV converts intact B-type natriuretic peptide into its des-SerPro form
    • Brandt I, Lambeir AM, Ketelslegers JM, Vanderheyden M, Scharpe S, De Meester I. Dipeptidyl-peptidase IV converts intact B-type natriuretic peptide into its des-SerPro form. Clin Chem. 2006;52(1):82-7. doi:10.1373/clinchem.2005.057638.
    • (2006) Clin Chem , vol.52 , Issue.1 , pp. 82-87
    • Brandt, I.1    Lambeir, A.M.2    Ketelslegers, J.M.3    Vanderheyden, M.4    Scharpe, S.5    De Meester, I.6
  • 20
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV, (CD26)-role in the inactivation of regulatory peptides
    • Mentlein R. Dipeptidyl-peptidase IV, (CD26)-role in the inactivation of regulatory peptides. Regul Pept. 1999;85(1):9-24.
    • (1999) Regul Pept , vol.85 , Issue.1 , pp. 9-24
    • Mentlein, R.1
  • 21
    • 84856713524 scopus 로고    scopus 로고
    • High mobility group box 1 is a novel substrate ofdipeptidyl peptidase-IV
    • Marchetti C, Di Carlo A, Facchiano F, Senatore C, De Cristofaro R, Luzi A, et al. High mobility group box 1 is a novel substrate ofdipeptidyl peptidase-IV. Diabetologia. 2012;55(1):236-44. doi:10.1007/s00125-011-2213-6.
    • (2012) Diabetologia , vol.55 , Issue.1 , pp. 236-244
    • Marchetti, C.1    Di Carlo, A.2    Facchiano, F.3    Senatore, C.4    De Cristofaro, R.5    Luzi, A.6
  • 22
    • 70549096922 scopus 로고    scopus 로고
    • Inhibitor selectivity in the clinical application of dipeptidyl peptidase-4 inhibition
    • Kirby M, Yu DM, O'Connor S, Gorrell MD. Inhibitor selectivity in the clinical application of dipeptidyl peptidase-4 inhibition. Clinical science. 2010;118(1): 31-41. doi:10.1042/CS20090047.
    • (2010) Clinical science , vol.118 , Issue.1 , pp. 31-41
    • Kirby, M.1    Yu, D.M.2    O'Connor, S.3    Gorrell, M.D.4
  • 23
    • 0035723325 scopus 로고    scopus 로고
    • CD26: A multifunctional integral membrane and secreted protein of activated lymphocytes
    • Gorrell MD, Gysbers V, McCaughan GW. CD26: a multifunctional integral membrane and secreted protein of activated lymphocytes. Scand J Immunol. 2001;54(3):249-64.
    • (2001) Scand J Immunol , vol.54 , Issue.3 , pp. 249-264
    • Gorrell, M.D.1    Gysbers, V.2    McCaughan, G.W.3
  • 25
    • 10644296948 scopus 로고    scopus 로고
    • One site mutation disrupts dimer formation in human DPP-IV proteins
    • Chien CH, Huang LH, Chou CY, Chen YS, Han YS, Chang GG, et al. One site mutation disrupts dimer formation in human DPP-IV proteins. J Biol Chem. 2004;279(50):52338-45. doi:10.1074/jbc. M406185200.
    • (2004) J Biol Chem , vol.279 , Issue.50 , pp. 52338-52345
    • Chien, C.H.1    Huang, L.H.2    Chou, C.Y.3    Chen, Y.S.4    Han, Y.S.5    Chang, G.G.6
  • 26
    • 0033852128 scopus 로고    scopus 로고
    • Molecular characterization of dipeptidyl peptidase activity in serum: Soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides
    • Durinx C, Lambeir AM, Bosmans E, Falmagne JB, Berghmans R, Haemers A, et al. Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides. Eur J Biochem. 2000;267(17):5608-13.
    • (2000) Eur J Biochem , vol.267 , Issue.17 , pp. 5608-5613
    • Durinx, C.1    Lambeir, A.M.2    Bosmans, E.3    Falmagne, J.B.4    Berghmans, R.5    Haemers, A.6
  • 27
    • 70349774693 scopus 로고    scopus 로고
    • On the origin of serum CD26 and its altered concentration in cancer patients
    • Cordero OJ, Salgado FJ, Nogueira M. On the origin of serum CD26 and its altered concentration in cancer patients. Cancer Immunol Immunother. 2009;58(11):1723-47. doi:10.1007/s00262-009-0728-1.
    • (2009) Cancer Immunol Immunother , vol.58 , Issue.11 , pp. 1723-1747
    • Cordero, O.J.1    Salgado, F.J.2    Nogueira, M.3
  • 28
    • 78650799604 scopus 로고    scopus 로고
    • Soluble CD26 / dipeptidyl peptidase IV enhances human lymphocyte proliferation in vitro independent of dipeptidyl peptidase enzyme activity and adenosine deaminase binding
    • Yu DM, Slaitini L, Gysbers V, Riekhoff AG, Kahne T, Knott HM, et al. Soluble CD26 / dipeptidyl peptidase IV enhances human lymphocyte proliferation in vitro independent of dipeptidyl peptidase enzyme activity and adenosine deaminase binding. Scand J Immunol. 2011;73(2):102-11. doi:10.1111/j.1365-3083.2010.02488.x.
    • (2011) Scand J Immunol , vol.73 , Issue.2 , pp. 102-111
    • Yu, D.M.1    Slaitini, L.2    Gysbers, V.3    Riekhoff, A.G.4    Kahne, T.5    Knott, H.M.6
  • 29
    • 80052096595 scopus 로고    scopus 로고
    • Dipeptidyl peptidase 4 is a novel adipokine potentially linking obesity to the metabolic syndrome
    • Lamers D, Famulla S, Wronkowitz N, Hartwig S, Lehr S, Ouwens DM, et al. Dipeptidyl peptidase 4 is a novel adipokine potentially linking obesity to the metabolic syndrome. Diabetes. 2011;60(7):1917-25. doi:10.2337/db10-1707.
    • (2011) Diabetes , vol.60 , Issue.7 , pp. 1917-1925
    • Lamers, D.1    Famulla, S.2    Wronkowitz, N.3    Hartwig, S.4    Lehr, S.5    Ouwens, D.M.6
  • 30
    • 0034642525 scopus 로고    scopus 로고
    • Regulation of CD26/DPPIV gene expression by interferons and retinoic acid in tumor B cells
    • Bauvois B, Djavaheri-Mergny M, Rouillard D, Dumont J, Wietzerbin J. Regulation of CD26/DPPIV gene expression by interferons and retinoic acid in tumor B cells. Oncogene. 2000;19(2):265-72. doi:10.1038/sj. onc.1203292.
    • (2000) Oncogene , vol.19 , Issue.2 , pp. 265-272
    • Bauvois, B.1    Djavaheri-Mergny, M.2    Rouillard, D.3    Dumont, J.4    Wietzerbin, J.5
  • 32
    • 84902552092 scopus 로고    scopus 로고
    • Soluble DPP4 originates in part from bone marrow cells and not from the kidney
    • Wang Z, Grigo C, Steinbeck J, von Horsten S, Amann K, Daniel C. Soluble DPP4 originates in part from bone marrow cells and not from the kidney. Peptides. 2014;57:109-17. doi:10.1016/j. peptides.2014.05.006.
    • (2014) Peptides , vol.57 , pp. 109-117
    • Wang, Z.1    Grigo, C.2    Steinbeck, J.3    von Horsten, S.4    Amann, K.5    Daniel, C.6
  • 33
    • 33644618433 scopus 로고    scopus 로고
    • The biology of incretin hormones
    • Drucker DJ. The biology of incretin hormones. Cell Metab. 2006;3(3):153-65. doi:10.1016/j. cmet.2006.01.004.
    • (2006) Cell Metab , vol.3 , Issue.3 , pp. 153-165
    • Drucker, D.J.1
  • 34
    • 0037234531 scopus 로고    scopus 로고
    • Therapeutic potential of dipeptidyl peptidase IV inhibitors for the treatment of type 2 diabetes
    • Drucker DJ. Therapeutic potential of dipeptidyl peptidase IV inhibitors for the treatment of type 2 diabetes. Expert opinion on investigational drugs. 2003;12(1):87-100. doi:10.1517/13543784.12.1.87.
    • (2003) Expert opinion on investigational drugs , vol.12 , Issue.1 , pp. 87-100
    • Drucker, D.J.1
  • 35
    • 0028323205 scopus 로고
    • CD26: A surface protease involved in T-cell activation
    • Fleischer B. CD26: a surface protease involved in T-cell activation. Immunology today. 1994;15(4):180-4. doi:10.1016/0167-5699(94)90316-6.
    • (1994) Immunology today , vol.15 , Issue.4 , pp. 180-184
    • Fleischer, B.1
  • 36
    • 0036583164 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in type 2 diabetes
    • Ahren B, Simonsson E, Larsson H, Landin-Olsson M, Torgeirsson H, Jansson PA, et al. Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in type 2 diabetes. Diabetes care. 2002;25(5):869-75.
    • (2002) Diabetes care , vol.25 , Issue.5 , pp. 869-875
    • Ahren, B.1    Simonsson, E.2    Larsson, H.3    Landin-Olsson, M.4    Torgeirsson, H.5    Jansson, P.A.6
  • 37
    • 84891888112 scopus 로고    scopus 로고
    • Adipose dipeptidyl peptidase-4 and obesity: Correlation with insulin resistance and depot-specific release from adipose tissue in vivo and in vitro
    • Sell H, Bluher M, Kloting N, Schlich R, Willems M, Ruppe F, et al. Adipose dipeptidyl peptidase-4 and obesity: correlation with insulin resistance and depot-specific release from adipose tissue in vivo and in vitro. Diabetes care. 2013;36(12):4083-90. doi:10.2337/dc13-0496.
    • (2013) Diabetes care , vol.36 , Issue.12 , pp. 4083-4090
    • Sell, H.1    Bluher, M.2    Kloting, N.3    Schlich, R.4    Willems, M.5    Ruppe, F.6
  • 38
    • 84930625640 scopus 로고    scopus 로고
    • DPP4 in cardiometabolic disease: Recent insights from the laboratory and clinical trials of DPP4 inhibition
    • Zhong J, Maiseyeu A, Davis SN, Rajagopalan S. DPP4 in cardiometabolic disease: recent insights from the laboratory and clinical trials of DPP4 inhibition. Circulation research. 2015;116(8):1491-504. doi:10.1161/CIRCRESAHA.116.305665.
    • (2015) Circulation research , vol.116 , Issue.8 , pp. 1491-1504
    • Zhong, J.1    Maiseyeu, A.2    Davis, S.N.3    Rajagopalan, S.4
  • 39
    • 84859174317 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitors for treatment of type 2 diabetes mellitus in the clinical setting: Systematic review and meta-analysis
    • Karagiannis T, Paschos P, Paletas K, Matthews DR, Tsapas A. Dipeptidyl peptidase-4 inhibitors for treatment of type 2 diabetes mellitus in the clinical setting: systematic review and meta-analysis. Bmj. 2012;344:e1369. doi:10.1136/bmj. e1369.
    • (2012) Bmj , vol.344 , pp. e1369
    • Karagiannis, T.1    Paschos, P.2    Paletas, K.3    Matthews, D.R.4    Tsapas, A.5
  • 40
    • 84890568491 scopus 로고    scopus 로고
    • Efficacy and safety ofdipeptidyl peptidase-4 inhibitors and metformin as initial combination therapy and as monotherapy in patients with type 2 diabetes mellitus: A meta-analysis
    • Wu D, Li L, Liu C. Efficacy and safety ofdipeptidyl peptidase-4 inhibitors and metformin as initial combination therapy and as monotherapy in patients with type 2 diabetes mellitus: a meta-analysis. Diabetes, obesity & metabolism. 2014;16(1):30-7. doi:10.1111/dom.12174.
    • (2014) Diabetes, obesity & metabolism , vol.16 , Issue.1 , pp. 30-37
    • Wu, D.1    Li, L.2    Liu, C.3
  • 41
    • 84864373256 scopus 로고    scopus 로고
    • Effect of antidiabetic agents added to metformin on glycaemic control, hypoglycaemia and weight change in patients with type 2 diabetes: A network meta-analysis
    • Liu SC, Tu YK, Chien MN, Chien KL. Effect of antidiabetic agents added to metformin on glycaemic control, hypoglycaemia and weight change in patients with type 2 diabetes: a network meta-analysis. Diabetes, obesity & metabolism. 2012;14(9):810-20. doi:10.1111/j.1463-1326.2012.01606.x.
    • (2012) Diabetes, obesity & metabolism , vol.14 , Issue.9 , pp. 810-820
    • Liu, S.C.1    Tu, Y.K.2    Chien, M.N.3    Chien, K.L.4
  • 43
    • 84900884793 scopus 로고    scopus 로고
    • Clinical audit of patients using DPP4 inhibitors in longstanding type 2 diabetes
    • Kumar KV, Gupta AK. Clinical audit of patients using DPP4 inhibitors in longstanding type 2 diabetes. Diabetes & metabolic syndrome. 2014. doi:10.1016/j. dsx.2014.04.031.
    • (2014) Diabetes & metabolic syndrome
    • Kumar, K.V.1    Gupta, A.K.2
  • 44
    • 77955406467 scopus 로고    scopus 로고
    • Effects of sitagliptin treatment on dysmetabolism, inflammation, and oxidative stress in an animal model of type 2 diabetes (ZDF rat)
    • Ferreira L, Teixeira-de-Lemos E, Pinto F, Parada B, Mega C, Vala H, et al. Effects of sitagliptin treatment on dysmetabolism, inflammation, and oxidative stress in an animal model of type 2 diabetes (ZDF rat). Mediators Inflamm. 2010;2010:592760. doi:10.1155/2010/592760.
    • (2010) Mediators Inflamm , vol.2010 , pp. 592760
    • Ferreira, L.1    Teixeira-de-Lemos, E.2    Pinto, F.3    Parada, B.4    Mega, C.5    Vala, H.6
  • 45
    • 84929494285 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitor decreases abdominal aortic aneurysm formation through GLP-1-dependent monocytic activity in mice
    • Lu HY, Huang CY, Shih CM, Chang WH, Tsai CS, Lin FY, et al. Dipeptidyl peptidase-4 inhibitor decreases abdominal aortic aneurysm formation through GLP-1-dependent monocytic activity in mice. PloS one. 2015;10(4): e0121077. doi:10.1371/journal. pone.0121077.
    • (2015) PloS one , vol.10 , Issue.4 , pp. e0121077
    • Lu, H.Y.1    Huang, C.Y.2    Shih, C.M.3    Chang, W.H.4    Tsai, C.S.5    Lin, F.Y.6
  • 46
    • 12144260853 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 can directly protect the heart against ischemia/reperfusion injury
    • Bose AK, Mocanu MM, Carr RD, Brand CL, Yellon DM. Glucagon-like peptide 1 can directly protect the heart against ischemia/reperfusion injury. Diabetes. 2005;54(1):146-51.
    • (2005) Diabetes , vol.54 , Issue.1 , pp. 146-151
    • Bose, A.K.1    Mocanu, M.M.2    Carr, R.D.3    Brand, C.L.4    Yellon, D.M.5
  • 47
    • 81855222104 scopus 로고    scopus 로고
    • Long-term dipeptidyl-peptidase 4 inhibition reduces atherosclerosis and inflammation via effects on monocyte recruitment and chemotaxis
    • Shah Z, Kampfrath T, Deiuliis JA, Zhong J, Pineda C, Ying Z, et al. Long-term dipeptidyl-peptidase 4 inhibition reduces atherosclerosis and inflammation via effects on monocyte recruitment and chemotaxis. Circulation. 2011; 124(21):2338-49. doi:10.1161/CIRCULATIONAHA.111.041418.
    • (2011) Circulation , vol.124 , Issue.21 , pp. 2338-2349
    • Shah, Z.1    Kampfrath, T.2    Deiuliis, J.A.3    Zhong, J.4    Pineda, C.5    Ying, Z.6
  • 48
    • 84868642036 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitor improves neovascularization by increasing circulating endothelial progenitor cells
    • Huang CY, Shih CM, Tsao NW, Lin YW, Huang PH, Wu SC, et al. Dipeptidyl peptidase-4 inhibitor improves neovascularization by increasing circulating endothelial progenitor cells. Br J Pharmacol. 2012;167(7):1506-19. doi:10.1111/j.1476-5381.2012.02102.x.
    • (2012) Br J Pharmacol , vol.167 , Issue.7 , pp. 1506-1519
    • Huang, C.Y.1    Shih, C.M.2    Tsao, N.W.3    Lin, Y.W.4    Huang, P.H.5    Wu, S.C.6
  • 49
    • 79959774265 scopus 로고    scopus 로고
    • Therapy in the early stage: Incretins
    • Cernea S, Raz I. Therapy in the early stage: incretins. Diabetes care. 2011;34 Suppl 2:S264-71. doi:10.2337/dc11-s223.
    • (2011) Diabetes care , vol.34 , pp. S264-S271
    • Cernea, S.1    Raz, I.2
  • 50
    • 84904391726 scopus 로고    scopus 로고
    • Dipeptidyl peptidase inhibition prevents diastolic dysfunction and reduces myocardial fibrosis in a mouse model of Western diet induced obesity
    • Bostick B, Habibi J, Ma L, Aroor A, Rehmer N, Hayden MR, et al. Dipeptidyl peptidase inhibition prevents diastolic dysfunction and reduces myocardial fibrosis in a mouse model of Western diet induced obesity. Metabolism: clinical and experimental. 2014;63(8):1000-11. doi:10.1016/j. metabol.2014.04.002.
    • (2014) Metabolism: Clinical and experimental , vol.63 , Issue.8 , pp. 1000-1011
    • Bostick, B.1    Habibi, J.2    Ma, L.3    Aroor, A.4    Rehmer, N.5    Hayden, M.R.6
  • 51
    • 84929483826 scopus 로고    scopus 로고
    • A DPP-4 inhibitor suppresses fibrosis and inflammation on experimental autoimmune myocarditis in mice
    • Hirakawa H, Zempo H, Ogawa M, Watanabe R, Suzuki J, Akazawa H, et al. A DPP-4 inhibitor suppresses fibrosis and inflammation on experimental autoimmune myocarditis in mice. PloS one. 2015;10(3):e0119360. doi:10.1371/journal. pone.0119360.
    • (2015) PloS one , vol.10 , Issue.3 , pp. e0119360
    • Hirakawa, H.1    Zempo, H.2    Ogawa, M.3    Watanabe, R.4    Suzuki, J.5    Akazawa, H.6
  • 52
    • 84897109133 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitor attenuates hepatic fibrosis via suppression ofactivated hepatic stellate cell in rats
    • KajiK, YoshijiH, IkenakaY, NoguchiR, AiharaY, DouharaA, etal. Dipeptidyl peptidase-4 inhibitor attenuates hepatic fibrosis via suppression ofactivated hepatic stellate cell in rats. J Gastroenterol. 2013. doi:10.1007A00535013-0783-4.
    • (2013) J Gastroenterol
    • Kaji, K.1    Yoshiji, H.2    Ikenaka, Y.3    Noguchi, R.4    Aihara, Y.5    Douhara, A.6
  • 53
    • 84901309585 scopus 로고    scopus 로고
    • Linagliptin-mediated DPP-4 inhibition ameliorates kidney fibrosis in streptozotocin-induced diabetic mice by inhibiting endothelial-to-mesenchymal transition in a therapeutic regimen
    • Kanasaki K, Shi S, Kanasaki M, He J, Nagai T, Nakamura Y, et al. Linagliptin-mediated DPP-4 inhibition ameliorates kidney fibrosis in streptozotocin-induced diabetic mice by inhibiting endothelial-to-mesenchymal transition in a therapeutic regimen. Diabetes. 2014;63(6):2120-31. doi:10.2337/db13-1029.
    • (2014) Diabetes , vol.63 , Issue.6 , pp. 2120-2131
    • Kanasaki, K.1    Shi, S.2    Kanasaki, M.3    He, J.4    Nagai, T.5    Nakamura, Y.6
  • 54
    • 84866718544 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV is a potential molecular biomarker in diabetic kidney disease
    • Sun AL, Deng JT, Guan GJ, Chen SH, Liu YT, Cheng J, et al Dipeptidyl peptidase-IV is a potential molecular biomarker in diabetic kidney disease. Diabetes & vascular disease research. 2012;9(4):301-8. doi:10.1177/1479164111434318.
    • (2012) Diabetes & vascular disease research , vol.9 , Issue.4 , pp. 301-308
    • Sun, A.L.1    Deng, J.T.2    Guan, G.J.3    Chen, S.H.4    Liu, Y.T.5    Cheng, J.6
  • 55
    • 0027497013 scopus 로고
    • Interferon-gamma induces dipeptidylpeptidase IV expression in human glomerular epithelial cells
    • Stefanovic V, Ardaillou N, Vlahovic P, Placier S, Ronco P, Ardaillou R. Interferon-gamma induces dipeptidylpeptidase IV expression in human glomerular epithelial cells. Immunology. 1993;80(3):465-70.
    • (1993) Immunology , vol.80 , Issue.3 , pp. 465-470
    • Stefanovic, V.1    Ardaillou, N.2    Vlahovic, P.3    Placier, S.4    Ronco, P.5    Ardaillou, R.6
  • 56
    • 34447103388 scopus 로고    scopus 로고
    • Increase in DPP-IV in the intestine, liver and kidney of the rat treated with high fat diet and streptozotocin
    • Yang J, Campitelli J, Hu G, Lin Y, Luo J, Xue C. Increase in DPP-IV in the intestine, liver and kidney of the rat treated with high fat diet and streptozotocin. Life sciences. 2007;81(4):272-9. doi:10.1016/j. lfs.2007.04.040.
    • (2007) Life sciences , vol.81 , Issue.4 , pp. 272-279
    • Yang, J.1    Campitelli, J.2    Hu, G.3    Lin, Y.4    Luo, J.5    Xue, C.6
  • 57
    • 84871706890 scopus 로고    scopus 로고
    • Role of GLP-1 and DPP-4 in diabetic nephropathy and cardiovascular disease
    • Panchapakesan U, Mather A, Pollock C. Role of GLP-1 and DPP-4 in diabetic nephropathy and cardiovascular disease. Clinical science. 2013;124(1):17-26. doi:10.1042/CS20120167.
    • (2013) Clinical science , vol.124 , Issue.1 , pp. 17-26
    • Panchapakesan, U.1    Mather, A.2    Pollock, C.3
  • 58
    • 54249132506 scopus 로고    scopus 로고
    • Diagnostic value of the aminopeptidase N, N-acetyl-beta-D-glucosaminidase and dipeptidylpeptidase IV in evaluating tubular dysfunction in patients with glomerulopathies
    • Mitic B, Lazarevic G, Vlahovic P, Rajic M, Stefanovic V. Diagnostic value of the aminopeptidase N, N-acetyl-beta-D-glucosaminidase and dipeptidylpeptidase IV in evaluating tubular dysfunction in patients with glomerulopathies. Renal failure. 2008;30(9):896-903. doi:10.1080/08860220802359048.
    • (2008) Renal failure , vol.30 , Issue.9 , pp. 896-903
    • Mitic, B.1    Lazarevic, G.2    Vlahovic, P.3    Rajic, M.4    Stefanovic, V.5
  • 59
    • 84862944057 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitor attenuates kidney injury in streptozotocin-induced diabetic rats
    • Liu WJ, Xie SH, Liu YN, Kim W, Jin HY, Park SK, et al. Dipeptidyl peptidase IV inhibitor attenuates kidney injury in streptozotocin-induced diabetic rats. J Pharmacol Exp Ther. 2012;340(2):248-55. doi:10.1124/jpet.111.186866.
    • (2012) J Pharmacol Exp Ther , vol.340 , Issue.2 , pp. 248-255
    • Liu, W.J.1    Xie, S.H.2    Liu, Y.N.3    Kim, W.4    Jin, H.Y.5    Park, S.K.6
  • 60
    • 84855611505 scopus 로고    scopus 로고
    • Diabetic nephropathy amelioration by a low-dose sitagliptin in an animal model of type 2 diabetes (Zucker diabetic fatty rat)
    • Mega C, de Lemos ET, Vala H, Fernandes R, Oliveira J, Mascarenhas-Melo F, et al. Diabetic nephropathy amelioration by a low-dose sitagliptin in an animal model of type 2 diabetes (Zucker diabetic fatty rat). Experimental diabetes research. 2011;2011:162092. doi:10.1155/2011/162092.
    • (2011) Experimental diabetes research , vol.2011 , pp. 162092
    • Mega, C.1    de Lemos, E.T.2    Vala, H.3    Fernandes, R.4    Oliveira, J.5    Mascarenhas-Melo, F.6
  • 62
    • 84884178268 scopus 로고    scopus 로고
    • Linagliptin: A thorough characterization beyond its clinical efficacy
    • Sortino MA, Sinagra T, Canonico PL. Linagliptin: a thorough characterization beyond its clinical efficacy. Frontiers in endocrinology. 2013;4:16. doi:10.3389/fendo.2013.00016.
    • (2013) Frontiers in endocrinology , vol.4 , pp. 16
    • Sortino, M.A.1    Sinagra, T.2    Canonico, P.L.3
  • 63
    • 84890476805 scopus 로고    scopus 로고
    • Linagliptin lowers albuminuria on top of recommended standard treatment in patients with type 2 diabetes and renal dysfunction
    • Groop PH, Cooper ME, Perkovic V, Emser A, Woerle HJ, von Eynatten M. Linagliptin lowers albuminuria on top of recommended standard treatment in patients with type 2 diabetes and renal dysfunction. Diabetes care. 2013;36(11):3460-8. doi:10.2337/dc13-0323.
    • (2013) Diabetes care , vol.36 , Issue.11 , pp. 3460-3468
    • Groop, P.H.1    Cooper, M.E.2    Perkovic, V.3    Emser, A.4    Woerle, H.J.5    von Eynatten, M.6
  • 64
    • 80051653327 scopus 로고    scopus 로고
    • A randomized, open-label, crossover study evaluating the effect of food on the relative bioavailability of linagliptin in healthy subjects
    • Graefe-Mody U, Giessmann T, Ring A, Iovino M, Woerle HJ. A randomized, open-label, crossover study evaluating the effect of food on the relative bioavailability of linagliptin in healthy subjects. Clinical therapeutics. 2011; 33(8):1096-103. doi:10.1016/j. clinthera.2011.07.005.
    • (2011) Clinical therapeutics , vol.33 , Issue.8 , pp. 1096-1103
    • Graefe-Mody, U.1    Giessmann, T.2    Ring, A.3    Iovino, M.4    Woerle, H.J.5
  • 65
    • 84904172623 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitor protects against renal interstitial fibrosis in a mouse model of ureteral obstruction
    • Min HS, Kim JE, Lee MH, Song HK, Kang YS, Lee MJ, et al. Dipeptidyl peptidase IV inhibitor protects against renal interstitial fibrosis in a mouse model of ureteral obstruction. Lab Invest. 2014;94(6):598-607. doi:10.1038/labinvest.2014.50.
    • (2014) Lab Invest , vol.94 , Issue.6 , pp. 598-607
    • Min, H.S.1    Kim, J.E.2    Lee, M.H.3    Song, H.K.4    Kang, Y.S.5    Lee, M.J.6
  • 66
    • 14844337071 scopus 로고    scopus 로고
    • Transforming growth factor-beta and Smad signalling in kidney diseases
    • Wang W, Koka V, Lan HY. Transforming growth factor-beta and Smad signalling in kidney diseases. Nephrology. 2005;10(1):48-56. doi:10.1111/j.1440-1797.2005.00334.x.
    • (2005) Nephrology , vol.10 , Issue.1 , pp. 48-56
    • Wang, W.1    Koka, V.2    Lan, H.Y.3
  • 67
    • 0029061401 scopus 로고
    • Molecular regulation of atrioventricular valvuloseptal morphogenesis
    • Eisenberg LM, Markwald RR. Molecular regulation of atrioventricular valvuloseptal morphogenesis. Circulation research. 1995;77(1):1-6.
    • (1995) Circulation research , vol.77 , Issue.1 , pp. 1-6
    • Eisenberg, L.M.1    Markwald, R.R.2
  • 68
    • 80052851503 scopus 로고    scopus 로고
    • Role of endothelial-mesenchymal transition (EndoMT) in the pathogenesis of fibrotic disorders
    • Piera-Velazquez S, Li Z, Jimenez SA. Role of endothelial-mesenchymal transition (EndoMT) in the pathogenesis of fibrotic disorders. The American journal of pathology. 2011;179(3):1074-80. doi:10.1016/j. ajpath.2011.06.001.
    • (2011) The American journal of pathology , vol.179 , Issue.3 , pp. 1074-1080
    • Piera-Velazquez, S.1    Li, Z.2    Jimenez, S.A.3
  • 70
    • 33750712380 scopus 로고    scopus 로고
    • Renal fibroblasts and myofibroblasts in chronic kidney disease
    • Strutz F, Zeisberg M. Renal fibroblasts and myofibroblasts in chronic kidney disease. Journal of the American Society of Nephrology: JASN. 2006;17(11): 2992-8. doi:10.1681/ASN.2006050420.
    • (2006) Journal of the American Society of Nephrology: JASN , vol.17 , Issue.11 , pp. 2992-2998
    • Strutz, F.1    Zeisberg, M.2
  • 71
    • 84906322326 scopus 로고    scopus 로고
    • Increased concentration of circulating angiogenesis and nitric oxide inhibitors induces endothelial to mesenchymal transition and myocardial fibrosis in patients with chronic kidney disease
    • Charytan DM, Padera R, Helfand AM, Zeisberg M, Xu X, Liu X, et al. Increased concentration of circulating angiogenesis and nitric oxide inhibitors induces endothelial to mesenchymal transition and myocardial fibrosis in patients with chronic kidney disease. Int J Cardiol. 2014;176(1):99-109. doi:10.1016/j. ijcard.2014.06.062.
    • (2014) Int J Cardiol , vol.176 , Issue.1 , pp. 99-109
    • Charytan, D.M.1    Padera, R.2    Helfand, A.M.3    Zeisberg, M.4    Xu, X.5    Liu, X.6
  • 72
    • 35948945337 scopus 로고    scopus 로고
    • Discovery of endothelial to mesenchymal transition as a source for carcinoma-associated fibroblasts
    • Zeisberg EM, Potenta S, Xie L, Zeisberg M, Kalluri R. Discovery of endothelial to mesenchymal transition as a source for carcinoma-associated fibroblasts. Cancer Res. 2007;67(21):10123-8.
    • (2007) Cancer Res , vol.67 , Issue.21 , pp. 10123-10128
    • Zeisberg, E.M.1    Potenta, S.2    Xie, L.3    Zeisberg, M.4    Kalluri, R.5
  • 74
    • 55249126800 scopus 로고    scopus 로고
    • The role of endothelial-to-mesenchymal transition in cancer progression
    • Potenta S, Zeisberg E, Kalluri R. The role of endothelial-to-mesenchymal transition in cancer progression. Br J Cancer. 2008;99(9):1375-9.
    • (2008) Br J Cancer , vol.99 , Issue.9 , pp. 1375-1379
    • Potenta, S.1    Zeisberg, E.2    Kalluri, R.3
  • 75
    • 84924608904 scopus 로고    scopus 로고
    • Endocardial fibroelastosis is caused by aberrant endothelial to mesenchymal transition
    • Xu X, Friehs I, Zhong Hu T, Melnychenko I, Tampe B, Alnour F, et al. Endocardial fibroelastosis is caused by aberrant endothelial to mesenchymal transition. Circulation research. 2015;116(5):857-66. doi:10.1161/CIRCRESAHA.116.305629.
    • (2015) Circulation research , vol.116 , Issue.5 , pp. 857-866
    • Xu, X.1    Friehs, I.2    Zhong Hu, T.3    Melnychenko, I.4    Tampe, B.5    Alnour, F.6
  • 76
    • 84942088525 scopus 로고    scopus 로고
    • Epigenetic balance of aberrant Rasal1 promoter methylation and hydroxymethylation regulates cardiac fibrosis
    • Xu X, Tan X, Tampe B, Nyamsuren G, Liu X, Maier LS, et al. Epigenetic balance of aberrant Rasal1 promoter methylation and hydroxymethylation regulates cardiac fibrosis. Cardiovasc Res. 2015;105(3):279-91. doi:10.1093/cvr/cvv015.
    • (2015) Cardiovasc Res , vol.105 , Issue.3 , pp. 279-291
    • Xu, X.1    Tan, X.2    Tampe, B.3    Nyamsuren, G.4    Liu, X.5    Maier, L.S.6
  • 77
    • 84936802418 scopus 로고    scopus 로고
    • Snail is a direct target of hypoxia-inducible factor 1alpha (HIF1alpha) in hypoxia-induced endothelial to mesenchymal transition of human coronary endothelial cells
    • Xu X, Tan X, Tampe B, Sanchez E, Zeisberg M, Zeisberg EM. Snail is a direct target of hypoxia-inducible factor 1alpha (HIF1alpha) in hypoxia-induced endothelial to mesenchymal transition of human coronary endothelial cells. J Biol Chem. 2015;290(27):16653-64. doi:10.1074/jbc. M115.636944.
    • (2015) J Biol Chem , vol.290 , Issue.27 , pp. 16653-16664
    • Xu, X.1    Tan, X.2    Tampe, B.3    Sanchez, E.4    Zeisberg, M.5    Zeisberg, E.M.6
  • 78
    • 84940767662 scopus 로고    scopus 로고
    • Evidence for antifibrotic incretin-independent effects of the DPP-4 inhibitor linagliptin
    • Zeisberg M, Zeisberg EM. Evidence for antifibrotic incretin-independent effects of the DPP-4 inhibitor linagliptin. Kidney international. 2015;88(3): 429-31. doi:10.1038/ki.2015.175.
    • (2015) Kidney international , vol.88 , Issue.3 , pp. 429-431
    • Zeisberg, M.1    Zeisberg, E.M.2
  • 79
    • 84940791235 scopus 로고    scopus 로고
    • Interactions of DPP-4 and integrin beta1 influences endothelial-to-mesenchymal transition
    • Shi S, Srivastava SP, Kanasaki M, He J, Kitada M, Nagai T, et al. Interactions of DPP-4 and integrin beta1 influences endothelial-to-mesenchymal transition. Kidney international. 2015;88(3):479-89. doi:10.1038/ki.2015.103.
    • (2015) Kidney international , vol.88 , Issue.3 , pp. 479-489
    • Shi, S.1    Srivastava, S.P.2    Kanasaki, M.3    He, J.4    Kitada, M.5    Nagai, T.6
  • 80
    • 80053335949 scopus 로고    scopus 로고
    • Extracellular matrix receptors in branched organs
    • Pozzi A, Zent R. Extracellular matrix receptors in branched organs. Curr Opin Cell Biol. 2011;23(5):547-53. doi:10.1016/j. ceb.2011.04.003.
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.5 , pp. 547-553
    • Pozzi, A.1    Zent, R.2
  • 81
    • 0348198389 scopus 로고    scopus 로고
    • Integrins: Sensors of extracellular matrix and modulators of cell function, 72025
    • Pozzi A, Zent R. Integrins: sensors of extracellular matrix and modulators of cell function. Nephron Exp Nephrol. 2003;94(3):e77-84. doi:72025.
    • (2003) Nephron Exp Nephrol , vol.94 , Issue.3 , pp. e77-e84
    • Pozzi, A.1    Zent, R.2
  • 82
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell. 2002; 110(6):673-87.
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 84
    • 84935418112 scopus 로고    scopus 로고
    • Structural basis of blocking integrin activation and deactivation for anti-inflammation
    • Park EJ, Yuki Y, Kiyono H, Shimaoka M. Structural basis of blocking integrin activation and deactivation for anti-inflammation. J Biomed Sci. 2015;22:51. doi:10.1186/s12929-015-0159-6.
    • (2015) J Biomed Sci , vol.22 , pp. 51
    • Park, E.J.1    Yuki, Y.2    Kiyono, H.3    Shimaoka, M.4
  • 86
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis ofintegrin regulation and signaling
    • Luo BH, Carman CV, Springer TA. Structural basis ofintegrin regulation and signaling. Annu Rev Immunol. 2007;25:619-47. doi:10.1146/annurev. immunol.25.022106.141618.
    • (2007) Annu Rev Immunol , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.A.3
  • 87
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • Arnaout MA, Goodman SL, Xiong JP. Structure and mechanics of integrin-based cell adhesion. Curr Opin Cell Biol. 2007;19(5):495-507. doi:10.1016/j. ceb.2007.08.002.
    • (2007) Curr Opin Cell Biol , vol.19 , Issue.5 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.P.3
  • 88
    • 33746531062 scopus 로고    scopus 로고
    • Glomerular injury is exacerbated in diabetic integrin alpha1-null mice
    • Zent R, Yan X, Su Y, Hudson BG, Borza DB, Moeckel GW, et al. Glomerular injury is exacerbated in diabetic integrin alpha1-null mice. Kidney international. 2006;70(3):460-70. doi:10.1038/sj. ki.5000359.
    • (2006) Kidney international , vol.70 , Issue.3 , pp. 460-470
    • Zent, R.1    Yan, X.2    Su, Y.3    Hudson, B.G.4    Borza, D.B.5    Moeckel, G.W.6
  • 89
    • 34247626764 scopus 로고    scopus 로고
    • Integrin alpha1beta1 controls reactive oxygen species synthesis by negatively regulating epidermal growth factor receptor-mediated Rac activation
    • Chen X, Abair TD, Ibanez MR, Su Y, Frey MR, Dise RS, et al. Integrin alpha1beta1 controls reactive oxygen species synthesis by negatively regulating epidermal growth factor receptor-mediated Rac activation. Mol Cell Biol. 2007;27(9):3313-26. doi:10.1128/MCB.01476-06.
    • (2007) Mol Cell Biol , vol.27 , Issue.9 , pp. 3313-3326
    • Chen, X.1    Abair, T.D.2    Ibanez, M.R.3    Su, Y.4    Frey, M.R.5    Dise, R.S.6
  • 90
    • 77957334362 scopus 로고    scopus 로고
    • Transforming growth factor--beta}1 induces Smad3-dependent-beta}1 integrin gene expression in epithelial-to-mesenchymal transition during chronic tubulointerstitial fibrosis
    • Yeh YC, Wei WC, Wang YK, Lin SC, Sung JM, Tang MJ. Transforming growth factor--beta}1 induces Smad3-dependent-beta}1 integrin gene expression in epithelial-to-mesenchymal transition during chronic tubulointerstitial fibrosis. The American journal of pathology. 2010;177(4):1743-54. doi:10.2353/ajpath.2010.091183.
    • (2010) The American journal of pathology , vol.177 , Issue.4 , pp. 1743-1754
    • Yeh, Y.C.1    Wei, W.C.2    Wang, Y.K.3    Lin, S.C.4    Sung, J.M.5    Tang, M.J.6
  • 91
    • 84924026310 scopus 로고    scopus 로고
    • Cyclic stretch-induced TGF-beta1 and fibronectin expression is mediated by beta1-integrin through c-Src-and STAT3-dependent pathways in renal epithelial cells
    • Hamzeh MT, Sridhara R, Alexander LD. Cyclic stretch-induced TGF-beta1 and fibronectin expression is mediated by beta1-integrin through c-Src-and STAT3-dependent pathways in renal epithelial cells. American journal of physiology Renal physiology. 2015;308(5):F425-36. doi:10.1152/ajprenal.00589.2014.
    • (2015) American journal of physiology Renal physiology , vol.308 , Issue.5 , pp. F425-F436
    • Hamzeh, M.T.1    Sridhara, R.2    Alexander, L.D.3
  • 92
    • 33947730444 scopus 로고    scopus 로고
    • Effect of rosiglitazone on integrin beta1 expression and apoptosis of proximal tubular cell exposed to high glucose
    • Tang XH, Huang SM, Tan SQ, Ma YL. Effect of rosiglitazone on integrin beta1 expression and apoptosis of proximal tubular cell exposed to high glucose. Sichuan Da Xue Xue Bao Yi Xue Ban. 2007;38(2):291-4.
    • (2007) Sichuan Da Xue Xue Bao Yi Xue Ban , vol.38 , Issue.2 , pp. 291-294
    • Tang, X.H.1    Huang, S.M.2    Tan, S.Q.3    Ma, Y.L.4
  • 93
    • 0034758802 scopus 로고    scopus 로고
    • Coexpressed nitric oxide synthase and apical beta(1) integrins influence tubule cell adhesion after cytokine-induced injury
    • Glynne PA, Picot J, Evans TJ. Coexpressed nitric oxide synthase and apical beta(1) integrins influence tubule cell adhesion after cytokine-induced injury. Journal of the American Society of Nephrology: JASN. 2001;12(11):2370-83.
    • (2001) Journal of the American Society of Nephrology: JASN , vol.12 , Issue.11 , pp. 2370-2383
    • Glynne, P.A.1    Picot, J.2    Evans, T.J.3
  • 94
    • 84896931147 scopus 로고    scopus 로고
    • The integrin beta1 subunit regulates paracellular permeability of kidney proximal tubule cells
    • Elias BC, Mathew S, Srichai MB, Palamuttam R, Bulus N, Mernaugh G, et al. The integrin beta1 subunit regulates paracellular permeability of kidney proximal tubule cells. J Biol Chem. 2014;289(12):8532-44. doi:10.1074/jbc. M113.526509.
    • (2014) J Biol Chem , vol.289 , Issue.12 , pp. 8532-8544
    • Elias, B.C.1    Mathew, S.2    Srichai, M.B.3    Palamuttam, R.4    Bulus, N.5    Mernaugh, G.6
  • 96
    • 84861376261 scopus 로고    scopus 로고
    • Integrin structure and function
    • In: Zent R, Pozzi A, editors. New York: Springer
    • Srichai M, Zent R. Integrin structure and function. In: Zent R, Pozzi A, editors. Cell-Extracellular Matrix Interactions in Cancer. New York: Springer; 2010. p. 19-41.
    • (2010) Cell-Extracellular Matrix Interactions in Cancer , pp. 19-41
    • Srichai, M.1    Zent, R.2
  • 97
    • 84899092336 scopus 로고    scopus 로고
    • Down-regulation of integrin beta1 and focal adhesion kinase in renal glomeruli under various hemodynamic conditions
    • Yuan X, Wang W, Wang J, Yin X, Zhai X, Wang L, et al. Down-regulation of integrin beta1 and focal adhesion kinase in renal glomeruli under various hemodynamic conditions. PloS one. 2014;9(4):e94212. doi:10.1371/journal. pone.0094212.
    • (2014) PloS one , vol.9 , Issue.4 , pp. e94212
    • Yuan, X.1    Wang, W.2    Wang, J.3    Yin, X.4    Zhai, X.5    Wang, L.6
  • 98
    • 69449108113 scopus 로고    scopus 로고
    • Loss of beta1 integrin in mouse fibroblasts results in resistance to skin scleroderma in a mouse model
    • Liu S, Kapoor M, Denton CP, Abraham DJ, Leask A. Loss of beta1 integrin in mouse fibroblasts results in resistance to skin scleroderma in a mouse model. Arthritis and rheumatism. 2009;60(9):2817-21. doi:10.1002/art.24801.
    • (2009) Arthritis and rheumatism , vol.60 , Issue.9 , pp. 2817-2821
    • Liu, S.1    Kapoor, M.2    Denton, C.P.3    Abraham, D.J.4    Leask, A.5
  • 99
    • 23044510616 scopus 로고    scopus 로고
    • CD26 regulates p38 mitogen-activated protein kinase-dependent phosphorylation ofintegrin beta1, adhesion to extracellular matrix, and tumorigenicity of T-anaplastic large cell lymphoma Karpas 299
    • Sato T, Yamochi T, Yamochi T, Aytac U, Ohnuma K, McKee KS, et al. CD26 regulates p38 mitogen-activated protein kinase-dependent phosphorylation ofintegrin beta1, adhesion to extracellular matrix, and tumorigenicity of T-anaplastic large cell lymphoma Karpas 299. Cancer Res. 2005;65(15):6950-6. doi:10.1158/0008-5472. CAN-05-0647.
    • (2005) Cancer Res , vol.65 , Issue.15 , pp. 6950-6956
    • Sato, T.1    Yamochi, T.2    Yamochi, T.3    Aytac, U.4    Ohnuma, K.5    McKee, K.S.6
  • 100
    • 78650018824 scopus 로고    scopus 로고
    • Conversion of vascular endothelial cells into multipotent stem-like cells
    • Medici D, Shore EM, Lounev VY, Kaplan FS, Kalluri R, Olsen BR. Conversion of vascular endothelial cells into multipotent stem-like cells. Nat Med. 2010; 16(12):1400-6. doi:10.1038/nm.2252.
    • (2010) Nat Med , vol.16 , Issue.12 , pp. 1400-1406
    • Medici, D.1    Shore, E.M.2    Lounev, V.Y.3    Kaplan, F.S.4    Kalluri, R.5    Olsen, B.R.6
  • 101
    • 84899528177 scopus 로고    scopus 로고
    • N-acetyl-seryl-aspartyl-lysyl-proline inhibits diabetes-associated kidney fibrosis and endothelial-Mesenchymal transition
    • Nagai T, Kanasaki M, Srivastava S, Nakamura Y, Ishigaki Y, Kitada M et al. N-acetyl-seryl-aspartyl-lysyl-proline inhibits diabetes-associated kidney fibrosis and endothelial-Mesenchymal transition. BioMed research international. 2014;2014. doi:10.1155/2014/696475.
    • (2014) BioMed research international
    • Nagai, T.1    Kanasaki, M.2    Srivastava, S.3    Nakamura, Y.4    Ishigaki, Y.5    Kitada, M.6
  • 102
    • 84884853106 scopus 로고    scopus 로고
    • MicroRNAs in kidney fibrosis and diabetic nephropathy: Roles on EMT and EndMT
    • Srivastava SP, Koya D, Kanasaki K. MicroRNAs in kidney fibrosis and diabetic nephropathy: roles on EMT and EndMT. BioMed research international. 2013;2013:125469. doi:10.1155/2013/125469.
    • (2013) BioMed research international , vol.2013 , pp. 125469
    • Srivastava, S.P.1    Koya, D.2    Kanasaki, K.3
  • 103
    • 84871676561 scopus 로고    scopus 로고
    • FGF regulates TGF-beta signaling and endothelial-to-mesenchymal transition via control of let-7 miRNA expression
    • Chen PY, Qin L, Barnes C, Charisse K, Yi T, Zhang X, et al. FGF regulates TGF-beta signaling and endothelial-to-mesenchymal transition via control of let-7 miRNA expression. Cell reports. 2012;2(6):1684-96. doi:10.1016/j. celrep.2012.10.021.
    • (2012) Cell reports , vol.2 , Issue.6 , pp. 1684-1696
    • Chen, P.Y.1    Qin, L.2    Barnes, C.3    Charisse, K.4    Yi, T.5    Zhang, X.6
  • 106
    • 80052596763 scopus 로고    scopus 로고
    • MicroRNA-23 restricts cardiac valve formation by inhibiting Has2 and extracellular hyaluronic acid production
    • Lagendijk AK, Goumans MJ, Burkhard SB, Bakkers J. MicroRNA-23 restricts cardiac valve formation by inhibiting Has2 and extracellular hyaluronic acid production. Circulation research. 2011;109(6):649-57. doi:10.1161/CIRCRESAHA.111.247635.
    • (2011) Circulation research , vol.109 , Issue.6 , pp. 649-657
    • Lagendijk, A.K.1    Goumans, M.J.2    Burkhard, S.B.3    Bakkers, J.4
  • 107
    • 84927739773 scopus 로고    scopus 로고
    • Skin fibrosis. Identification and isolation of a dermal lineage with intrinsic fibrogenic potential
    • Rinkevich Y, Walmsley GG, Hu MS, Maan ZN, Newman AM, Drukker M, et al. Skin fibrosis. Identification and isolation of a dermal lineage with intrinsic fibrogenic potential. Science. 2015;348(6232):aaa2151. doi:10.1126/science. aaa2151.
    • (2015) Science , vol.348 , Issue.6232 , pp. 2151
    • Rinkevich, Y.1    Walmsley, G.G.2    Hu, M.S.3    Maan, Z.N.4    Newman, A.M.5    Drukker, M.6
  • 108
    • 84906957817 scopus 로고    scopus 로고
    • Significance ofvascular dipeptidyl peptidase-4 inhibition on vascular protection in Zucker diabetic fatty rats
    • Takai S, Sakonjo H, Jin D. Significance ofvascular dipeptidyl peptidase-4 inhibition on vascular protection in Zucker diabetic fatty rats. J Pharmacol Sci.2014;125(4):386-93.
    • (2014) J Pharmacol Sci , vol.125 , Issue.4 , pp. 386-393
    • Takai, S.1    Sakonjo, H.2    Jin, D.3
  • 109
    • 67651024959 scopus 로고    scopus 로고
    • Localization of CD26/DPPIV in nucleus and its nuclear translocation enhanced by anti-CD26 monoclonal antibody with anti-tumor effect
    • Yamada K, Hayashi M, Du W, Ohnuma K, Sakamoto M, Morimoto C, et al. Localization of CD26/DPPIV in nucleus and its nuclear translocation enhanced by anti-CD26 monoclonal antibody with anti-tumor effect. Cancer Cell Int. 2009;9:17. doi:10.1186/1475-2867-9-17.
    • (2009) Cancer Cell Int , vol.9 , pp. 17
    • Yamada, K.1    Hayashi, M.2    Du, W.3    Ohnuma, K.4    Sakamoto, M.5    Morimoto, C.6
  • 110
    • 84958890242 scopus 로고    scopus 로고
    • Linagliptin but not Sitagliptin inhibited transforming growth factor-β2-induced endothelial DPP-4 activity and the endothelial-mesenchymal transition
    • Jan 27. S0006-291X(16)30154-1
    • Shi S, Kanasaki K, Koya D. Linagliptin but not Sitagliptin inhibited transforming growth factor-β2-induced endothelial DPP-4 activity and the endothelial-mesenchymal transition. Biochem Biophys Res Commun. 2016 Jan 27. pii: S0006-291X(16)30154-1. doi:10.1016/j. bbrc.2016.01.154.
    • (2016) Biochem Biophys Res Commun
    • Shi, S.1    Kanasaki, K.2    Koya, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.