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Volumn 132, Issue 4, 2018, Pages 489-507

Correction: The role of renal dipeptidyl peptidase-4 in kidney disease: Renal effects of dipeptidyl peptidase-4 inhibitors with a focus on linagliptin (Clinical Science (2018) 132:4 (489–507) DOI: 10.1042/CS20180031);The role of renal dipeptidyl peptidase-4 in kidney disease: Renal effects of dipeptidyl peptidase-4 inhibitors with a focus on linagliptin

Author keywords

[No Author keywords available]

Indexed keywords

ANTIDIABETIC AGENT; DIPEPTIDYL PEPTIDASE IV; DIPEPTIDYL PEPTIDASE IV INHIBITOR; LINAGLIPTIN;

EID: 85045643924     PISSN: 01435221     EISSN: 14708736     Source Type: Journal    
DOI: 10.1042/CS20180031_COR     Document Type: Erratum
Times cited : (80)

References (158)
  • 1
    • 84907573731 scopus 로고    scopus 로고
    • 8th edn, International Diabetes Federation, Brussels, Belgium
    • International Diabetes Federation (2017) IDF Diabetes Atlas, 8th edn, International Diabetes Federation, Brussels, Belgium, http://www.diabetesatlas.org/resources/2017-atlas.html
    • (2017) IDF Diabetes Atlas
  • 2
    • 85184349984 scopus 로고    scopus 로고
    • U.S. Dept of Health and Human Services, Atlanta, GA
    • Centers for Disease Control and Prevention (2017) National Diabetes Statistics Report, 2017, Centers for Disease Control and Prevention, U.S. Dept of Health and Human Services, Atlanta, GA, https://www.cdc.gov/diabetes/pdfs/data/statistics/national-diabetes-statistics-report.pdf
    • (2017) National Diabetes Statistics Report, 2017, Centers for Disease Control and Prevention
  • 3
    • 84946761555 scopus 로고    scopus 로고
    • Changing epidemiology of type 2 diabetes mellitus and associated chronic kidney disease
    • Thomas, M.C., Cooper, M.E. and Zimmet, P. (2016) Changing epidemiology of type 2 diabetes mellitus and associated chronic kidney disease. Nat. Rev. Nephrol. 12, 73-81, https://doi.org/10.1038/nrneph.2015.173
    • (2016) Nat. Rev. Nephrol , vol.12 , pp. 73-81
    • Thomas, M.C.1    Cooper, M.E.2    Zimmet, P.3
  • 4
    • 84867497463 scopus 로고    scopus 로고
    • KDOQI Clinical Practice Guideline for Diabetes and CKD: 2012 update
    • National Kidney Foundation (2012) KDOQI Clinical Practice Guideline for Diabetes and CKD: 2012 update. Am. J. Kidney Dis. 60, 850-886, https://doi.org/10.1053/j.ajkd.2012.07.005
    • (2012) Am. J. Kidney Dis , vol.60 , pp. 850-886
  • 5
    • 0032511583 scopus 로고    scopus 로고
    • Intensive blood-glucose control with sulphonylureas or insulin compared with conventional treatment and risk of complications in patients with type 2 diabetes (UKPDS 33)
    • UK Prospective Diabetes Study (UKPDS) Group (1998) Intensive blood-glucose control with sulphonylureas or insulin compared with conventional treatment and risk of complications in patients with type 2 diabetes (UKPDS 33). . Lancet 352, 837-853, https://doi.org/10.1016/S0140-6736(98)07019-6
    • (1998) . Lancet , vol.352 , pp. 837-853
  • 6
    • 85016474227 scopus 로고    scopus 로고
    • Effects of intensive glucose control on microvascular outcomes in patients with type 2 diabetes: a meta-analysis of individual participant data from randomised controlled trials
    • Zoungas, S., Arima, H., Gerstein, H.C., Holman, R.R., Woodward, M., Reaven, P. et al. (2017) Effects of intensive glucose control on microvascular outcomes in patients with type 2 diabetes: a meta-analysis of individual participant data from randomised controlled trials. Lancet Diabetes Endocrinol. 5, 431-437, https://doi.org/10.1016/S2213-8587(17)30104-3
    • (2017) Lancet Diabetes Endocrinol , vol.5 , pp. 431-437
    • Zoungas, S.1    Arima, H.2    Gerstein, H.C.3    Holman, R.R.4    Woodward, M.5    Reaven, P.6
  • 7
    • 77955585592 scopus 로고    scopus 로고
    • Effect of intensive treatment of hyperglycaemia on microvascular outcomes in type 2 diabetes: an analysis of the ACCORD randomised trial
    • Ismail-Beigi, F., Craven, T., Banerji, M.A., Basile, J., Calles, J., Cohen, R.M. et al. (2010) Effect of intensive treatment of hyperglycaemia on microvascular outcomes in type 2 diabetes: an analysis of the ACCORD randomised trial. Lancet 376, 419-430, https://doi.org/10.1016/S0140-6736(10)60576-4
    • (2010) Lancet , vol.376 , pp. 419-430
    • Ismail-Beigi, F.1    Craven, T.2    Banerji, M.A.3    Basile, J.4    Calles, J.5    Cohen, R.M.6
  • 8
    • 45149133036 scopus 로고    scopus 로고
    • Intensive blood glucose control and vascular outcomes in patients with type 2 diabetes
    • Patel, A., MacMahon, S., Chalmers, J., Neal, B., Billot, L., Woodward, M. et al. (2008) Intensive blood glucose control and vascular outcomes in patients with type 2 diabetes. N. Engl. J. Med. 358, 2560-2572, https://doi.org/10.1056/NEJMoa0802987
    • (2008) N. Engl. J. Med , vol.358 , pp. 2560-2572
    • Patel, A.1    Macmahon, S.2    Chalmers, J.3    Neal, B.4    Billot, L.5    Woodward, M.6
  • 9
    • 84874662499 scopus 로고    scopus 로고
    • Intensive glucose control improves kidney outcomes in patients with type 2 diabetes
    • Perkovic, V., Heerspink, H.L., Chalmers, J., Woodward, M., Jun, M., Li, Q. et al. (2013) Intensive glucose control improves kidney outcomes in patients with type 2 diabetes. Kidney Int. 83, 517-523, https://doi.org/10.1038/ki.2012.401
    • (2013) Kidney Int , vol.83 , pp. 517-523
    • Perkovic, V.1    Heerspink, H.L.2    Chalmers, J.3    Woodward, M.4    Jun, M.5    Li, Q.6
  • 10
    • 84964733198 scopus 로고    scopus 로고
    • Long-term benefits of intensive glucose control for preventing end-stage kidney disease: ADVANCE-ON
    • Wong, M.G., Perkovic, V., Chalmers, J., Woodward, M., Li, Q., Cooper, M.E. et al. (2016) Long-term benefits of intensive glucose control for preventing end-stage kidney disease: ADVANCE-ON. Diabetes Care 39, 694-700, https://doi.org/10.2337/dc15-2322
    • (2016) Diabetes Care , vol.39 , pp. 694-700
    • Wong, M.G.1    Perkovic, V.2    Chalmers, J.3    Woodward, M.4    Li, Q.5    Cooper, M.E.6
  • 12
    • 0035922447 scopus 로고    scopus 로고
    • Renoprotective effect of the angiotensin-receptor antagonist irbesartan in patients with nephropathy due to type 2 diabetes
    • Lewis, E.J., Hunsicker, L.G., Clarke, W.R., Berl, T., Pohl, M.A., Lewis, J.B. et al. (2001) Renoprotective effect of the angiotensin-receptor antagonist irbesartan in patients with nephropathy due to type 2 diabetes. N. Engl. J. Med. 345, 851-860, https://doi.org/10.1056/NEJMoa011303
    • (2001) N. Engl. J. Med , vol.345 , pp. 851-860
    • Lewis, E.J.1    Hunsicker, L.G.2    Clarke, W.R.3    Berl, T.4    Pohl, M.A.5    Lewis, J.B.6
  • 13
    • 0035922441 scopus 로고    scopus 로고
    • Effects of losartan on renal and cardiovascular outcomes in patients with type 2 diabetes and nephropathy
    • Brenner, B.M., Cooper, M.E., de Zeeuw, D., Keane, W.F., Mitch, W.E., Parving, H.H. et al. (2001) Effects of losartan on renal and cardiovascular outcomes in patients with type 2 diabetes and nephropathy. N. Engl. J. Med. 345, 861-869, https://doi.org/10.1056/NEJMoa011161
    • (2001) N. Engl. J. Med , vol.345 , pp. 861-869
    • Brenner, B.M.1    Cooper, M.E.2    De Zeeuw, D.3    Keane, W.F.4    Mitch, W.E.5    Parving, H.H.6
  • 14
    • 84965028768 scopus 로고    scopus 로고
    • Unmet need in diabetic nephropathy: failed drugs or trials?
    • de Zeeuw, D. and Heerspink, H.J. (2016) Unmet need in diabetic nephropathy: failed drugs or trials? Lancet Diabetes Endocrinol. 4, 638-640, https://doi.org/10.1016/S2213-8587(16)30045-6
    • (2016) Lancet Diabetes Endocrinol , vol.4 , pp. 638-640
    • De Zeeuw, D.1    Heerspink, H.J.2
  • 15
    • 84979895487 scopus 로고    scopus 로고
    • Empagliflozin and progression of kidney disease in type 2 diabetes
    • Wanner, C., Inzucchi, S.E. and Zinman, B. (2016) Empagliflozin and progression of kidney disease in type 2 diabetes. N. Engl. J. Med. 375, 323-334, https://doi.org/10.1056/NEJMoa1515920
    • (2016) N. Engl. J. Med , vol.375 , pp. 323-334
    • Wanner, C.1    Inzucchi, S.E.2    Zinman, B.3
  • 16
    • 85023777061 scopus 로고    scopus 로고
    • Canagliflozin and cardiovascular and renal events in type 2 diabetes
    • Neal, B., Perkovic, V., Mahaffey, K.W., de Zeeuw, D., Fulcher, G., Erondu, N. et al. (2017) Canagliflozin and cardiovascular and renal events in type 2 diabetes. N. Engl. J. Med. 377, 644-657, https://doi.org/10.1056/NEJMoa1611925
    • (2017) N. Engl. J. Med , vol.377 , pp. 644-657
    • Neal, B.1    Perkovic, V.2    Mahaffey, K.W.3    De Zeeuw, D.4    Fulcher, G.5    Erondu, N.6
  • 17
    • 84919999219 scopus 로고    scopus 로고
    • Management of hyperglycemia in type 2 diabetes, 2015: a patient-centered approach: update to a position statement of the American Diabetes Association and the European Association for the Study of Diabetes
    • Inzucchi, S.E., Bergenstal, R.M., Buse, J.B., Diamant, M., Ferrannini, E., Nauck, M. et al. (2015) Management of hyperglycemia in type 2 diabetes, 2015: a patient-centered approach: update to a position statement of the American Diabetes Association and the European Association for the Study of Diabetes. Diabetes Care 38, 140-149, https://doi.org/10.2337/dc14-2441
    • (2015) Diabetes Care , vol.38 , pp. 140-149
    • Inzucchi, S.E.1    Bergenstal, R.M.2    Buse, J.B.3    Diamant, M.4    Ferrannini, E.5    Nauck, M.6
  • 18
    • 84957629803 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 and kidney fibrosis in diabetes
    • Shi, S., Koya, D. and Kanasaki, K. (2016) Dipeptidyl peptidase-4 and kidney fibrosis in diabetes. Fibrogenesis Tissue Repair 9, 1, https://doi.org/10.1186/s13069-016-0038-0
    • (2016) Fibrogenesis Tissue Repair , vol.9 , pp. 1
    • Shi, S.1    Koya, D.2    Kanasaki, K.3
  • 19
    • 85003875974 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibition and renoprotection: the role of antifibrotic effects
    • Takagaki, Y., Koya, D. and Kanasaki, K. (2017) Dipeptidyl peptidase-4 inhibition and renoprotection: the role of antifibrotic effects. Curr. Opin. Nephrol. Hypertens. 26, 56-66, https://doi.org/10.1097/MNH.0000000000000291
    • (2017) Curr. Opin. Nephrol. Hypertens , vol.26 , pp. 56-66
    • Takagaki, Y.1    Koya, D.2    Kanasaki, K.3
  • 20
    • 84863436536 scopus 로고    scopus 로고
    • Comparative clinical pharmacokinetics of dipeptidyl peptidase-4 inhibitors
    • Golightly, L.K., Drayna, C.C. and McDermott, M.T. (2012) Comparative clinical pharmacokinetics of dipeptidyl peptidase-4 inhibitors. Clin. Pharmacokinet. 51, 501-514, https://doi.org/10.1007/BF03261927
    • (2012) Clin. Pharmacokinet , vol.51 , pp. 501-514
    • Golightly, L.K.1    Drayna, C.C.2    Mcdermott, M.T.3
  • 21
    • 77950197593 scopus 로고    scopus 로고
    • The metabolism and disposition of the oral dipeptidyl peptidase-4 inhibitor, linagliptin, in humans
    • Blech, S., Ludwig-Schwellinger, E., Grafe-Mody, E.U., Withopf, B. and Wagner, K. (2010) The metabolism and disposition of the oral dipeptidyl peptidase-4 inhibitor, linagliptin, in humans. Drug Metab. Dispos. 38, 667-678, https://doi.org/10.1124/dmd.109.031476
    • (2010) Drug Metab. Dispos , vol.38 , pp. 667-678
    • Blech, S.1    Ludwig-Schwellinger, E.2    Grafe-Mody, E.U.3    Withopf, B.4    Wagner, K.5
  • 22
    • 80052530183 scopus 로고    scopus 로고
    • Effect of renal impairment on the pharmacokinetics of the dipeptidyl peptidase-4 inhibitor linagliptin(*)
    • Graefe-Mody, U., Friedrich, C., Port, A., Ring, A., Retlich, S., Heise, T. et al. (2011) Effect of renal impairment on the pharmacokinetics of the dipeptidyl peptidase-4 inhibitor linagliptin(*). Diabetes Obes. Metab. 13, 939-946, https://doi.org/10.1111/j.1463-1326.2011.01458.x
    • (2011) Diabetes Obes. Metab , vol.13 , pp. 939-946
    • Graefe-Mody, U.1    Friedrich, C.2    Port, A.3    Ring, A.4    Retlich, S.5    Heise, T.6
  • 23
    • 85192027249 scopus 로고    scopus 로고
    • Eli Lilly and Company, Indianapolis, IN
    • (2016) Tradjenta (linagliptin) prescribing information. Eli Lilly and Company, Indianapolis, IN, https://www.accessdata.fda.gov/drugsatfda docs/label/2017/201280s016lbl.pdf
    • (2016) Tradjenta (linagliptin) prescribing information
  • 24
    • 85192028729 scopus 로고    scopus 로고
    • Merck & Co., Inc., Whitehouse Station, NJ
    • Merck & Co., Inc. (2017) Januvia (sitagliptin) Prescribing Information, Merck & Co., Inc., Whitehouse Station, NJ, https://www.accessdata.fda.gov/drugsatfda docs/label/2017/021995s038lbl.pdf
    • (2017) Januvia (sitagliptin) Prescribing Information
  • 26
    • 85044986630 scopus 로고    scopus 로고
    • Takeda Pharmaceuticals America, Inc., Deerfield, IL
    • Takeda Pharmaceuticals America, Inc. (2016) Nesina (alogliptin) prescribing information, Takeda Pharmaceuticals America, Inc., Deerfield, IL, https://www.accessdata.fda.gov/drugsatfda docs/label/2016/022271s011lbl.pdf
    • (2016) Nesina (alogliptin) prescribing information
  • 27
    • 85192028226 scopus 로고    scopus 로고
    • Novartis Europharm Limited, Camberely, United Kingdom
    • Novartis Europharm Limited (2014) Galvus (vildagliptin) Summary of Product Characteristics, Novartis Europharm Limited, Camberely, United Kingdom, http://www.ema.europa.eu/docs/en GB/document library/EPAR-Product Information/human/000771/WC500020327.pdf
    • (2014) Galvus (vildagliptin) Summary of Product Characteristics
  • 28
    • 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, A.M., Durinx, C., Scharpe, S. and De Meester, I. (2003) 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. 40, 209-294, https://doi.org/10.1080/713609354
    • (2003) Crit. Rev. Clin. Lab. Sci , vol.40 , pp. 209-294
    • Lambeir, A.M.1    Durinx, C.2    Scharpe, S.3    De Meester, I.4
  • 29
    • 0037966007 scopus 로고    scopus 로고
    • The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism
    • Engel, M., Hoffmann, T., Wagner, L., Wermann, M., Heiser, U., Kiefersauer, R. et al. (2003) The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism. Proc. Natl. Acad. Sci. U.S.A. 100, 5063-5068, https://doi.org/10.1073/pnas.0230620100
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 5063-5068
    • Engel, M.1    Hoffmann, T.2    Wagner, L.3    Wermann, M.4    Heiser, U.5    Kiefersauer, R.6
  • 30
    • 10644296948 scopus 로고    scopus 로고
    • One site mutation disrupts dimer formation in human DPP-IV proteins
    • Chien, C.H., Huang, L.H., Chou, C.Y., Chen, Y.S., Han, Y.S., Chang, G.G. et al. (2004) One site mutation disrupts dimer formation in human DPP-IV proteins. J. Biol. Chem. 279, 52338-52345, https://doi.org/10.1074/jbc.M406185200
    • (2004) J. Biol. Chem , vol.279 , 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
  • 31
    • 84974808180 scopus 로고    scopus 로고
    • Cut to the chase: a review of CD26/dipeptidyl peptidase-4's (DPP4) entanglement in the immune system
    • Klemann, C., Wagner, L., Stephan, M. and von Horsten, S. (2016) Cut to the chase: a review of CD26/dipeptidyl peptidase-4's (DPP4) entanglement in the immune system. Clin. Exp. Immunol. 185, 1-21, https://doi.org/10.1111/cei.12781
    • (2016) Clin. Exp. Immunol , vol.185 , pp. 1-21
    • Klemann, C.1    Wagner, L.2    Stephan, M.3    Von Horsten, S.4
  • 32
    • 84920095184 scopus 로고    scopus 로고
    • Pharmacology, physiology, and mechanisms of action of dipeptidyl peptidase-4 inhibitors
    • Mulvihill, E.E. and Drucker, D.J. (2014) Pharmacology, physiology, and mechanisms of action of dipeptidyl peptidase-4 inhibitors. Endocr. Rev. 35, 992-1019, https://doi.org/10.1210/er.2014-1035
    • (2014) Endocr. Rev , vol.35 , pp. 992-1019
    • Mulvihill, E.E.1    Drucker, D.J.2
  • 33
    • 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. and Daniel, C. (2014) Soluble DPP4 originates in part from bone marrow cells and not from the kidney. Peptides 57, 109-117, https://doi.org/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
  • 34
    • 0013986243 scopus 로고
    • A new dipeptide naphthylamidase hydrolyzing glycyl-prolyl-beta-naphthylamide
    • Hopsu-Havu, V.K. and Glenner, G.G. (1966) A new dipeptide naphthylamidase hydrolyzing glycyl-prolyl-beta-naphthylamide. Histochemie 7, 197-201, https://doi.org/10.1007/BF00577838
    • (1966) Histochemie , vol.7 , pp. 197-201
    • Hopsu-Havu, V.K.1    Glenner, G.G.2
  • 35
    • 84938497115 scopus 로고    scopus 로고
    • The dipeptidyl peptidase family, prolyl oligopeptidase, and prolyl carboxypeptidase in the immune system and inflammatory disease, including atherosclerosis
    • Waumans, Y., Baerts, L., Kehoe, K., Lambeir, A.M. and De Meester, I. (2015) The dipeptidyl peptidase family, prolyl oligopeptidase, and prolyl carboxypeptidase in the immune system and inflammatory disease, including atherosclerosis. Front. Immunol. 6, 387, https://doi.org/10.3389/fimmu.2015.00387
    • (2015) Front. Immunol , vol.6 , pp. 387
    • Waumans, Y.1    Baerts, L.2    Kehoe, K.3    Lambeir, A.M.4    De Meester, I.5
  • 37
    • 85023613722 scopus 로고    scopus 로고
    • Do we know the true mechanism of action of the DPP-4 inhibitors? Diabetes Obes
    • Andersen, E.S., Deacon, C.F. and Holst, J.J. (2017) Do we know the true mechanism of action of the DPP-4 inhibitors? Diabetes Obes. Metab. 20, 34-41, https://doi.org/10.1111/dom.13018
    • (2017) Metab , vol.20 , pp. 34-41
    • Andersen, E.S.1    Deacon, C.F.2    Holst, J.J.3
  • 38
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides
    • Mentlein, R. (1999) Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides. Regul. Pept. 85, 9-24, https://doi.org/10.1016/S0167-0115(99)00089-0
    • (1999) Regul. Pept , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 39
    • 0026703489 scopus 로고
    • Ultrastructural localization of dipeptidylpeptidase IV in the glomerulum of the rat kidney
    • Kettmann, U., Humbel, B. and Holzhausen, H.J. (1992) Ultrastructural localization of dipeptidylpeptidase IV in the glomerulum of the rat kidney. Acta Histochem. 92, 225-227, https://doi.org/10.1016/S0065-1281(11)80085-1
    • (1992) Acta Histochem , vol.92 , pp. 225-227
    • Kettmann, U.1    Humbel, B.2    Holzhausen, H.J.3
  • 40
    • 85030749499 scopus 로고    scopus 로고
    • KLK5 induces shedding of DPP4 from circulatory Th17 cells in type 2 diabetes
    • Nargis, T., Kumar, K., Ghosh, A.R., Sharma, A., Rudra, D., Sen, D. et al. (2017) KLK5 induces shedding of DPP4 from circulatory Th17 cells in type 2 diabetes. Mol. Metab. 6, 1529-1539, https://doi.org/10.1016/j.molmet.2017.09.004
    • (2017) Mol. Metab , vol.6 , pp. 1529-1539
    • Nargis, T.1    Kumar, K.2    Ghosh, A.R.3    Sharma, A.4    Rudra, D.5    Sen, D.6
  • 41
    • 0023875249 scopus 로고
    • Dipeptidyl peptidase (DPP) IV in rat organs Comparison of immunohistochemistry and activity histochemistry
    • Hartel, S., Gossrau, R., Hanski, C. and Reutter, W. (1988) Dipeptidyl peptidase (DPP) IV in rat organs. Comparison of immunohistochemistry and activity histochemistry. Histochemistry 89, 151-161, https://doi.org/10.1007/BF00489918
    • (1988) Histochemistry , vol.89 , pp. 151-161
    • Hartel, S.1    Gossrau, R.2    Hanski, C.3    Reutter, W.4
  • 42
    • 0035824614 scopus 로고    scopus 로고
    • Association of Na(+)-H(+) exchanger isoform NHE3 and dipeptidyl peptidase IV in the renal proximal tubule
    • Girardi, A.C., Degray, B.C., Nagy, T., Biemesderfer, D. and Aronson, P.S. (2001) Association of Na(+)-H(+) exchanger isoform NHE3 and dipeptidyl peptidase IV in the renal proximal tubule. J. Biol. Chem. 276, 46671-46677, https://doi.org/10.1074/jbc.M106897200
    • (2001) J. Biol. Chem , vol.276 , pp. 46671-46677
    • Girardi, A.C.1    Degray, B.C.2    Nagy, T.3    Biemesderfer, D.4    Aronson, P.S.5
  • 43
    • 6044261454 scopus 로고    scopus 로고
    • Role of dipeptidyl peptidase IV in regulating activity of Na+/H+ exchanger isoform NHE3 in proximal tubule cells
    • Girardi, A.C., Knauf, F., Demuth, H.U. and Aronson, P.S. (2004) Role of dipeptidyl peptidase IV in regulating activity of Na+/H+ exchanger isoform NHE3 in proximal tubule cells. Am. J. Physiol. Cell Physiol. 287, C1238-C1245, https://doi.org/10.1152/ajpcell.00186.2004
    • (2004) Am. J. Physiol. Cell Physiol , vol.287 , pp. C1238-C1245
    • Girardi, A.C.1    Knauf, F.2    Demuth, H.U.3    Aronson, P.S.4
  • 44
    • 0025137029 scopus 로고
    • Hydrolysis and transport of proline-containing peptides in renal brush-border membrane vesicles from dipeptidyl peptidase IV-positive and dipeptidyl peptidase IV-negative rat strains
    • Tiruppathi, C., Miyamoto, Y., Ganapathy, V., Roesel, R.A., Whitford, G.M. and Leibach, F.H. (1990) Hydrolysis and transport of proline-containing peptides in renal brush-border membrane vesicles from dipeptidyl peptidase IV-positive and dipeptidyl peptidase IV-negative rat strains. J. Biol. Chem. 265, 1476-1483
    • (1990) J. Biol. Chem , vol.265 , pp. 1476-1483
    • Tiruppathi, C.1    Miyamoto, Y.2    Ganapathy, V.3    Roesel, R.A.4    Whitford, G.M.5    Leibach, F.H.6
  • 45
    • 84865447930 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV regulates proliferation of preglomerular vascular smooth muscle and mesangial cells
    • Jackson, E.K., Kochanek, S.J. and Gillespie, D.G. (2012) Dipeptidyl peptidase IV regulates proliferation of preglomerular vascular smooth muscle and mesangial cells. Hypertension 60, 757-764, https://doi.org/10.1161/HYPERTENSIONAHA.112.196501
    • (2012) Hypertension , vol.60 , pp. 757-764
    • Jackson, E.K.1    Kochanek, S.J.2    Gillespie, D.G.3
  • 46
    • 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. and Xue, C. (2007) Increase in DPP-IV in the intestine, liver and kidney of the rat treated with high fat diet and streptozotocin. Life Sci. 81, 272-279, https://doi.org/10.1016/j.lfs.2007.04.040
    • (2007) Life Sci , vol.81 , pp. 272-279
    • Yang, J.1    Campitelli, J.2    Hu, G.3    Lin, Y.4    Luo, J.5    Xue, C.6
  • 47
    • 85029088749 scopus 로고    scopus 로고
    • DPP-4 enzyme deficiency protects kidney from acute ischemia-reperfusion injury: role for remote intermittent bowel ischemia-reperfusion preconditioning
    • Chen, Y.T., Wallace, C.G., Yang, C.C., Chen, C.H., Chen, K.H., Sung, P.H. et al. (2017) DPP-4 enzyme deficiency protects kidney from acute ischemia-reperfusion injury: role for remote intermittent bowel ischemia-reperfusion preconditioning. Oncotarget 8, 54821-54837
    • (2017) Oncotarget , vol.8 , pp. 54821-54837
    • Chen, Y.T.1    Wallace, C.G.2    Yang, C.C.3    Chen, C.H.4    Chen, K.H.5    Sung, P.H.6
  • 48
    • 0021879016 scopus 로고
    • Induction of dipeptidylpeptidase IV activity in human renal glomeruli-a histochemical study
    • Elleder, M. and Stejskal, J. (1985) Induction of dipeptidylpeptidase IV activity in human renal glomeruli-a histochemical study. Acta Histochem. 77, 75-78, https://doi.org/10.1016/S0065-1281(85)80019-2
    • (1985) Acta Histochem , vol.77 , pp. 75-78
    • Elleder, M.1    Stejskal, J.2
  • 49
    • 0026014886 scopus 로고
    • Demonstration of glomerular DPP IV activity in kidney diseases
    • Stiller, D., Bahn, H. and August, C. (1991) Demonstration of glomerular DPP IV activity in kidney diseases. Acta Histochem. 91, 105-109, https://doi.org/10.1016/S0065-1281(11)80302-8
    • (1991) Acta Histochem , vol.91 , pp. 105-109
    • Stiller, D.1    Bahn, H.2    August, C.3
  • 50
    • 84927640087 scopus 로고    scopus 로고
    • Blood pressure and glucose independent renoprotective effects of dipeptidyl peptidase-4 inhibition in a mouse model of type-2 diabetic nephropathy
    • Sharkovska, Y., Reichetzeder, C., Alter, M., Tsuprykov, O., Bachmann, S., Secher, T. et al. (2014) Blood pressure and glucose independent renoprotective effects of dipeptidyl peptidase-4 inhibition in a mouse model of type-2 diabetic nephropathy. J. Hypertens. 32, 2211-2223, https://doi.org/10.1097/HJH.0000000000000328
    • (2014) J. Hypertens , vol.32 , pp. 2211-2223
    • Sharkovska, Y.1    Reichetzeder, C.2    Alter, M.3    Tsuprykov, O.4    Bachmann, S.5    Secher, T.6
  • 51
    • 0027497013 scopus 로고
    • Interferon-gamma induces dipeptidylpeptidase IV expression in human glomerular epithelial cells
    • Stefanovic, V., Ardaillou, N., Vlahovic, P., Placier, S., Ronco, P. and Ardaillou, R. (1993) Interferon-gamma induces dipeptidylpeptidase IV expression in human glomerular epithelial cells. Immunology 80, 465-470
    • (1993) Immunology , vol.80 , pp. 465-470
    • Stefanovic, V.1    Ardaillou, N.2    Vlahovic, P.3    Placier, S.4    Ronco, P.5    Ardaillou, R.6
  • 52
    • 0141737555 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV expression and activity in human glomerular endothelial cells
    • Pala, L., Mannucci, E., Pezzatini, A., Ciani, S., Sardi, J., Raimondi, L. et al. (2003) Dipeptidyl peptidase-IV expression and activity in human glomerular endothelial cells. Biochem. Biophys. Res. Commun. 310, 28-31, https://doi.org/10.1016/j.bbrc.2003.08.111
    • (2003) Biochem. Biophys. Res. Commun , vol.310 , pp. 28-31
    • Pala, L.1    Mannucci, E.2    Pezzatini, A.3    Ciani, S.4    Sardi, J.5    Raimondi, L.6
  • 53
    • 0033859805 scopus 로고    scopus 로고
    • Immunoelectron microscopic demonstration of the membrane proteases aminopeptidase N/CD13 and dipeptidyl peptidase IV/CD26 in normal and neoplastic renal parenchymal tissues and cells
    • Stange, T., Kettmann, U. and Holzhausen, H.J. (2000) Immunoelectron microscopic demonstration of the membrane proteases aminopeptidase N/CD13 and dipeptidyl peptidase IV/CD26 in normal and neoplastic renal parenchymal tissues and cells. Eur. J. Histochem. 44, 157-164
    • (2000) Eur. J. Histochem , vol.44 , pp. 157-164
    • Stange, T.1    Kettmann, U.2    Holzhausen, H.J.3
  • 54
    • 0029785894 scopus 로고    scopus 로고
    • Immunoelectron microscopic single and double labelling of aminopeptidase N (CD 13) and dipeptidyl peptidase IV (CD 26)
    • Stange, T., Kettmann, U. and Holzhausen, H.J. (1996) Immunoelectron microscopic single and double labelling of aminopeptidase N (CD 13) and dipeptidyl peptidase IV (CD 26). Acta Histochem. 98, 323-331, https://doi.org/10.1016/S0065-1281(96)80025-0
    • (1996) Acta Histochem , vol.98 , pp. 323-331
    • Stange, T.1    Kettmann, U.2    Holzhausen, H.J.3
  • 55
    • 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. and Stefanovic, V. (2008) Diagnostic value of the aminopeptidase N, N-acetyl-beta-D-glucosaminidase and dipeptidylpeptidase IV in evaluating tubular dysfunction in patients with glomerulopathies. Ren. Fail. 30, 896-903, https://doi.org/10.1080/08860220802359048
    • (2008) Ren. Fail , vol.30 , pp. 896-903
    • Mitic, B.1    Lazarevic, G.2    Vlahovic, P.3    Rajic, M.4    Stefanovic, V.5
  • 56
    • 84866718544 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV is a potential molecular biomarker in diabetic kidney disease
    • Sun, A.L., Deng, J.T., Guan, G.J., Chen, S.H., Liu, Y.T., Cheng, J. et al. (2012) Dipeptidyl peptidase-IV is a potential molecular biomarker in diabetic kidney disease. Diab. Vasc. Dis. Res. 9, 301-308, https://doi.org/10.1177/1479164111434318
    • (2012) Diab. Vasc. Dis. Res , vol.9 , 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
  • 57
    • 85012899360 scopus 로고    scopus 로고
    • Serum protease activity in chronic kidney disease patients: The GANI MED renal cohort
    • Wolke, C., Teumer, A., Endlich, K., Endlich, N., Rettig, R., Stracke, S. et al. (2017) Serum protease activity in chronic kidney disease patients: The GANI MED renal cohort. Exp. Biol. Med. (Maywood) 242, 554-563, https://doi.org/10.1177/1535370216684040
    • (2017) Exp. Biol. Med. (Maywood) , vol.242 , pp. 554-563
    • Wolke, C.1    Teumer, A.2    Endlich, K.3    Endlich, N.4    Rettig, R.5    Stracke, S.6
  • 58
    • 84924408372 scopus 로고    scopus 로고
    • Increased plasma dipeptidyl peptidase 4 activities predict new-onset microalbuminuria in association with its proinflammatory effects in Chinese without diabetes: a four-year prospective study
    • Zheng, T., Baskota, A., Gao, Y., Tian, H. and Yang, F. (2015) Increased plasma dipeptidyl peptidase 4 activities predict new-onset microalbuminuria in association with its proinflammatory effects in Chinese without diabetes: a four-year prospective study. Nephrol. Dial. Transplant. 30, 460-466, https://doi.org/10.1093/ndt/gfu312
    • (2015) Nephrol. Dial. Transplant , vol.30 , pp. 460-466
    • Zheng, T.1    Baskota, A.2    Gao, Y.3    Tian, H.4    Yang, F.5
  • 59
    • 84958154465 scopus 로고    scopus 로고
    • Increased plasma dipeptidyl peptidase-4 activities are associated with high prevalence of diabetic nephropathy in Chinese patients with newly diagnosed type 2 diabetes: a cross-sectional study
    • Zheng, T., Liu, Y., Qin, S., Liu, H., Zhang, X. and Zhao, H. (2016) Increased plasma dipeptidyl peptidase-4 activities are associated with high prevalence of diabetic nephropathy in Chinese patients with newly diagnosed type 2 diabetes: a cross-sectional study. Diab. Vasc. Dis. Res. 13, 127-136, https://doi.org/10.1177/1479164115615356
    • (2016) Diab. Vasc. Dis. Res , vol.13 , pp. 127-136
    • Zheng, T.1    Liu, Y.2    Qin, S.3    Liu, H.4    Zhang, X.5    Zhao, H.6
  • 60
    • 84992688688 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 activity is associated with urine albumin excretion in type 1 diabetes
    • Duvnjak, L., Perkovic, M.N. and Blaslov, K. (2017) Dipeptidyl peptidase-4 activity is associated with urine albumin excretion in type 1 diabetes. J. Diabetes Complications 31, 218-222, https://doi.org/10.1016/j.jdiacomp.2016.08.022
    • (2017) J. Diabetes Complications , vol.31 , pp. 218-222
    • Duvnjak, L.1    Perkovic, M.N.2    Blaslov, K.3
  • 61
    • 84869238002 scopus 로고    scopus 로고
    • DPP-4 inhibition on top of angiotensin receptor blockade offers a new therapeutic approach for diabetic nephropathy
    • Alter, M.L., Ott, I.M., von Websky, K., Tsuprykov, O., Sharkovska, Y., Krause-Relle, K. et al. (2012) DPP-4 inhibition on top of angiotensin receptor blockade offers a new therapeutic approach for diabetic nephropathy. Kidney Blood Press. Res. 36, 119-130, https://doi.org/10.1159/000341487
    • (2012) Kidney Blood Press. Res , vol.36 , 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
  • 62
    • 84929469873 scopus 로고    scopus 로고
    • Linagliptin blocks renal damage in type 1 diabetic rats by suppressing advanced glycation end products-receptor axis
    • Nakashima, S., Matsui, T., Takeuchi, M. and Yamagishi, S.I. (2014) Linagliptin blocks renal damage in type 1 diabetic rats by suppressing advanced glycation end products-receptor axis. Horm. Metab. Res. 46, 717-721, https://doi.org/10.1055/s-0034-1371892
    • (2014) Horm. Metab. Res , vol.46 , pp. 717-721
    • Nakashima, S.1    Matsui, T.2    Takeuchi, M.3    Yamagishi, S.I.4
  • 63
    • 84929074723 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 deficiency protects against experimental diabetic nephropathy partly by blocking the advanced glycation end products-receptor axis
    • Matsui, T., Nakashima, S., Nishino, Y., Ojima, A., Nakamura, N., Arima, K. et al. (2015) Dipeptidyl peptidase-4 deficiency protects against experimental diabetic nephropathy partly by blocking the advanced glycation end products-receptor axis. Lab. Invest. 95, 525-533, https://doi.org/10.1038/labinvest.2015.35
    • (2015) Lab. Invest , vol.95 , pp. 525-533
    • Matsui, T.1    Nakashima, S.2    Nishino, Y.3    Ojima, A.4    Nakamura, N.5    Arima, K.6
  • 64
    • 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. (2014) Linagliptin-mediated DPP-4 inhibition ameliorates kidney fibrosis in streptozotocin-induced diabetic mice by inhibiting endothelial-to-mesenchymal transition in a therapeutic regimen. Diabetes 63, 2120-2131, https://doi.org/10.2337/db13-1029
    • (2014) Diabetes , vol.63 , pp. 2120-2131
    • Kanasaki, K.1    Shi, S.2    Kanasaki, M.3    He, J.4    Nagai, T.5    Nakamura, Y.6
  • 65
    • 84940791235 scopus 로고    scopus 로고
    • Interactions of DPP-4 and integrin beta1 influences endothelial-to-mesenchymal transition
    • Shi, S., Srivastava, S.P., Kanasaki, M., He, J., Kitada, M., Nagai, T. et al. (2015) Interactions of DPP-4 and integrin beta1 influences endothelial-to-mesenchymal transition. Kidney Int. 88, 479-489, https://doi.org/10.1038/ki.2015.103
    • (2015) Kidney Int , vol.88 , pp. 479-489
    • Shi, S.1    Srivastava, S.P.2    Kanasaki, M.3    He, J.4    Kitada, M.5    Nagai, T.6
  • 66
    • 84997428811 scopus 로고    scopus 로고
    • Stromal cell-derived factor-1 is upregulated by dipeptidyl peptidase-4 inhibition and has protective roles in progressive diabetic nephropathy
    • Takashima, S., Fujita, H., Fujishima, H., Shimizu, T., Sato, T., Morii, T. et al. (2016) Stromal cell-derived factor-1 is upregulated by dipeptidyl peptidase-4 inhibition and has protective roles in progressive diabetic nephropathy. Kidney Int. 90, 783-796, https://doi.org/10.1016/j.kint.2016.06.012
    • (2016) Kidney Int , vol.90 , pp. 783-796
    • Takashima, S.1    Fujita, H.2    Fujishima, H.3    Shimizu, T.4    Sato, T.5    Morii, T.6
  • 67
    • 85046461244 scopus 로고    scopus 로고
    • Renoprotective effects of linagliptin and empagliflozin in a rat model of early diabetic nephropathy
    • (492-P)
    • Gill, A., Gray, S.P., Watson, A.M.D., Cooper, M.E. and Jandeleit-Dahm, K. A.M. (2017) Renoprotective effects of linagliptin and empagliflozin in a rat model of early diabetic nephropathy. Diabetes 66, A130 (492-P)
    • (2017) Diabetes , vol.66
    • Gill, A.1    Gray, S.P.2    Watson, A.M.D.3    Cooper, M.E.4    Jandeleit-Dahm, K.A.M.5
  • 68
    • 84885662277 scopus 로고    scopus 로고
    • Effects of telmisartan and linagliptin when used in combination on blood pressure and oxidative stress in rats with 2-kidney-1-clip hypertension
    • Chaykovska, L., Alter, M.L., von Websky, K., Hohmann, M., Tsuprykov, O., Reichetzeder, C. et al. (2013) Effects of telmisartan and linagliptin when used in combination on blood pressure and oxidative stress in rats with 2-kidney-1-clip hypertension. J. Hypertens. 31, 2290-2298, https://doi.org/10.1097/HJH.0b013e3283649b4d
    • (2013) J. Hypertens , vol.31 , pp. 2290-2298
    • Chaykovska, L.1    Alter, M.L.2    Von Websky, K.3    Hohmann, M.4    Tsuprykov, O.5    Reichetzeder, C.6
  • 69
    • 84907883358 scopus 로고    scopus 로고
    • DPP4 inhibition attenuates filtration barrier injury and oxidant stress in the zucker obese rat
    • Nistala, R., Habibi, J., Aroor, A., Sowers, J.R., Hayden, M.R., Meuth, A. et al. (2014) DPP4 inhibition attenuates filtration barrier injury and oxidant stress in the zucker obese rat. Obesity 22, 2172-2179, https://doi.org/10.1002/oby.20833
    • (2014) Obesity , vol.22 , pp. 2172-2179
    • Nistala, R.1    Habibi, J.2    Aroor, A.3    Sowers, J.R.4    Hayden, M.R.5    Meuth, A.6
  • 70
    • 84964689544 scopus 로고    scopus 로고
    • The dipeptidyl peptidase inhibitor linagliptin and the angiotensin II receptor blocker telmisartan show renal benefit by different pathways in rats with 5/6 nephrectomy
    • Tsuprykov, O., Ando, R., Reichetzeder, C., von Websky, K., Antonenko, V., Sharkovska, Y. et al. (2016) The dipeptidyl peptidase inhibitor linagliptin and the angiotensin II receptor blocker telmisartan show renal benefit by different pathways in rats with 5/6 nephrectomy. Kidney Int. 89, 1049-1061, https://doi.org/10.1016/j.kint.2016.01.016
    • (2016) Kidney Int , vol.89 , pp. 1049-1061
    • Tsuprykov, O.1    Ando, R.2    Reichetzeder, C.3    Von Websky, K.4    Antonenko, V.5    Sharkovska, Y.6
  • 71
    • 84957428998 scopus 로고    scopus 로고
    • Renoprotective effect of DPP-4 inhibitors against free fatty acid-bound albumin-induced renal proximal tubular cell injury
    • Tanaka, Y., Kume, S., Chin-Kanasaki, M., Araki, H., Araki, S.I., Ugi, S. et al. (2016) Renoprotective effect of DPP-4 inhibitors against free fatty acid-bound albumin-induced renal proximal tubular cell injury. Biochem. Biophys. Res. Commun. 470, 539-545, https://doi.org/10.1016/j.bbrc.2016.01.109
    • (2016) Biochem. Biophys. Res. Commun , vol.470 , pp. 539-545
    • Tanaka, Y.1    Kume, S.2    Chin-Kanasaki, M.3    Araki, H.4    Araki, S.I.5    Ugi, S.6
  • 72
    • 85192027940 scopus 로고    scopus 로고
    • GLP-1 receptor independent effects of DPP-4 inhibition in mice with 5/6 nephrectomy
    • Hasan, A.A., Reichetzeder, C., Guo, J., von Websky, K., Tsuprykov, O., Klein, T. et al. (2016) GLP-1 receptor independent effects of DPP-4 inhibition in mice with 5/6 nephrectomy. Diabetes 65, A132
    • (2016) Diabetes , vol.65
    • Hasan, A.A.1    Reichetzeder, C.2    Guo, J.3    Von Websky, K.4    Tsuprykov, O.5    Klein, T.6
  • 73
    • 85024907511 scopus 로고    scopus 로고
    • Role of soluble and membrane-bound dipeptidyl peptidase-4 in diabetic nephropathy
    • Hasan, A.A. and Hocher, B. (2017) Role of soluble and membrane-bound dipeptidyl peptidase-4 in diabetic nephropathy. J. Mol. Endocrinol. 59, R1-R10, https://doi.org/10.1530/JME-17-0005
    • (2017) J. Mol. Endocrinol , vol.59 , pp. R1-R10
    • Hasan, A.A.1    Hocher, B.2
  • 74
    • 84870818167 scopus 로고    scopus 로고
    • Pathophysiology of the aging kidney and therapeutic interventions
    • Kanasaki, K., Kitada, M. and Koya, D. (2012) Pathophysiology of the aging kidney and therapeutic interventions. Hypertens. Res. 35, 1121-1128, https://doi.org/10.1038/hr.2012.159
    • (2012) Hypertens. Res , vol.35 , pp. 1121-1128
    • Kanasaki, K.1    Kitada, M.2    Koya, D.3
  • 76
    • 0014890525 scopus 로고
    • Structural-functional correlations in renal disease I. A method for assaying and classifying histopathologic changes in renal disease
    • Striker, G.E., Schainuck, L.I., Cutler, R.E. and Benditt, E.P. (1970) Structural-functional correlations in renal disease. I. A method for assaying and classifying histopathologic changes in renal disease. Hum. Pathol. 1, 615-630, https://doi.org/10.1016/S0046-8177(70)80060-0
    • (1970) Hum. Pathol , vol.1 , pp. 615-630
    • Striker, G.E.1    Schainuck, L.I.2    Cutler, R.E.3    Benditt, E.P.4
  • 77
    • 0014421532 scopus 로고
    • Relationship between renal function and histological changes found in renal-biopsy specimens from patients with persistent glomerular nephritis
    • Risdon, R.A., Sloper, J.C. and De Wardener, H.E. (1968) Relationship between renal function and histological changes found in renal-biopsy specimens from patients with persistent glomerular nephritis. Lancet 2, 363-366, https://doi.org/10.1016/S0140-6736(68)90589-8
    • (1968) Lancet , vol.2 , pp. 363-366
    • Risdon, R.A.1    Sloper, J.C.2    De Wardener, H.E.3
  • 78
    • 0026769228 scopus 로고
    • Tubulointerstitial changes as a major determinant in the progression of renal damage
    • Nath, K.A. (1992) Tubulointerstitial changes as a major determinant in the progression of renal damage. Am. J. Kidney Dis. 20, 1-17, https://doi.org/10.1016/S0272-6386(12)80312-X
    • (1992) Am. J. Kidney Dis , vol.20 , pp. 1-17
    • Nath, K.A.1
  • 79
    • 0019432032 scopus 로고
    • Correlations between renal cortical interstitial fibrosis, atrophy of the proximal tubules and impairment of the glomerular filtration rate
    • Mackensen-Haen, S., Bader, R., Grund, K.E. and Bohle, A. (1981) Correlations between renal cortical interstitial fibrosis, atrophy of the proximal tubules and impairment of the glomerular filtration rate. Clin. Nephrol. 15, 167-171
    • (1981) Clin. Nephrol , vol.15 , pp. 167-171
    • Mackensen-Haen, S.1    Bader, R.2    Grund, K.E.3    Bohle, A.4
  • 80
    • 84938415449 scopus 로고    scopus 로고
    • Preservation of glucagon-like peptide-1 level attenuates angiotensin II-induced tissue fibrosis by altering AT1/AT 2 receptor expression and angiotensin-converting enzyme 2 activity in rat heart
    • Zhang, L.H., Pang, X.F., Bai, F., Wang, N.P., Shah, A.I., McKallip, R.J. et al. (2015) Preservation of glucagon-like peptide-1 level attenuates angiotensin II-induced tissue fibrosis by altering AT1/AT 2 receptor expression and angiotensin-converting enzyme 2 activity in rat heart. Cardiovasc. Drugs Ther. 29, 243-255, https://doi.org/10.1007/s10557-015-6592-7
    • (2015) Cardiovasc. Drugs Ther , vol.29 , pp. 243-255
    • Zhang, L.H.1    Pang, X.F.2    Bai, F.3    Wang, N.P.4    Shah, A.I.5    Mckallip, R.J.6
  • 81
    • 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. (2015) A DPP-4 inhibitor suppresses fibrosis and inflammation on experimental autoimmune myocarditis in mice. PLoS ONE 10, e0119360, https://doi.org/10.1371/journal.pone.0119360
    • (2015) PLoS ONE , vol.10
    • Hirakawa, H.1    Zempo, H.2    Ogawa, M.3    Watanabe, R.4    Suzuki, J.5    Akazawa, H.6
  • 82
    • 84964314896 scopus 로고    scopus 로고
    • DPP-4 inhibitor linagliptin ameliorates cardiovascular injury in salt-sensitive hypertensive rats independently of blood glucose and blood pressure
    • Koibuchi, N., Hasegawa, Y., Katayama, T., Toyama, K., Uekawa, K., Sueta, D. et al. (2014) DPP-4 inhibitor linagliptin ameliorates cardiovascular injury in salt-sensitive hypertensive rats independently of blood glucose and blood pressure. Cardiovasc. Diabetol. 13, 157, https://doi.org/10.1186/s12933-014-0157-0
    • (2014) Cardiovasc. Diabetol , vol.13 , pp. 157
    • Koibuchi, N.1    Hasegawa, Y.2    Katayama, T.3    Toyama, K.4    Uekawa, K.5    Sueta, D.6
  • 83
    • 85018727375 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 (DPP-4) inhibition with linagliptin reduces western diet-induced myocardial TRAF3IP2 expression, inflammation and fibrosis in female mice
    • Aroor, A.R., Habibi, J., Kandikattu, H.K., Garro-Kacher, M., Barron, B., Chen, D. et al. (2017) Dipeptidyl peptidase-4 (DPP-4) inhibition with linagliptin reduces western diet-induced myocardial TRAF3IP2 expression, inflammation and fibrosis in female mice. Cardiovasc. Diabetol. 16, 61, https://doi.org/10.1186/s12933-017-0544-4
    • (2017) Cardiovasc. Diabetol , vol.16 , pp. 61
    • Aroor, A.R.1    Habibi, J.2    Kandikattu, H.K.3    Garro-Kacher, M.4    Barron, B.5    Chen, D.6
  • 84
    • 84991810131 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibition with linagliptin prevents western diet-induced vascular abnormalities in female mice
    • Manrique, C., Habibi, J., Aroor, A.R., Sowers, J.R., Jia, G., Hayden, M.R. et al. (2016) Dipeptidyl peptidase-4 inhibition with linagliptin prevents western diet-induced vascular abnormalities in female mice. Cardiovasc. Diabetol. 15, 94, https://doi.org/10.1186/s12933-016-0414-5
    • (2016) Cardiovasc. Diabetol , vol.15 , pp. 94
    • Manrique, C.1    Habibi, J.2    Aroor, A.R.3    Sowers, J.R.4    Jia, G.5    Hayden, M.R.6
  • 85
    • 84983504669 scopus 로고    scopus 로고
    • Linagliptin ameliorates methylglyoxal-induced peritoneal fibrosis in mice
    • Nagai, T., Doi, S., Nakashima, A., Irifuku, T., Sasaki, K., Ueno, T. et al. (2016) Linagliptin ameliorates methylglyoxal-induced peritoneal fibrosis in mice. PLoS ONE 11, e0160993, https://doi.org/10.1371/journal.pone.0160993
    • (2016) PLoS ONE , vol.11
    • Nagai, T.1    Doi, S.2    Nakashima, A.3    Irifuku, T.4    Sasaki, K.5    Ueno, T.6
  • 86
    • 55249103431 scopus 로고    scopus 로고
    • Fibroblasts in kidney fibrosis emerge via endothelial-to-mesenchymal transition
    • Zeisberg, E.M., Potenta, S.E., Sugimoto, H., Zeisberg, M. and Kalluri, R. (2008) Fibroblasts in kidney fibrosis emerge via endothelial-to-mesenchymal transition. J. Am. Soc. Nephrol. 19, 2282-2287, https://doi.org/10.1681/ASN.2008050513
    • (2008) J. Am. Soc. Nephrol , vol.19 , pp. 2282-2287
    • Zeisberg, E.M.1    Potenta, S.E.2    Sugimoto, H.3    Zeisberg, M.4    Kalluri, R.5
  • 87
    • 84883296447 scopus 로고    scopus 로고
    • Role of the endothelial-to-mesenchymal transition in renal fibrosis of chronic kidney disease
    • He, J., Xu, Y., Koya, D. and Kanasaki, K. (2013) Role of the endothelial-to-mesenchymal transition in renal fibrosis of chronic kidney disease. Clin. Exp. Nephrol. 17, 488-497, https://doi.org/10.1007/s10157-013-0781-0
    • (2013) Clin. Exp. Nephrol , vol.17 , pp. 488-497
    • He, J.1    Xu, Y.2    Koya, D.3    Kanasaki, K.4
  • 88
    • 73549092294 scopus 로고    scopus 로고
    • Endothelial-myofibroblast transition contributes to the early development of diabetic renal interstitial fibrosis in streptozotocin-induced diabetic mice
    • Li, J., Qu, X. and Bertram, J.F. (2009) Endothelial-myofibroblast transition contributes to the early development of diabetic renal interstitial fibrosis in streptozotocin-induced diabetic mice. Am. J. Pathol. 175, 1380-1388, https://doi.org/10.2353/ajpath.2009.090096
    • (2009) Am. J. Pathol , vol.175 , pp. 1380-1388
    • Li, J.1    Qu, X.2    Bertram, J.F.3
  • 89
    • 73549087447 scopus 로고    scopus 로고
    • Endothelial-mesenchymal transition as a novel mechanism for generating myofibroblasts during diabetic nephropathy
    • Kizu, A., Medici, D. and Kalluri, R. (2009) Endothelial-mesenchymal transition as a novel mechanism for generating myofibroblasts during diabetic nephropathy. Am. J. Pathol. 175, 1371-1373, https://doi.org/10.2353/ajpath.2009.090698
    • (2009) Am. J. Pathol , vol.175 , pp. 1371-1373
    • Kizu, A.1    Medici, D.2    Kalluri, R.3
  • 90
    • 33750712380 scopus 로고    scopus 로고
    • Renal fibroblasts and myofibroblasts in chronic kidney disease
    • Strutz, F. and Zeisberg, M. (2006) Renal fibroblasts and myofibroblasts in chronic kidney disease. J. Am. Soc. Nephrol. 17, 2992-2998, https://doi.org/10.1681/ASN.2006050420
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 2992-2998
    • Strutz, F.1    Zeisberg, M.2
  • 91
    • 85114281020 scopus 로고    scopus 로고
    • Endothelial to mesenchymal transition (EndoMT) in the pathogenesis of human fibrotic diseases
    • Piera-Velazquez, S., Mendoza, F.A. and Jimenez, S.A. (2016) Endothelial to mesenchymal transition (EndoMT) in the pathogenesis of human fibrotic diseases. J. Clin. Med. 5, 45, https://doi.org/10.3390/jcm5040045
    • (2016) J. Clin. Med , vol.5 , pp. 45
    • Piera-Velazquez, S.1    Mendoza, F.A.2    Jimenez, S.A.3
  • 92
    • 80052851503 scopus 로고    scopus 로고
    • Role of endothelial-mesenchymal transition (EndoMT) in the pathogenesis of fibrotic disorders
    • Piera-Velazquez, S., Li, Z. and Jimenez, S.A. (2011) Role of endothelial-mesenchymal transition (EndoMT) in the pathogenesis of fibrotic disorders. Am. J. Pathol. 179, 1074-1080, https://doi.org/10.1016/j.ajpath.2011.06.001
    • (2011) Am. J. Pathol , vol.179 , pp. 1074-1080
    • Piera-Velazquez, S.1    Li, Z.2    Jimenez, S.A.3
  • 93
    • 33845937474 scopus 로고    scopus 로고
    • Does transformation of microvascular endothelial cells into myofibroblasts play a key role in the etiology and pathology of fibrotic disease? Med
    • Karasek, M.A. (2007) Does transformation of microvascular endothelial cells into myofibroblasts play a key role in the etiology and pathology of fibrotic disease? Med. Hypotheses 68, 650-655, https://doi.org/10.1016/j.mehy.2006.07.053
    • (2007) Hypotheses , vol.68 , pp. 650-655
    • Karasek, M.A.1
  • 94
    • 85192028358 scopus 로고    scopus 로고
    • Dipeptidyl peptidase inhibitor linagliptin-and angiotensin II receptor blocker telmisartan-induced effects on renal and urinary exosomal miRNA expression in rats with 5/6 nephrectomy
    • (496-P)
    • Delic, D., Sontheimer, K., Tsuprykov, O., Hasan, A.A., Hocher, B., Baum, P. et al. (2017) Dipeptidyl peptidase inhibitor linagliptin-and angiotensin II receptor blocker telmisartan-induced effects on renal and urinary exosomal miRNA expression in rats with 5/6 nephrectomy. Diabetes 66, A131 (496-P)
    • (2017) Diabetes , vol.66
    • Delic, D.1    Sontheimer, K.2    Tsuprykov, O.3    Hasan, A.A.4    Hocher, B.5    Baum, P.6
  • 95
    • 84926474906 scopus 로고    scopus 로고
    • MicroRNAs in renal fibrosis
    • Chung, A.C. and Lan, H.Y. (2015) MicroRNAs in renal fibrosis. Front Physiol. 6, 50, https://doi.org/10.3389/fphys.2015.00050
    • (2015) Front Physiol , vol.6 , pp. 50
    • Chung, A.C.1    Lan, H.Y.2
  • 96
    • 84984607311 scopus 로고    scopus 로고
    • MicroRNAs as novel therapeutic targets to treat kidney injury and fibrosis
    • Gomez, I.G., Nakagawa, N. and Duffield, J.S. (2016) MicroRNAs as novel therapeutic targets to treat kidney injury and fibrosis. Am. J. Physiol. Renal Physiol. 310, F931-F944, https://doi.org/10.1152/ajprenal.00523.2015
    • (2016) Am. J. Physiol. Renal Physiol , vol.310 , pp. F931-F944
    • Gomez, I.G.1    Nakagawa, N.2    Duffield, J.S.3
  • 97
    • 84884853106 scopus 로고    scopus 로고
    • MicroRNAs in kidney fibrosis and diabetic nephropathy: roles on EMT and EndMT
    • Srivastava, S.P., Koya, D. and Kanasaki, K. (2013) MicroRNAs in kidney fibrosis and diabetic nephropathy: roles on EMT and EndMT. Biomed. Res. Int. 2013, 125469, https://doi.org/10.1155/2013/125469
    • (2013) Biomed. Res. Int , vol.2013
    • Srivastava, S.P.1    Koya, D.2    Kanasaki, K.3
  • 98
    • 84871676561 scopus 로고    scopus 로고
    • FGF regulates TGF-beta signaling and endothelial-to-mesenchymal transition via control of let-7 miRNA expression
    • Chen, P.Y., Qin, L., Barnes, C., Charisse, K., Yi, T., Zhang, X. et al. (2012) FGF regulates TGF-beta signaling and endothelial-to-mesenchymal transition via control of let-7 miRNA expression. Cell Rep. 2, 1684-1696, https://doi.org/10.1016/j.celrep.2012.10.021
    • (2012) Cell Rep , vol.2 , pp. 1684-1696
    • Chen, P.Y.1    Qin, L.2    Barnes, C.3    Charisse, K.4    Yi, T.5    Zhang, X.6
  • 99
    • 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.P., Nakamura, Y., Ishigaki, Y., Kitada, M. et al. (2014) N-acetyl-seryl-aspartyl-lysyl-proline inhibits diabetes-associated kidney fibrosis and endothelial-mesenchymal transition. Biomed. Res. Int. 2014, 696475, https://doi.org/10.1155/2014/696475
    • (2014) Biomed. Res. Int , vol.2014
    • Nagai, T.1    Kanasaki, M.2    Srivastava, S.P.3    Nakamura, Y.4    Ishigaki, Y.5    Kitada, M.6
  • 100
    • 84978898095 scopus 로고    scopus 로고
    • Effect of antifibrotic microRNAs crosstalk on the action of N-acetyl-seryl-aspartyl-lysyl-proline in diabetes-related kidney fibrosis
    • Srivastava, S.P., Shi, S., Kanasaki, M., Nagai, T., Kitada, M., He, J. et al. (2016) Effect of antifibrotic microRNAs crosstalk on the action of N-acetyl-seryl-aspartyl-lysyl-proline in diabetes-related kidney fibrosis. Sci. Rep. 6, 29884, https://doi.org/10.1038/srep29884
    • (2016) Sci. Rep , vol.6 , pp. 29884
    • Srivastava, S.P.1    Shi, S.2    Kanasaki, M.3    Nagai, T.4    Kitada, M.5    He, J.6
  • 101
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes, R.O. (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687, https://doi.org/10.1016/S0092-8674(02)00971-6
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 102
    • 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, C.P., Abraham, D.J. and Leask, A. (2009) Loss of beta1 integrin in mouse fibroblasts results in resistance to skin scleroderma in a mouse model. Arthritis Rheum. 60, 2817-2821, https://doi.org/10.1002/art.24801
    • (2009) Arthritis Rheum , vol.60 , pp. 2817-2821
    • Liu, S.1    Kapoor, M.2    Denton, C.P.3    Abraham, D.J.4    Leask, A.5
  • 103
    • 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, Y.C., Wei, W.C., Wang, Y.K., Lin, S.C., Sung, J.M. and Tang, M.J. (2010) Transforming growth factor-(beta)1 induces Smad3-dependent (beta)1 integrin gene expression in epithelial-to-mesenchymal transition during chronic tubulointerstitial fibrosis. Am. J. Pathol. 177, 1743-1754, https://doi.org/10.2353/ajpath.2010.091183
    • (2010) Am. J. Pathol , vol.177 , 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
  • 104
    • 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, M.T., Sridhara, R. and Alexander, L.D. (2015) Cyclic stretch-induced TGF-beta1 and fibronectin expression is mediated by beta1-integrin through c-Src-and STAT3-dependent pathways in renal epithelial cells. Am. J. Physiol. Renal Physiol. 308, F425-F436, https://doi.org/10.1152/ajprenal.00589.2014
    • (2015) Am. J. Physiol. Renal Physiol , vol.308 , pp. F425-F436
    • Hamzeh, M.T.1    Sridhara, R.2    Alexander, L.D.3
  • 105
    • 23044510616 scopus 로고    scopus 로고
    • CD26 regulates p38 mitogen-activated protein kinase-dependent phosphorylation of integrin beta1, adhesion to extracellular matrix, and tumorigenicity of T-anaplastic large cell lymphoma Karpas 299
    • Sato, T., Yamochi, T., Aytac, U., Ohnuma, K., McKee, K.S., Morimoto, C. et al. (2005) CD26 regulates p38 mitogen-activated protein kinase-dependent phosphorylation of integrin beta1, adhesion to extracellular matrix, and tumorigenicity of T-anaplastic large cell lymphoma Karpas 299. Cancer Res. 65, 6950-6956, https://doi.org/10.1158/0008-5472.CAN-05-0647
    • (2005) Cancer Res , vol.65 , pp. 6950-6956
    • Sato, T.1    Yamochi, T.2    Aytac, U.3    Ohnuma, K.4    Mckee, K.S.5    Morimoto, C.6
  • 106
    • 78650018824 scopus 로고    scopus 로고
    • Conversion of vascular endothelial cells into multipotent stem-like cells
    • Medici, D., Shore, E.M., Lounev, V.Y., Kaplan, F.S., Kalluri, R. and Olsen, B.R. (2010) Conversion of vascular endothelial cells into multipotent stem-like cells. Nat. Med. 16, 1400-1406, https://doi.org/10.1038/nm.2252
    • (2010) Nat. Med , vol.16 , 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
  • 107
    • 84940767662 scopus 로고    scopus 로고
    • Evidence for antifibrotic incretin-independent effects of the DPP-4 inhibitor linagliptin
    • Zeisberg, M. and Zeisberg, E.M. (2015) Evidence for antifibrotic incretin-independent effects of the DPP-4 inhibitor linagliptin. Kidney Int. 88, 429-431, https://doi.org/10.1038/ki.2015.175
    • (2015) Kidney Int , vol.88 , pp. 429-431
    • Zeisberg, M.1    Zeisberg, E.M.2
  • 108
    • 84983638433 scopus 로고    scopus 로고
    • The pathological significance of dipeptidyl peptidase-4 in endothelial cell homeostasis and kidney fibrosis
    • Kanasaki, K. (2016) The pathological significance of dipeptidyl peptidase-4 in endothelial cell homeostasis and kidney fibrosis. Diabetol. Int. 7, 212-220, https://doi.org/10.1007/s13340-016-0281-z
    • (2016) Diabetol. Int , vol.7 , pp. 212-220
    • Kanasaki, K.1
  • 109
    • 77950500403 scopus 로고    scopus 로고
    • Renal medullary microRNAs in Dahl salt-sensitive rats: miR-29b regulates several collagens and related genes
    • Liu, Y., Taylor, N.E., Lu, L., Usa, K., Cowley, Jr, A.W., Ferreri, N.R. et al. (2010) Renal medullary microRNAs in Dahl salt-sensitive rats: miR-29b regulates several collagens and related genes. Hypertension 55, 974-982, https://doi.org/10.1161/HYPERTENSIONAHA.109.144428
    • (2010) Hypertension , vol.55 , pp. 974-982
    • Liu, Y.1    Taylor, N.E.2    Lu, L.3    Usa, K.4    Cowley, A.W.5    Ferreri, N.R.6
  • 110
    • 79960067831 scopus 로고    scopus 로고
    • Cation-independent mannose 6-phosphate receptor inhibitor (PXS25) inhibits fibrosis in human proximal tubular cells by inhibiting conversion of latent to active TGF-beta1
    • Wong, M.G., Panchapakesan, U., Qi, W., Silva, D.G., Chen, X.M. and Pollock, C.A. (2011) Cation-independent mannose 6-phosphate receptor inhibitor (PXS25) inhibits fibrosis in human proximal tubular cells by inhibiting conversion of latent to active TGF-beta1. Am. J. Physiol. Renal Physiol. 301, F84-F93, https://doi.org/10.1152/ajprenal.00287.2010
    • (2011) Am. J. Physiol. Renal Physiol , vol.301 , pp. F84-F93
    • Wong, M.G.1    Panchapakesan, U.2    Qi, W.3    Silva, D.G.4    Chen, X.M.5    Pollock, C.A.6
  • 111
    • 84901296916 scopus 로고    scopus 로고
    • DPP4 inhibition in human kidney proximal tubular cells-renoprotection in diabetic nephropathy? J
    • Panchapakesan, U., Gross, S., Komala, M.G., Pegg, K. and Pollock, C.A. (2013) DPP4 inhibition in human kidney proximal tubular cells-renoprotection in diabetic nephropathy? J. Diabetes Metab. S9, 007, https://doi.org/10.4172/2155-6156.S9-007
    • (2013) Diabetes Metab , vol.S9 , pp. 7
    • Panchapakesan, U.1    Gross, S.2    Komala, M.G.3    Pegg, K.4    Pollock, C.A.5
  • 112
    • 84951041234 scopus 로고    scopus 로고
    • Linagliptin limits high glucose induced conversion of latent to active TGFss through interaction with CIM6PR and limits renal tubulointerstitial fibronectin
    • Gangadharan Komala, M., Gross, S., Zaky, A., Pollock, C. and Panchapakesan, U. (2015) Linagliptin limits high glucose induced conversion of latent to active TGFss through interaction with CIM6PR and limits renal tubulointerstitial fibronectin. PLoS ONE 10, e0141143, https://doi.org/10.1371/journal.pone.0141143
    • (2015) PLoS ONE , vol.10
    • Gangadharan Komala, M.1    Gross, S.2    Zaky, A.3    Pollock, C.4    Panchapakesan, U.5
  • 113
    • 84957441808 scopus 로고    scopus 로고
    • Microvascular effects of the inhibition of dipeptidylpeptidase IV by linagliptin in nondiabetic hypertensive patients
    • Forst, T., Michelson, G., Diessel, S., Jahnke, J. and Kapitza, C. (2016) Microvascular effects of the inhibition of dipeptidylpeptidase IV by linagliptin in nondiabetic hypertensive patients. J. Hypertens. 34, 345-350, https://doi.org/10.1097/HJH.0000000000000776
    • (2016) J. Hypertens , vol.34 , pp. 345-350
    • Forst, T.1    Michelson, G.2    Diessel, S.3    Jahnke, J.4    Kapitza, C.5
  • 114
    • 84945940465 scopus 로고    scopus 로고
    • Advanced glycation end products: a molecular target for vascular complications in diabetes
    • Yamagishi, S., Nakamura, N., Suematsu, M., Kaseda, K. and Matsui, T. (2015) Advanced glycation end products: a molecular target for vascular complications in diabetes. Mol. Med. 21, S32-S40, https://doi.org/10.2119/molmed.2015.00067
    • (2015) Mol. Med , vol.21 , pp. S32-S40
    • Yamagishi, S.1    Nakamura, N.2    Suematsu, M.3    Kaseda, K.4    Matsui, T.5
  • 115
    • 84883084459 scopus 로고    scopus 로고
    • Advanced glycation end products evoke endothelial cell damage by stimulating soluble dipeptidyl peptidase-4 production and its interaction with mannose 6-phosphate/insulin-like growth factor II receptor
    • Ishibashi, Y., Matsui, T., Maeda, S., Higashimoto, Y. and Yamagishi, S. (2013) Advanced glycation end products evoke endothelial cell damage by stimulating soluble dipeptidyl peptidase-4 production and its interaction with mannose 6-phosphate/insulin-like growth factor II receptor. Cardiovasc. Diabetol. 12, 125, https://doi.org/10.1186/1475-2840-12-125
    • (2013) Cardiovasc. Diabetol , vol.12 , pp. 125
    • Ishibashi, Y.1    Matsui, T.2    Maeda, S.3    Higashimoto, Y.4    Yamagishi, S.5
  • 116
    • 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. and Matsui, T. (2015) Crosstalk between advanced glycation end products (AGEs)-receptor RAGE axis and dipeptidyl peptidase-4-incretin system in diabetic vascular complications. Cardiovasc. Diabetol. 14, 2, https://doi.org/10.1186/s12933-015-0176-5
    • (2015) Cardiovasc. Diabetol , vol.14 , pp. 2
    • Yamagishi, S.1    Fukami, K.2    Matsui, T.3
  • 117
    • 84866644965 scopus 로고    scopus 로고
    • Glucose-independent improvement of vascular dysfunction in experimental sepsis by dipeptidyl-peptidase 4 inhibition
    • Kroller-Schon, S., Knorr, M., Hausding, M., Oelze, M., Schuff, A., Schell, R. et al. (2012) Glucose-independent improvement of vascular dysfunction in experimental sepsis by dipeptidyl-peptidase 4 inhibition. Cardiovasc. Res. 96, 140-149, https://doi.org/10.1093/cvr/cvs246
    • (2012) Cardiovasc. Res , vol.96 , pp. 140-149
    • Kroller-Schon, S.1    Knorr, M.2    Hausding, M.3    Oelze, M.4    Schuff, A.5    Schell, R.6
  • 118
    • 84922404737 scopus 로고    scopus 로고
    • Linagliptin, a xanthine-based dipeptidyl peptidase-4 inhibitor, decreases serum uric acid levels in type 2 diabetic patients partly by suppressing xanthine oxidase activity
    • Yamagishi, S., Ishibashi, Y., Ojima, A., Sugiura, T. and Matsui, T. (2014) Linagliptin, a xanthine-based dipeptidyl peptidase-4 inhibitor, decreases serum uric acid levels in type 2 diabetic patients partly by suppressing xanthine oxidase activity. Int. J. Cardiol. 176, 550-552, https://doi.org/10.1016/j.ijcard.2014.07.023
    • (2014) Int. J. Cardiol , vol.176 , pp. 550-552
    • Yamagishi, S.1    Ishibashi, Y.2    Ojima, A.3    Sugiura, T.4    Matsui, T.5
  • 119
    • 85192028467 scopus 로고    scopus 로고
    • Linagliptin ameliorates kidney hypertrophy and albuminuria in diabetic mice in a glucose-independent manner via increased antioxidant function
    • (504-P)
    • Yang, Z., Spencer, N.Y. and Stanton, R.C. (2016) Linagliptin ameliorates kidney hypertrophy and albuminuria in diabetic mice in a glucose-independent manner via increased antioxidant function. Diabetes 65, A131-2 (504-P)
    • (2016) Diabetes , vol.65 , pp. A131-A132
    • Yang, Z.1    Spencer, N.Y.2    Stanton, R.C.3
  • 120
    • 84983751884 scopus 로고    scopus 로고
    • Vascular effects of linagliptin in non-obese diabetic mice are glucose-independent and involve positive modulation of the endothelial nitric oxide synthase (eNOS)/caveolin-1 (CAV-1) pathway
    • Vellecco, V., Mitidieri, E., Gargiulo, A., Brancaleone, V., Matassa, D., Klein, T. et al. (2016) Vascular effects of linagliptin in non-obese diabetic mice are glucose-independent and involve positive modulation of the endothelial nitric oxide synthase (eNOS)/caveolin-1 (CAV-1) pathway. Diabetes Obes. Metab. 18, 1236-1243, https://doi.org/10.1111/dom.12750
    • (2016) Diabetes Obes. Metab , vol.18 , pp. 1236-1243
    • Vellecco, V.1    Mitidieri, E.2    Gargiulo, A.3    Brancaleone, V.4    Matassa, D.5    Klein, T.6
  • 121
    • 84923574254 scopus 로고    scopus 로고
    • The DPP-4 inhibitor linagliptin and the GLP-1 receptor agonist exendin-4 improve endothelium-dependent relaxation of rat mesenteric arteries in the presence of high glucose
    • Salheen, S.M., Panchapakesan, U., Pollock, C.A. and Woodman, O.L. (2015) The DPP-4 inhibitor linagliptin and the GLP-1 receptor agonist exendin-4 improve endothelium-dependent relaxation of rat mesenteric arteries in the presence of high glucose. Pharmacol. Res. 94, 26-33, https://doi.org/10.1016/j.phrs.2015.02.003
    • (2015) Pharmacol. Res , vol.94 , pp. 26-33
    • Salheen, S.M.1    Panchapakesan, U.2    Pollock, C.A.3    Woodman, O.L.4
  • 122
    • 78149329921 scopus 로고    scopus 로고
    • SDF-1 provides morphological and functional protection against renal ischaemia/reperfusion injury
    • Stokman, G., Stroo, I., Claessen, N., Teske, G.J., Florquin, S. and Leemans, J.C. (2010) SDF-1 provides morphological and functional protection against renal ischaemia/reperfusion injury. Nephrol. Dial. Transplant. 25, 3852-3859, https://doi.org/10.1093/ndt/gfq311
    • (2010) Nephrol. Dial. Transplant , vol.25 , pp. 3852-3859
    • Stokman, G.1    Stroo, I.2    Claessen, N.3    Teske, G.J.4    Florquin, S.5    Leemans, J.C.6
  • 123
    • 17744387942 scopus 로고    scopus 로고
    • Renal SDF-1 signals mobilization and homing of CXCR4-positive cells to the kidney after ischemic injury
    • Togel, F., Isaac, J., Hu, Z., Weiss, K. and Westenfelder, C. (2005) Renal SDF-1 signals mobilization and homing of CXCR4-positive cells to the kidney after ischemic injury. Kidney Int. 67, 1772-1784, https://doi.org/10.1111/j.1523-1755.2005.00275.x
    • (2005) Kidney Int , vol.67 , pp. 1772-1784
    • Togel, F.1    Isaac, J.2    Hu, Z.3    Weiss, K.4    Westenfelder, C.5
  • 124
    • 84878587722 scopus 로고    scopus 로고
    • The novel DPP-4 inhibitors linagliptin and BI 14361 reduce infarct size after myocardial ischemia/reperfusion in rats
    • Hocher, B., Sharkovska, Y., Mark, M., Klein, T. and Pfab, T. (2013) The novel DPP-4 inhibitors linagliptin and BI 14361 reduce infarct size after myocardial ischemia/reperfusion in rats. Int. J. Cardiol. 167, 87-93, https://doi.org/10.1016/j.ijcard.2011.12.007
    • (2013) Int. J. Cardiol , vol.167 , pp. 87-93
    • Hocher, B.1    Sharkovska, Y.2    Mark, M.3    Klein, T.4    Pfab, T.5
  • 125
    • 84959386239 scopus 로고    scopus 로고
    • Acute effects of linagliptin on progenitor cells, monocyte phenotypes, and soluble mediators in type 2 diabetes
    • Fadini, G.P., Bonora, B.M., Cappellari, R., Menegazzo, L., Vedovato, M., Iori, E. et al. (2016) Acute effects of linagliptin on progenitor cells, monocyte phenotypes, and soluble mediators in type 2 diabetes. J. Clin. Endocrinol. Metab. 101, 748-756, https://doi.org/10.1210/jc.2015-3716
    • (2016) J. Clin. Endocrinol. Metab , vol.101 , pp. 748-756
    • Fadini, G.P.1    Bonora, B.M.2    Cappellari, R.3    Menegazzo, L.4    Vedovato, M.5    Iori, E.6
  • 126
    • 85028082197 scopus 로고    scopus 로고
    • Dipeptidyl peptidase 4 inhibition stimulates distal tubular natriuresis and increases in circulating SDF-1alpha1-67 in patients with type 2 diabetes
    • Lovshin, J.A., Rajasekeran, H., Lytvyn, Y., Lovblom, L.E., Khan, S., Alemu, R. et al. (2017) Dipeptidyl peptidase 4 inhibition stimulates distal tubular natriuresis and increases in circulating SDF-1alpha1-67 in patients with type 2 diabetes. Diabetes Care 40, 1073-1081, https://doi.org/10.2337/dc17-0061
    • (2017) Diabetes Care , vol.40 , pp. 1073-1081
    • Lovshin, J.A.1    Rajasekeran, H.2    Lytvyn, Y.3    Lovblom, L.E.4    Khan, S.5    Alemu, R.6
  • 127
    • 85029721534 scopus 로고    scopus 로고
    • The oral dipeptidyl-peptidase-4 inhibitor sitagliptin increases circulating levels of stromal-derived factor-1 alpha
    • Papazafiropoulou, A.K., Papanas, N., Trikkalinou, A., Fousteris, E. and Melidonis, A. (2017) The oral dipeptidyl-peptidase-4 inhibitor sitagliptin increases circulating levels of stromal-derived factor-1 alpha. Exp. Clin. Endocrinol. Diabetes, https://doi.org/10.1055/s-0043-118748
    • (2017) Exp. Clin. Endocrinol. Diabetes
    • Papazafiropoulou, A.K.1    Papanas, N.2    Trikkalinou, A.3    Fousteris, E.4    Melidonis, A.5
  • 129
    • 84908295120 scopus 로고    scopus 로고
    • Intestinal regulation of urinary sodium excretion and the pathophysiology of diabetic kidney disease: a focus on glucagon-like peptide 1 and dipeptidyl peptidase 4
    • Vallon, V. and Docherty, N.G. (2014) Intestinal regulation of urinary sodium excretion and the pathophysiology of diabetic kidney disease: a focus on glucagon-like peptide 1 and dipeptidyl peptidase 4. Exp. Physiol. 99, 1140-1145, https://doi.org/10.1113/expphysiol.2014.078766
    • (2014) Exp. Physiol , vol.99 , pp. 1140-1145
    • Vallon, V.1    Docherty, N.G.2
  • 130
    • 84865576863 scopus 로고    scopus 로고
    • Renal and cardiac effects of DPP4 inhibitors-from preclinical development to clinical research
    • Hocher, B., Reichetzeder, C. and Alter, M.L. (2012) Renal and cardiac effects of DPP4 inhibitors-from preclinical development to clinical research. Kidney Blood Press. Res. 36, 65-84, https://doi.org/10.1159/000339028
    • (2012) Kidney Blood Press. Res , vol.36 , pp. 65-84
    • Hocher, B.1    Reichetzeder, C.2    Alter, M.L.3
  • 131
    • 81355124070 scopus 로고    scopus 로고
    • Effects of DPP-4 inhibitors on the heart in a rat model of uremic cardiomyopathy
    • Chaykovska, L., von Websky, K., Rahnenfuhrer, J., Alter, M., Heiden, S., Fuchs, H. et al. (2011) Effects of DPP-4 inhibitors on the heart in a rat model of uremic cardiomyopathy. PLoS ONE 6, e27861, https://doi.org/10.1371/journal.pone.0027861
    • (2011) PLoS ONE , vol.6
    • Chaykovska, L.1    Von Websky, K.2    Rahnenfuhrer, J.3    Alter, M.4    Heiden, S.5    Fuchs, H.6
  • 132
    • 84902185713 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibition improves left ventricular function in chronic kidney disease
    • Connelly, K.A., Bowskill, B.B., Advani, S.L., Thai, K., Chen, L.H., Kabir, M.G. et al. (2014) Dipeptidyl peptidase-4 inhibition improves left ventricular function in chronic kidney disease. Clin. Invest. Med. 37, E172-E185, https://doi.org/10.25011/cim.v37i3.21384
    • (2014) Clin. Invest. Med , vol.37 , pp. E172-E185
    • Connelly, K.A.1    Bowskill, B.B.2    Advani, S.L.3    Thai, K.4    Chen, L.H.5    Kabir, M.G.6
  • 133
    • 84901303279 scopus 로고    scopus 로고
    • DPP-4 inhibitors-renoprotection in diabetic nephropathy?
    • Panchapakesan, U. and Pollock, C.A. (2014) DPP-4 inhibitors-renoprotection in diabetic nephropathy? Diabetes 63, 1829-1830, https://doi.org/10.2337/db14-0366
    • (2014) Diabetes , vol.63 , pp. 1829-1830
    • Panchapakesan, U.1    Pollock, C.A.2
  • 134
    • 84983591619 scopus 로고    scopus 로고
    • Comparative analysis of binding kinetics and thermodynamics of dipeptidyl peptidase-4 inhibitors and their relationship to structure
    • Schnapp, G., Klein, T., Hoevels, Y., Bakker, R.A. and Nar, H. (2016) Comparative analysis of binding kinetics and thermodynamics of dipeptidyl peptidase-4 inhibitors and their relationship to structure. J. Med. Chem. 59, 7466-7477, https://doi.org/10.1021/acs.jmedchem.6b00475
    • (2016) J. Med. Chem , vol.59 , pp. 7466-7477
    • Schnapp, G.1    Klein, T.2    Hoevels, Y.3    Bakker, R.A.4    Nar, H.5
  • 135
    • 70349733673 scopus 로고    scopus 로고
    • Tissue distribution of the novel DPP-4 inhibitor BI 1356 is dominated by saturable binding to its target in rats
    • Fuchs, H., Binder, R. and Greischel, A. (2009) Tissue distribution of the novel DPP-4 inhibitor BI 1356 is dominated by saturable binding to its target in rats. Biopharm. Drug Dispos. 30, 229-240, https://doi.org/10.1002/bdd.662
    • (2009) Biopharm. Drug Dispos , vol.30 , pp. 229-240
    • Fuchs, H.1    Binder, R.2    Greischel, A.3
  • 136
    • 77956007404 scopus 로고    scopus 로고
    • The dipeptidyl peptidase-4 inhibitor linagliptin exhibits time-and dose-dependent localization in kidney, liver, and intestine after intravenous dosing: results from high resolution autoradiography in rats
    • Greischel, A., Binder, R. and Baierl, J. (2010) The dipeptidyl peptidase-4 inhibitor linagliptin exhibits time-and dose-dependent localization in kidney, liver, and intestine after intravenous dosing: results from high resolution autoradiography in rats. Drug Metab. Dispos. 38, 1443-1448, https://doi.org/10.1124/dmd.110.034199
    • (2010) Drug Metab. Dispos , vol.38 , pp. 1443-1448
    • Greischel, A.1    Binder, R.2    Baierl, J.3
  • 137
    • 41149118550 scopus 로고    scopus 로고
    • (R)-8-(3-amino-piperidin-1-yl)-7-but-2-ynyl-3-methyl-1-(4-methyl-quinazolin-2-ylm ethyl)-3,7-dihydro-purine-2,6-dione (BI 1356), a novel xanthine-based dipeptidyl peptidase 4 inhibitor, has a superior potency and longer duration of action compared with other dipeptidyl peptidase-4 inhibitors
    • Thomas, L., Eckhardt, M., Langkopf, E., Tadayyon, M., Himmelsbach, F. and Mark, M. (2008) (R)-8-(3-amino-piperidin-1-yl)-7-but-2-ynyl-3-methyl-1-(4-methyl-quinazolin-2-ylm ethyl)-3,7-dihydro-purine-2,6-dione (BI 1356), a novel xanthine-based dipeptidyl peptidase 4 inhibitor, has a superior potency and longer duration of action compared with other dipeptidyl peptidase-4 inhibitors. J. Pharmacol. Exp. Ther. 325, 175-182, https://doi.org/10.1124/jpet.107.135723
    • (2008) J. Pharmacol. Exp. Ther , vol.325 , pp. 175-182
    • Thomas, L.1    Eckhardt, M.2    Langkopf, E.3    Tadayyon, M.4    Himmelsbach, F.5    Mark, M.6
  • 138
    • 85192027152 scopus 로고    scopus 로고
    • The binding kinetics of linagliptin uniquely mediate its kidney-specific DPP-4 inhibition
    • (54-OR)
    • Luippold, G., Klein, T., Mark, M., Amann, K. and Daniel, C. (2017) The binding kinetics of linagliptin uniquely mediate its kidney-specific DPP-4 inhibition. Diabetes 66, A14 (54-OR)
    • (2017) Diabetes , vol.66
    • Luippold, G.1    Klein, T.2    Mark, M.3    Amann, K.4    Daniel, C.5
  • 139
    • 84906957817 scopus 로고    scopus 로고
    • Significance of vascular dipeptidyl peptidase-4 inhibition on vascular protection in Zucker diabetic fatty rats
    • Takai, S., Sakonjo, H. and Jin, D. (2014) Significance of vascular dipeptidyl peptidase-4 inhibition on vascular protection in Zucker diabetic fatty rats. J. Pharmacol. Sci. 125, 386-393, https://doi.org/10.1254/jphs.14052FP
    • (2014) J. Pharmacol. Sci , vol.125 , pp. 386-393
    • Takai, S.1    Sakonjo, H.2    Jin, D.3
  • 140
    • 84958890242 scopus 로고    scopus 로고
    • Linagliptin but not sitagliptin inhibited transforming growth factor-beta2-induced endothelial DPP-4 activity and the endothelial-mesenchymal transition
    • Shi, S., Kanasaki, K. and Koya, D. (2016) Linagliptin but not sitagliptin inhibited transforming growth factor-beta2-induced endothelial DPP-4 activity and the endothelial-mesenchymal transition. Biochem. Biophys. Res. Commun. 471, 184-190, https://doi.org/10.1016/j.bbrc.2016.01.154
    • (2016) Biochem. Biophys. Res. Commun , vol.471 , pp. 184-190
    • Shi, S.1    Kanasaki, K.2    Koya, D.3
  • 141
    • 85020212494 scopus 로고    scopus 로고
    • Head-to-head comparison of structurally unrelated dipeptidyl peptidase 4 inhibitors in the setting of renal ischemia reperfusion injury
    • Reichetzeder, C., von Websky, K., Tsuprykov, O., Mohagheghi Samarin, A., Falke, L.G., Dwi Putra, S.E. et al. (2017) Head-to-head comparison of structurally unrelated dipeptidyl peptidase 4 inhibitors in the setting of renal ischemia reperfusion injury. Br. J. Pharmacol. 174, 2273-2286, https://doi.org/10.1111/bph.13822
    • (2017) Br. J. Pharmacol , vol.174 , pp. 2273-2286
    • Reichetzeder, C.1    Von Websky, K.2    Tsuprykov, O.3    Mohagheghi Samarin, A.4    Falke, L.G.5    Dwi Putra, S.E.6
  • 142
    • 85008230357 scopus 로고    scopus 로고
    • Effect of saxagliptin on renal outcomes in the SAVOR-TIMI 53 trial
    • Mosenzon, O., Leibowitz, G., Bhatt, D.L., Cahn, A., Hirshberg, B., Wei, C. et al. (2017) Effect of saxagliptin on renal outcomes in the SAVOR-TIMI 53 trial. Diabetes Care 40, 69-76, https://doi.org/10.2337/dc16-0621
    • (2017) Diabetes Care , vol.40 , pp. 69-76
    • Mosenzon, O.1    Leibowitz, G.2    Bhatt, D.L.3    Cahn, A.4    Hirshberg, B.5    Wei, C.6
  • 143
    • 85006117462 scopus 로고    scopus 로고
    • Effect of sitagliptin on kidney function and respective cardiovascular outcomes in type 2 diabetes: outcomes from TECOS
    • Cornel, J.H., Bakris, G.L., Stevens, S.R., Alvarsson, M., Bax, W.A., Chuang, L.M. et al. (2016) Effect of sitagliptin on kidney function and respective cardiovascular outcomes in type 2 diabetes: outcomes from TECOS. Diabetes Care 39, 2304-2310, https://doi.org/10.2337/dc16-1415
    • (2016) Diabetes Care , vol.39 , pp. 2304-2310
    • Cornel, J.H.1    Bakris, G.L.2    Stevens, S.R.3    Alvarsson, M.4    Bax, W.A.5    Chuang, L.M.6
  • 145
    • 84994361897 scopus 로고    scopus 로고
    • Renal effects of DPP-4 inhibitor sitagliptin or GLP-1 receptor agonist liraglutide in overweight patients with type 2 diabetes: a 12-week, randomized, double-blind, placebo-controlled trial
    • Tonneijck, L., Smits, M.M., Muskiet, M.H., Hoekstra, T., Kramer, M.H., Danser, A.H. et al. (2016) Renal effects of DPP-4 inhibitor sitagliptin or GLP-1 receptor agonist liraglutide in overweight patients with type 2 diabetes: a 12-week, randomized, double-blind, placebo-controlled trial. Diabetes Care 39, 2042-2050, https://doi.org/10.2337/dc16-1371
    • (2016) Diabetes Care , vol.39 , pp. 2042-2050
    • Tonneijck, L.1    Smits, M.M.2    Muskiet, M.H.3    Hoekstra, T.4    Kramer, M.H.5    Danser, A.H.6
  • 146
    • 85030093299 scopus 로고    scopus 로고
    • Dipeptidyl peptidase 4 inhibitor use is associated with a lower risk of incident acute kidney injury in patients with diabetes
    • Chao, C.T., Wang, J., Wu, H.Y., Chien, K.L. and Hung, K.Y. (2017) Dipeptidyl peptidase 4 inhibitor use is associated with a lower risk of incident acute kidney injury in patients with diabetes. Oncotarget 8, 53028-53040, https://doi.org/10.18632/oncotarget.18081
    • (2017) Oncotarget , vol.8 , pp. 53028-53040
    • Chao, C.T.1    Wang, J.2    Wu, H.Y.3    Chien, K.L.4    Hung, K.Y.5
  • 147
    • 84921908680 scopus 로고    scopus 로고
    • Treatment with the dipeptidyl peptidase-4 inhibitor linagliptin or placebo followed by glimepiride in patients with type 2 diabetes with moderate to severe renal impairment: a 52-week, randomized, double-blind clinical trial
    • Laakso, M., Rosenstock, J., Groop, P.H., Barnett, A.H., Gallwitz, B., Hehnke, U. et al. (2015) Treatment with the dipeptidyl peptidase-4 inhibitor linagliptin or placebo followed by glimepiride in patients with type 2 diabetes with moderate to severe renal impairment: a 52-week, randomized, double-blind clinical trial. Diabetes Care 38, e15-e17, https://doi.org/10.2337/dc14-1684
    • (2015) Diabetes Care , vol.38
    • Laakso, M.1    Rosenstock, J.2    Groop, P.H.3    Barnett, A.H.4    Gallwitz, B.5    Hehnke, U.6
  • 148
    • 84873864348 scopus 로고    scopus 로고
    • Long-term efficacy and safety of linagliptin in patients with type. diabetes and severe renal impairment: a 1-year, randomized, double-blind, placebo-controlled study
    • McGill, J.B., Sloan, L., Newman, J., Patel, S., Sauce, C., von Eynatten, M. et al. (2013) Long-term efficacy and safety of linagliptin in patients with type 2. diabetes and severe renal impairment: a 1-year, randomized, double-blind, placebo-controlled study. Diabetes Care 36, 237-244, https://doi.org/10.2337/dc12-0706
    • (2013) Diabetes Care , vol.36 , pp. 237-244
    • Mcgill, J.B.1    Sloan, L.2    Newman, J.3    Patel, S.4    Sauce, C.5    Von Eynatten, M.6
  • 149
    • 84875907876 scopus 로고    scopus 로고
    • Efficacy and safety of linagliptin in type 2 diabetes subjects at high risk for renal and cardiovascular disease: a pooled analysis of six phase III clinical trials
    • von Eynatten, M., Gong, Y., Emser, A. and Woerle, H.J. (2013) Efficacy and safety of linagliptin in type 2 diabetes subjects at high risk for renal and cardiovascular disease: a pooled analysis of six phase III clinical trials. Cardiovasc. Diabetol. 12, 60, https://doi.org/10.1186/1475-2840-12-60
    • (2013) Cardiovasc. Diabetol , vol.12 , pp. 60
    • Von Eynatten, M.1    Gong, Y.2    Emser, A.3    Woerle, H.J.4
  • 150
    • 84890476805 scopus 로고    scopus 로고
    • Linagliptin lowers albuminuria on top of recommended standard treatment in patients with type 2 diabetes and renal dysfunction
    • Groop, P.H., Cooper, M.E., Perkovic, V., Emser, A., Woerle, H.J. and von Eynatten, M. (2013) Linagliptin lowers albuminuria on top of recommended standard treatment in patients with type 2 diabetes and renal dysfunction. Diabetes Care 36, 3460-3468, https://doi.org/10.2337/dc13-0323
    • (2013) Diabetes Care , vol.36 , 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
  • 151
    • 84939565970 scopus 로고    scopus 로고
    • Kidney disease end points in a pooled analysis of individual patient-level data from a large clinical trials program of the dipeptidyl peptidase 4 inhibitor linagliptin in type 2 diabetes
    • Cooper, M.E., Perkovic, V., McGill, J.B., Groop, P.H., Wanner, C., Rosenstock, J. et al. (2015) Kidney disease end points in a pooled analysis of individual patient-level data from a large clinical trials program of the dipeptidyl peptidase 4 inhibitor linagliptin in type 2 diabetes. Am. J. Kidney Dis. 66, 441-449, https://doi.org/10.1053/j.ajkd.2015.03.024
    • (2015) Am. J. Kidney Dis , vol.66 , pp. 441-449
    • Cooper, M.E.1    Perkovic, V.2    Mcgill, J.B.3    Groop, P.H.4    Wanner, C.5    Rosenstock, J.6
  • 152
    • 85026454641 scopus 로고    scopus 로고
    • Linagliptin and its effects on hyperglycaemia and albuminuria in patients with type 2 diabetes and renal dysfunction: the randomized MARLINA-T2D trial
    • Groop, P.H., Cooper, M.E., Perkovic, V., Hocher, B., Kanasaki, K., Haneda, M. et al. (2017) Linagliptin and its effects on hyperglycaemia and albuminuria in patients with type 2 diabetes and renal dysfunction: the randomized MARLINA-T2D trial. Diabetes Obes. Metab. 19, 1610-1619, https://doi.org/10.1111/dom.13041
    • (2017) Diabetes Obes. Metab , vol.19 , pp. 1610-1619
    • Groop, P.H.1    Cooper, M.E.2    Perkovic, V.3    Hocher, B.4    Kanasaki, K.5    Haneda, M.6
  • 153
    • 84984791882 scopus 로고    scopus 로고
    • Effects of linagliptin on renal endothelial function in patients with type 2 diabetes: a randomised clinical trial
    • Ott, C., Kistner, I., Keller, M., Friedrich, S., Willam, C., Bramlage, P. et al. (2016) Effects of linagliptin on renal endothelial function in patients with type 2 diabetes: a randomised clinical trial. Diabetologia 59, 2579-2587, https://doi.org/10.1007/s00125-016-4083-4
    • (2016) Diabetologia , vol.59 , pp. 2579-2587
    • Ott, C.1    Kistner, I.2    Keller, M.3    Friedrich, S.4    Willam, C.5    Bramlage, P.6
  • 154
    • 0033982133 scopus 로고    scopus 로고
    • Nitric oxide synthase isoforms and glomerular hyperfiltration in early diabetic nephropathy
    • Veelken, R., Hilgers, K.F., Hartner, A., Haas, A., Bohmer, K.P. and Sterzel, R.B. (2000) Nitric oxide synthase isoforms and glomerular hyperfiltration in early diabetic nephropathy. J. Am. Soc. Nephrol. 11, 71-79
    • (2000) J. Am. Soc. Nephrol , vol.11 , pp. 71-79
    • Veelken, R.1    Hilgers, K.F.2    Hartner, A.3    Haas, A.4    Bohmer, K.P.5    Sterzel, R.B.6
  • 155
    • 37349073089 scopus 로고    scopus 로고
    • Basal nitric oxide synthase activity is a major determinant of glomerular haemodynamics in humans
    • Schlaich, M.P., Schmitt, D., Ott, C., Schmidt, B.M. and Schmieder, R.E. (2008) Basal nitric oxide synthase activity is a major determinant of glomerular haemodynamics in humans. J. Hypertens. 26, 110-116, https://doi.org/10.1097/HJH.0b013e3282f1a93e
    • (2008) J. Hypertens , vol.26 , pp. 110-116
    • Schlaich, M.P.1    Schmitt, D.2    Ott, C.3    Schmidt, B.M.4    Schmieder, R.E.5
  • 156
    • 85010190524 scopus 로고    scopus 로고
    • A randomised, active-and placebo-controlled, three-period crossover trial to investigate short-term effects of the dipeptidyl peptidase-4 inhibitor linagliptin on macro-and microvascular endothelial function in type 2 diabetes
    • Jax, T., Stirban, A., Terjung, A., Esmaeili, H., Berk, A., Thiemann, S. et al. (2017) A randomised, active-and placebo-controlled, three-period crossover trial to investigate short-term effects of the dipeptidyl peptidase-4 inhibitor linagliptin on macro-and microvascular endothelial function in type 2 diabetes. Cardiovasc. Diabetol. 16, 13, https://doi.org/10.1186/s12933-016-0493-3
    • (2017) Cardiovasc. Diabetol , vol.16 , pp. 13
    • Jax, T.1    Stirban, A.2    Terjung, A.3    Esmaeili, H.4    Berk, A.5    Thiemann, S.6
  • 157
    • 85015633317 scopus 로고    scopus 로고
    • Metabolomics for clinical use and research in chronic kidney disease
    • Hocher, B. and Adamski, J. (2017) Metabolomics for clinical use and research in chronic kidney disease. Nat. Rev. Nephrol. 13, 269-284, https://doi.org/10.1038/nrneph.2017.30
    • (2017) Nat. Rev. Nephrol , vol.13 , pp. 269-284
    • Hocher, B.1    Adamski, J.2
  • 158
    • 85046455753 scopus 로고    scopus 로고
    • CARMELINA R+ trial baseline characteristics: a cardiovascular and renal microvascular outcome trial with linagliptin in patients with type 2 diabetes at high vascular risk
    • (1284-P)
    • Rosenstock, J., Perkovic, V., Alexander, J.H., Cooper, M.E., Kahn, S.E., Marx, N. et al. (2017) CARMELINA R+ trial baseline characteristics: a cardiovascular and renal microvascular outcome trial with linagliptin in patients with type 2 diabetes at high vascular risk. Diabetes 66, A344 (1284-P)
    • (2017) Diabetes , vol.66
    • Rosenstock, J.1    Perkovic, V.2    Alexander, J.H.3    Cooper, M.E.4    Kahn, S.E.5    Marx, N.6


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