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Volumn 2015, Issue , 2015, Pages

Proteases and protease inhibitors of urinary extracellular vesicles in diabetic nephropathy

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN B; CATHEPSIN H; CATHEPSIN L; CYSTATIN B; ELAFIN; MYELOBLASTIN; NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN; PROTEINASE; PROTEINASE INHIBITOR; PYROXYLIN; BIOLOGICAL MARKER; PEPTIDE HYDROLASE;

EID: 84926434307     PISSN: 23146745     EISSN: 23146753     Source Type: Journal    
DOI: 10.1155/2015/289734     Document Type: Article
Times cited : (53)

References (78)
  • 1
    • 84889022122 scopus 로고    scopus 로고
    • The growing prevalence of type 2 diabetes: Increased incidence or improved survival?
    • N. M. Maruthur, "The growing prevalence of type 2 diabetes: increased incidence or improved survival?" Current Diabetes Reports, Vol. 13, no. 6, pp. 786-794, 2013.
    • (2013) Current Diabetes Reports , vol.13 , Issue.6 , pp. 786-794
    • Maruthur, N.M.1
  • 4
    • 74549184137 scopus 로고    scopus 로고
    • World kidney day 2010: Diabetic kidney disease - Act now or pay later
    • R. C. Atkins and P. Zimmet, "World Kidney Day 2010: diabetic kidney disease - act now or pay later," The American Journal of Kidney Diseases, Vol. 55, no. 2, pp. 205-208, 2010.
    • (2010) The American Journal of Kidney Diseases , vol.55 , Issue.2 , pp. 205-208
    • Atkins, R.C.1    Zimmet, P.2
  • 5
    • 84872608671 scopus 로고    scopus 로고
    • Renal impairment and all-cause mortality in cardiovascular disease: Effect modification by type 2 diabetes mellitus
    • S. Selvarajah, C. S. P. M. Uiterwaal, J. Haniff et al., "Renal impairment and all-cause mortality in cardiovascular disease: effect modification by type 2 diabetes mellitus," European Journal of Clinical Investigation, Vol. 43, no. 2, pp. 198-207, 2013.
    • (2013) European Journal of Clinical Investigation , vol.43 , Issue.2 , pp. 198-207
    • Selvarajah, S.1    Uiterwaal, C.S.P.M.2    Haniff, J.3
  • 6
    • 79952701832 scopus 로고    scopus 로고
    • Glomerular filtration rate, albuminuria and risk of cardiovascular and all-cause mortality in type 2 diabetic individuals
    • G. Targher, G. Zoppini, M. Chonchol et al., "Glomerular filtration rate, albuminuria and risk of cardiovascular and all-cause mortality in type 2 diabetic individuals," Nutrition, Metabolism and Cardiovascular Diseases, Vol. 21, no. 4, pp. 294-301, 2011.
    • (2011) Nutrition, Metabolism and Cardiovascular Diseases , vol.21 , Issue.4 , pp. 294-301
    • Targher, G.1    Zoppini, G.2    Chonchol, M.3
  • 7
    • 67650217963 scopus 로고    scopus 로고
    • The presence and severity of chronic kidney disease predicts all-cause mortality in type 1 diabetes
    • P.-H. Groop, M. C. Thomas, J. L. Moran et al., "The presence and severity of chronic kidney disease predicts all-cause mortality in type 1 diabetes," Diabetes, Vol. 58, no. 7, pp. 1651-1658, 2009.
    • (2009) Diabetes , vol.58 , Issue.7 , pp. 1651-1658
    • Groop, P.-H.1    Thomas, M.C.2    Moran, J.L.3
  • 9
    • 84875370568 scopus 로고    scopus 로고
    • Molecular mechanisms in the pathogenesis of diabetic nephropathy: An update
    • M. K. Arora and U. K. Singh, "Molecular mechanisms in the pathogenesis of diabetic nephropathy: an update," Vascular Pharmacology, Vol. 58, no. 4, pp. 259-271, 2013.
    • (2013) Vascular Pharmacology , vol.58 , Issue.4 , pp. 259-271
    • Arora, M.K.1    Singh, U.K.2
  • 11
    • 84867375222 scopus 로고    scopus 로고
    • High risk of ESRD in type 1 diabetes: New strategies are needed to retard progressive renal function decline
    • A. S. Krolewski and J. V. Bonventre, "High risk of ESRD in type 1 diabetes: new strategies are needed to retard progressive renal function decline," Seminars in Nephrology, Vol. 32, no. 5, pp. 407-414, 2012.
    • (2012) Seminars in Nephrology , vol.32 , Issue.5 , pp. 407-414
    • Krolewski, A.S.1    Bonventre, J.V.2
  • 12
    • 70349235678 scopus 로고    scopus 로고
    • Integrating albuminuria and GFR in the assessment of diabetic nephropathy
    • G. Jerums, S. Panagiotopoulos, E. Premaratne, and R. J. MacIsaac, "Integrating albuminuria and GFR in the assessment of diabetic nephropathy," Nature Reviews Nephrology, Vol. 5, no. 7, pp. 397-406, 2009.
    • (2009) Nature Reviews Nephrology , vol.5 , Issue.7 , pp. 397-406
    • Jerums, G.1    Panagiotopoulos, S.2    Premaratne, E.3    MacIsaac, R.J.4
  • 13
    • 63149173251 scopus 로고    scopus 로고
    • Standards of medical care in diabetes
    • American Diabetes Association, "Standards of medical care in diabetes," Diabetes Care, Vol. 32, supplement 1, pp. S13-S61, 2009.
    • (2009) Diabetes Care , vol.32 , pp. S13-S61
  • 14
    • 45849107043 scopus 로고    scopus 로고
    • Guideline 1: Screening and diagnosis of diabetic kidney disease
    • KDOQI, "Guideline 1: screening and diagnosis of diabetic kidney disease," The American Journal of Kidney Diseases, Vol. 49, supplement 2, pp. S42-S61, 2009.
    • (2009) The American Journal of Kidney Diseases , vol.49 , pp. S42-S61
    • KDOQI1
  • 15
    • 0037213037 scopus 로고    scopus 로고
    • Development and progression of nephropathy in type 2 diabetes: The united kingdom prospective diabetes study (UKPDS 64)
    • A. I. Adler, R. J. Stevens, S. E. Manley, R. W. Bilous, C. A. Cull, and R. R. Holman, "Development and progression of nephropathy in type 2 diabetes: the United Kingdom Prospective Diabetes Study (UKPDS 64)," Kidney International, Vol. 63, no. 1, pp. 225-232, 2003.
    • (2003) Kidney International , vol.63 , Issue.1 , pp. 225-232
    • Adler, A.I.1    Stevens, R.J.2    Manley, S.E.3    Bilous, R.W.4    Cull, C.A.5    Holman, R.R.6
  • 16
    • 32444451549 scopus 로고    scopus 로고
    • Mechanisms of progression and regression of renal lesions of chronic nephropathies and diabetes
    • G. Remuzzi, A. Benigni, and A. Remuzzi, "Mechanisms of progression and regression of renal lesions of chronic nephropathies and diabetes," Journal of Clinical Investigation, Vol. 116, no. 2, pp. 288-296, 2006.
    • (2006) Journal of Clinical Investigation , vol.116 , Issue.2 , pp. 288-296
    • Remuzzi, G.1    Benigni, A.2    Remuzzi, A.3
  • 17
    • 72949106696 scopus 로고    scopus 로고
    • In patients with type 1 diabetes and newonset microalbuminuria the development of advanced chronic kidney disease may not require progression to proteinuria
    • B. A. Perkins, L. H. Ficociello, B. Roshan, J. H. Warram, and A. S. Krolewski, "In patients with type 1 diabetes and newonset microalbuminuria the development of advanced chronic kidney disease may not require progression to proteinuria," Kidney International, Vol. 77, no. 1, pp. 57-64, 2010.
    • (2010) Kidney International , vol.77 , Issue.1 , pp. 57-64
    • Perkins, B.A.1    Ficociello, L.H.2    Roshan, B.3    Warram, J.H.4    Krolewski, A.S.5
  • 20
    • 77954244728 scopus 로고    scopus 로고
    • Nucleic acids within urinary exosomes/microvesicles are potential biomarkers for renal disease
    • K. C. Miranda, D. T. Bond, M. McKee et al., "Nucleic acids within urinary exosomes/microvesicles are potential biomarkers for renal disease," Kidney International, Vol. 78, no. 2, pp. 191-199, 2010.
    • (2010) Kidney International , vol.78 , Issue.2 , pp. 191-199
    • Miranda, K.C.1    Bond, D.T.2    McKee, M.3
  • 21
    • 84874377202 scopus 로고    scopus 로고
    • Extracellular vesicles: Exosomes, microvesicles, and friends
    • G. Raposo and W. Stoorvogel, "Extracellular vesicles: exosomes, microvesicles, and friends," The Journal of Cell Biology, Vol. 200, no. 4, pp. 373-383, 2013.
    • (2013) The Journal of Cell Biology , vol.200 , Issue.4 , pp. 373-383
    • Raposo, G.1    Stoorvogel, W.2
  • 22
    • 84874355076 scopus 로고    scopus 로고
    • Biogenesis of extracellular vesicles (EV): Exosomes, microvesicles, retrovirus-like vesicles, and apoptotic bodies
    • J. C. Akers, D. Gonda, R. Kim, B. S. Carter, and C. C. Chen, "Biogenesis of extracellular vesicles (EV): exosomes, microvesicles, retrovirus-like vesicles, and apoptotic bodies," Journal of Neuro-Oncology, Vol. 113, no. 1, pp. 1-11, 2013.
    • (2013) Journal of Neuro-Oncology , vol.113 , Issue.1 , pp. 1-11
    • Akers, J.C.1    Gonda, D.2    Kim, R.3    Carter, B.S.4    Chen, C.C.5
  • 23
    • 84866718544 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV is a potential molecular biomarker in diabetic kidney disease
    • A. L. Sun, J. T. Deng, G. J. Guan et al., "Dipeptidyl peptidase-IV is a potential molecular biomarker in diabetic kidney disease," Diabetes and Vascular Disease Research, Vol. 9, no. 4, pp. 301-308, 2012.
    • (2012) Diabetes and Vascular Disease Research , vol.9 , Issue.4 , pp. 301-308
    • Sun, A.L.1    Deng, J.T.2    Guan, G.J.3
  • 24
    • 84888098593 scopus 로고    scopus 로고
    • Diabetic nephropathy induces changes in the proteome of human urinary exosomes as revealed by label-free comparative analysis
    • I. Zubiri, M. Posada-Ayala, A. Sanz-Maroto et al., "Diabetic nephropathy induces changes in the proteome of human urinary exosomes as revealed by label-free comparative analysis," Journal of Proteomics, Vol. 96, pp. 92-102, 2014.
    • (2014) Journal of Proteomics , vol.96 , pp. 92-102
    • Zubiri, I.1    Posada-Ayala, M.2    Sanz-Maroto, A.3
  • 25
    • 84892387470 scopus 로고    scopus 로고
    • Urinary exosomal MicroRNAs in incipient diabetic nephropathy
    • F. Barutta, M. Tricarico, A. Corbelli et al., "Urinary exosomal MicroRNAs in incipient diabetic nephropathy," PLoS ONE, Vol. 8, no. 11, Article ID e73798, 2013.
    • (2013) PLoS ONE , vol.8 , Issue.11
    • Barutta, F.1    Tricarico, M.2    Corbelli, A.3
  • 26
    • 84940186999 scopus 로고    scopus 로고
    • A simplified method to recover urinary vesicles for clinical applications
    • L. Musante, D. Tataruch, D. Gu et al., "A simplified method to recover urinary vesicles for clinical applications," Scientific Reports, Vol. 4, article 7532, 2014.
    • (2014) Scientific Reports , vol.4
    • Musante, L.1    Tataruch, D.2    Gu, D.3
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • M. M. Bradford, "A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding," Analytical Biochemistry, Vol. 72, no. 1-2, pp. 248-254, 1976.
    • (1976) Analytical Biochemistry , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U. K. Laemmli, "Cleavage of structural proteins during the assembly of the head of bacteriophage T4," Nature, Vol. 227, no. 15, pp. 680-685, 1970.
    • (1970) Nature , vol.227 , Issue.15 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 62449158218 scopus 로고    scopus 로고
    • Detergents and chaotropes for protein solubilization before two-dimensional electrophoresis
    • T. Rabilloud, "Detergents and chaotropes for protein solubilization before two-dimensional electrophoresis," Methods in Molecular Biology, Vol. 528, no. 4, pp. 259-267, 2009.
    • (2009) Methods in Molecular Biology , vol.528 , Issue.4 , pp. 259-267
    • Rabilloud, T.1
  • 30
    • 3042665732 scopus 로고    scopus 로고
    • Blue silver: A very sensitive colloidal coomassie G-250 staining for proteome analysis
    • G. Candiano, M. Bruschi, L. Musante et al., "Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis," Electrophoresis, Vol. 25, no. 9, pp. 1327-1333, 2004.
    • (2004) Electrophoresis , vol.25 , Issue.9 , pp. 1327-1333
    • Candiano, G.1    Bruschi, M.2    Musante, L.3
  • 31
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin, T. Staehelin, and J. Gordon, "Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications," Proceedings of the National Academy of Sciences of the United States of America, Vol. 76, no. 9, pp. 4350-4354, 1979.
    • (1979) Proceedings of the National Academy of Sciences of the United States of America , vol.76 , Issue.9 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 32
    • 0028345645 scopus 로고
    • Quantitative zymography: Detection of picogram quantities of gelatinases
    • D. E. Kleiner and W. G. Stetler-Stevenson, "Quantitative zymography: detection of picogram quantities of gelatinases," Analytical Biochemistry, Vol. 218, no. 2, pp. 325-329, 1994.
    • (1994) Analytical Biochemistry , vol.218 , Issue.2 , pp. 325-329
    • Kleiner, D.E.1    Stetler-Stevenson, W.G.2
  • 34
    • 25844445300 scopus 로고    scopus 로고
    • Differences between human proteinase 3 and neutrophil elastase and their murine homologues are relevant for murine model experiments
    • O. Wiesner, R. D. Litwiller, A. M. Hummel et al., "Differences between human proteinase 3 and neutrophil elastase and their murine homologues are relevant for murine model experiments," FEBS Letters, Vol. 579, no. 24, pp. 5305-5312, 2005.
    • (2005) FEBS Letters , vol.579 , Issue.24 , pp. 5305-5312
    • Wiesner, O.1    Litwiller, R.D.2    Hummel, A.M.3
  • 35
    • 0027501371 scopus 로고
    • Thrombospondin 1 is a tight-binding competitive inhibitor of neutrophil cathepsin G. Determination of the kinetic mechanism of inhibition and localization of cathepsin G binding to the thrombospondin 1 type 3 repeats
    • P. J. Hogg, D. A. Owensby, and C. N. Chesterman, "Thrombospondin 1 is a tight-binding competitive inhibitor of neutrophil cathepsin G. Determination of the kinetic mechanism of inhibition and localization of cathepsin G binding to the thrombospondin 1 type 3 repeats," The Journal of Biological Chemistry, Vol. 268, no. 29, pp. 21811-21818, 1993.
    • (1993) The Journal of Biological Chemistry , vol.268 , Issue.29 , pp. 21811-21818
    • Hogg, P.J.1    Owensby, D.A.2    Chesterman, C.N.3
  • 36
    • 0017074206 scopus 로고
    • A solvent system for delipidation of plasma or serum without protein precipitation
    • B. E. Cham and B. R. Knowles, "A solvent system for delipidation of plasma or serum without protein precipitation," The Journal of Lipid Research, Vol. 17, no. 2, pp. 176-181, 1976.
    • (1976) The Journal of Lipid Research , vol.17 , Issue.2 , pp. 176-181
    • Cham, B.E.1    Knowles, B.R.2
  • 37
    • 84861881296 scopus 로고    scopus 로고
    • The ubiquitin system, an immense realm
    • A. Varshavsky, "The ubiquitin system, an immense realm," Annual Review of Biochemistry, Vol. 81, no. 9, pp. 167-176, 2012.
    • (2012) Annual Review of Biochemistry , vol.81 , Issue.9 , pp. 167-176
    • Varshavsky, A.1
  • 38
    • 84860913822 scopus 로고    scopus 로고
    • The KUPKB: A novel web application to access multiomics data on kidney disease
    • J. Klein, S. Jupp, P. Moulos et al., "The KUPKB: a novel Web application to access multiomics data on kidney disease," The FASEB Journal, Vol. 26, no. 5, pp. 2145-2153, 2012.
    • (2012) The FASEB Journal , vol.26 , Issue.5 , pp. 2145-2153
    • Klein, J.1    Jupp, S.2    Moulos, P.3
  • 39
    • 63449086757 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Their potential role in the pathogenesis of diabetic nephropathy
    • K. M. Thrailkill, R. Clay Bunn, and J. L. Fowlkes, "Matrix metalloproteinases: their potential role in the pathogenesis of diabetic nephropathy," Endocrine, Vol. 35, no. 1, pp. 1-10, 2009.
    • (2009) Endocrine , vol.35 , Issue.1 , pp. 1-10
    • Thrailkill, K.M.1    Clay Bunn, R.2    Fowlkes, J.L.3
  • 41
    • 84903788735 scopus 로고    scopus 로고
    • Progressive diabetic nephropathy. How useful is microalbuminuria?: Contra
    • R. J. MacIsaac, E. I. Ekinci, and G. Jerums, "'Progressive diabetic nephropathy. How useful is microalbuminuria?: contra'," Kidney International, Vol. 86, no. 1, pp. 50-57, 2014.
    • (2014) Kidney International , vol.86 , Issue.1 , pp. 50-57
    • MacIsaac, R.J.1    Ekinci, E.I.2    Jerums, G.3
  • 42
    • 84892905009 scopus 로고    scopus 로고
    • Markers of and risk factors for the development and progression of diabetic kidney disease
    • R. J. Macisaac, E. I. Ekinci, and G. Jerums, "Markers of and risk factors for the development and progression of diabetic kidney disease," American Journal of Kidney Diseases, Vol. 63, no. 2, pp. S39-S62, 2014.
    • (2014) American Journal of Kidney Diseases , vol.63 , Issue.2 , pp. S39-S62
    • Macisaac, R.J.1    Ekinci, E.I.2    Jerums, G.3
  • 43
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • T. Wollert and J. H. Hurley, "Molecular mechanism of multivesicular body biogenesis by ESCRT complexes," Nature, Vol. 464, no. 7290, pp. 864-869, 2010.
    • (2010) Nature , vol.464 , Issue.7290 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2
  • 44
    • 59249089695 scopus 로고    scopus 로고
    • Shedding microvesicles: Artefacts no more
    • E. Cocucci, G. Racchetti, and J. Meldolesi, "Shedding microvesicles: artefacts no more," Trends in Cell Biology, Vol. 19, no. 2, pp. 43-51, 2009.
    • (2009) Trends in Cell Biology , vol.19 , Issue.2 , pp. 43-51
    • Cocucci, E.1    Racchetti, G.2    Meldolesi, J.3
  • 45
    • 33644838780 scopus 로고    scopus 로고
    • The how and why of exocytic vesicles
    • T. J. Greenwalt, "The how and why of exocytic vesicles," Transfusion, Vol. 46, no. 1, pp. 143-152, 2006.
    • (2006) Transfusion , vol.46 , Issue.1 , pp. 143-152
    • Greenwalt, T.J.1
  • 46
    • 34249302620 scopus 로고    scopus 로고
    • Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells
    • H. Valadi, K. Ekström, A. Bossios, M. Sjöstrand, J. J. Lee, and J. O. Lötvall, "Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells," Nature Cell Biology, Vol. 9, no. 6, pp. 654-659, 2007.
    • (2007) Nature Cell Biology , vol.9 , Issue.6 , pp. 654-659
    • Valadi, H.1    Ekström, K.2    Bossios, A.3    Sjöstrand, M.4    Lee, J.J.5    Lötvall, J.O.6
  • 47
    • 84878627393 scopus 로고    scopus 로고
    • Urinary exosomes: A reservoir for biomarker discovery and potential mediators of intrarenal signalling
    • J. W. Dear, J. M. Street, and M. A. Bailey, "Urinary exosomes: a reservoir for biomarker discovery and potential mediators of intrarenal signalling," Proteomics, Vol. 13, no. 10-11, pp. 1572-1580, 2013.
    • (2013) Proteomics , vol.13 , Issue.10-11 , pp. 1572-1580
    • Dear, J.W.1    Street, J.M.2    Bailey, M.A.3
  • 48
    • 84863327331 scopus 로고    scopus 로고
    • Elevated urinary excretion of immunoglobulins in nonproteinuric patients with type 1 diabetes
    • T. Gohda, W. H. Walker, P. Wolkow et al., "Elevated urinary excretion of immunoglobulins in nonproteinuric patients with type 1 diabetes," The American Journal of Physiology - Renal Physiology, Vol. 303, no. 1, pp. F157-F162, 2012.
    • (2012) The American Journal of Physiology - Renal Physiology , vol.303 , Issue.1 , pp. F157-F162
    • Gohda, T.1    Walker, W.H.2    Wolkow, P.3
  • 49
    • 0036145377 scopus 로고    scopus 로고
    • Higher urinary IgM excretion in type 2 diabetic nephropathy compared to type 1 diabetic nephropathy
    • O. Bakoush, J. Tencer, J. Tapia, B. Rippe, and O. Torffvit, "Higher urinary IgM excretion in type 2 diabetic nephropathy compared to type 1 diabetic nephropathy," Kidney International, Vol. 61, no. 1, pp. 203-208, 2002.
    • (2002) Kidney International , vol.61 , Issue.1 , pp. 203-208
    • Bakoush, O.1    Tencer, J.2    Tapia, J.3    Rippe, B.4    Torffvit, O.5
  • 51
    • 3142742326 scopus 로고    scopus 로고
    • Tal, a tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus budding
    • I. Amit, L. Yakir, M. Katz et al., "Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus budding," Genes and Development, Vol. 18, no. 14, pp. 1737-1752, 2004.
    • (2004) Genes and Development , vol.18 , Issue.14 , pp. 1737-1752
    • Amit, I.1    Yakir, L.2    Katz, M.3
  • 53
    • 77950487987 scopus 로고    scopus 로고
    • Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems
    • V. I. Korolchuk, F. M. Menzies, and D. C. Rubinsztein, "Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems," FEBS Letters, Vol. 584, no. 7, pp. 1393-1398, 2010.
    • (2010) FEBS Letters , vol.584 , Issue.7 , pp. 1393-1398
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 54
    • 84871706890 scopus 로고    scopus 로고
    • Role of GLP-1 and DPP-4 in diabetic nephropathy and cardiovascular disease
    • U. Panchapakesan, A. Mather, and C. Pollock, "Role of GLP-1 and DPP-4 in diabetic nephropathy and cardiovascular disease," Clinical Science, Vol. 124, no. 1, pp. 17-26, 2013.
    • (2013) Clinical Science , vol.124 , Issue.1 , pp. 17-26
    • Panchapakesan, U.1    Mather, A.2    Pollock, C.3
  • 55
    • 77955415650 scopus 로고    scopus 로고
    • Application of direct renin inhibition to chronic kidney disease
    • C. W. Mende, "Application of direct renin inhibition to chronic kidney disease," Cardiovascular Drugs and Therapy, Vol. 24, no. 2, pp. 139-149, 2010.
    • (2010) Cardiovascular Drugs and Therapy , vol.24 , Issue.2 , pp. 139-149
    • Mende, C.W.1
  • 56
    • 84870600452 scopus 로고    scopus 로고
    • Strong association between fibronectin accumulation and lowered cathepsin B activity in glomeruli of diabetic rats
    • A. Wyczalkowska-Tomasik, I. Bartlomiejczyk, B. Gornicka, and L. Paczek, "Strong association between fibronectin accumulation and lowered cathepsin B activity in glomeruli of diabetic rats," Journal of Physiology and Pharmacology, Vol. 63, no. 5, pp. 525-530, 2012.
    • (2012) Journal of Physiology and Pharmacology , vol.63 , Issue.5 , pp. 525-530
    • Wyczalkowska-Tomasik, A.1    Bartlomiejczyk, I.2    Gornicka, B.3    Paczek, L.4
  • 57
    • 0033001724 scopus 로고    scopus 로고
    • Decreased glomerular proteinase activity in the streptozotocin diabetic rat
    • R. H. Song, A. K. Singh, and D. J. Leehey, "Decreased glomerular proteinase activity in the streptozotocin diabetic rat," American Journal of Nephrology, Vol. 19, no. 3, pp. 441-446, 1999.
    • (1999) American Journal of Nephrology , vol.19 , Issue.3 , pp. 441-446
    • Song, R.H.1    Singh, A.K.2    Leehey, D.J.3
  • 58
    • 0025817602 scopus 로고
    • The cystatins: Protein inhibitors of cysteine proteinases
    • V. Turk and W. Bode, "The cystatins: protein inhibitors of cysteine proteinases," FEBS Letters, Vol. 285, no. 2, pp. 213-219, 1991.
    • (1991) FEBS Letters , vol.285 , Issue.2 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 60
    • 84890549685 scopus 로고    scopus 로고
    • 'Normoalbuminuric' diabetic nephropathy: Tubular damage and NGAL
    • A. Lacquaniti, V. Donato, B. Pintaudi et al., "'Normoalbuminuric' diabetic nephropathy: tubular damage and NGAL," Acta Diabetologica, Vol. 50, no. 6, pp. 935-942, 2013.
    • (2013) Acta Diabetologica , vol.50 , Issue.6 , pp. 935-942
    • Lacquaniti, A.1    Donato, V.2    Pintaudi, B.3
  • 61
    • 0141737555 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-IV expression and activity in human glomerular endothelial cells
    • L. Pala, E. Mannucci, A. Pezzatini et al., "Dipeptidyl peptidase-IV expression and activity in human glomerular endothelial cells," Biochemical and Biophysical Research Communications, Vol. 310, no. 1, pp. 28-31, 2003.
    • (2003) Biochemical and Biophysical Research Communications , vol.310 , Issue.1 , pp. 28-31
    • Pala, L.1    Mannucci, E.2    Pezzatini, A.3
  • 62
    • 0026014886 scopus 로고
    • Demonstration of glomerular DPP IV activity in kidney diseases
    • D. Stiller, H. Bahn, and C. August, "Demonstration of glomerular DPP IV activity in kidney diseases," Acta Histochemica, Vol. 91, no. 1, pp. 105-109, 1991.
    • (1991) Acta Histochemica , vol.91 , Issue.1 , pp. 105-109
    • Stiller, D.1    Bahn, H.2    August, C.3
  • 63
    • 0021879016 scopus 로고
    • Induction of dipeptidylpeptidase IV activity in human renal glomeruli - A histochemical study
    • M. Elleder and J. Stejskal, "Induction of dipeptidylpeptidase IV activity in human renal glomeruli - a histochemical study," Acta Histochemica, Vol. 77, no. 1, pp. 75-78, 1985.
    • (1985) Acta Histochemica , vol.77 , Issue.1 , pp. 75-78
    • Elleder, M.1    Stejskal, J.2
  • 64
    • 0028597971 scopus 로고
    • Detachment and cytolysis of human endothelial cells by proteinase 3
    • B. E. P. B. Ballieux, P. S. Hiemstra, N. Klar-Mohamad et al., "Detachment and cytolysis of human endothelial cells by proteinase 3," European Journal of Immunology, Vol. 24, no. 12, pp. 3211-3215, 1994.
    • (1994) European Journal of Immunology , vol.24 , Issue.12 , pp. 3211-3215
    • Ballieux, B.E.P.B.1    Hiemstra, P.S.2    Klar-Mohamad, N.3
  • 66
    • 84903748373 scopus 로고    scopus 로고
    • Proteomic characterization of serine hydrolase activity and composition in normal urine
    • M. Navarrete, J. Ho, O. Krokhin et al., "Proteomic characterization of serine hydrolase activity and composition in normal urine," Clinical Proteomics, Vol. 10, article 17, 2013.
    • (2013) Clinical Proteomics , vol.10
    • Navarrete, M.1    Ho, J.2    Krokhin, O.3
  • 67
    • 84865602319 scopus 로고    scopus 로고
    • Neutrophil serine proteases mediate inflammatory cell recruitment by glomerular endothelium and progression towards dysfunction
    • S. J. Kuravi, A. Bevins, S. C. Satchell et al., "Neutrophil serine proteases mediate inflammatory cell recruitment by glomerular endothelium and progression towards dysfunction," Nephrology Dialysis Transplantation, Vol. 27, no. 12, pp. 4331-4338, 2012.
    • (2012) Nephrology Dialysis Transplantation , vol.27 , Issue.12 , pp. 4331-4338
    • Kuravi, S.J.1    Bevins, A.2    Satchell, S.C.3
  • 68
    • 84903618700 scopus 로고    scopus 로고
    • Podocytes regulate neutrophil recruitment by glomerular endothelial cells via IL-6-mediated crosstalk
    • S. J. Kuravi, H. M. McGettrick, S. C. Satchell et al., "Podocytes regulate neutrophil recruitment by glomerular endothelial cells via IL-6-mediated crosstalk," The Journal of Immunology, Vol. 193, no. 1, pp. 234-243, 2014.
    • (2014) The Journal of Immunology , vol.193 , Issue.1 , pp. 234-243
    • Kuravi, S.J.1    McGettrick, H.M.2    Satchell, S.C.3
  • 69
    • 0000165143 scopus 로고    scopus 로고
    • Apoptosis of endothelial cells induced by the neutrophil serine proteases proteinase 3 and elastase
    • J. J. Yang, R. Kettritz, R. J. Falk, J. C. Jennette, and M. L. Gaido, "Apoptosis of endothelial cells induced by the neutrophil serine proteases proteinase 3 and elastase," The American Journal of Pathology, Vol. 149, no. 5, pp. 1617-1626, 1996.
    • (1996) The American Journal of Pathology , vol.149 , Issue.5 , pp. 1617-1626
    • Yang, J.J.1    Kettritz, R.2    Falk, R.J.3    Jennette, J.C.4    Gaido, M.L.5
  • 70
    • 0035135617 scopus 로고    scopus 로고
    • Internalization of proteinase 3 is concomitant with endothelial cell apoptosis and internalization of myeloperoxidase with generation of intracellular oxidants
    • J. J. Yang, G. A. Preston, W. F. Pendergraft et al., "Internalization of proteinase 3 is concomitant with endothelial cell apoptosis and internalization of myeloperoxidase with generation of intracellular oxidants," The American Journal of Pathology, Vol. 158, no. 2, pp. 581-592, 2001.
    • (2001) The American Journal of Pathology , vol.158 , Issue.2 , pp. 581-592
    • Yang, J.J.1    Preston, G.A.2    Pendergraft, W.F.3
  • 71
    • 84255167460 scopus 로고    scopus 로고
    • Neutrophil proteinase 3 induces diabetes in a mouse model of glucose tolerance
    • S. Bae, J. Choi, J. Hong et al., "Neutrophil proteinase 3 induces diabetes in a mouse model of glucose tolerance," Endocrine Research, Vol. 37, no. 1, pp. 35-45, 2012.
    • (2012) Endocrine Research , vol.37 , Issue.1 , pp. 35-45
    • Bae, S.1    Choi, J.2    Hong, J.3
  • 72
    • 84922267842 scopus 로고    scopus 로고
    • Markers of endothelial dysfunction and inflammation predict progression of diabetic nephropathy in african Americans with type 1 diabetes
    • M. S. Roy, M. N. Janal, J. Crosby, and R. Donnelly, "Markers of endothelial dysfunction and inflammation predict progression of diabetic nephropathy in African Americans with type 1 diabetes," Kidney International, Vol. 87, pp. 427-433, 2014.
    • (2014) Kidney International , vol.87 , pp. 427-433
    • Roy, M.S.1    Janal, M.N.2    Crosby, J.3    Donnelly, R.4
  • 73
    • 84899929877 scopus 로고    scopus 로고
    • The interplaybetween autophagy and apoptosis in the diabetic heart
    • C. Ouyang, J. You, and Z. Xie, "The interplaybetween autophagy and apoptosis in the diabetic heart," Journal of Molecular and Cellular Cardiology, Vol. 71, pp. 71-80, 2014.
    • (2014) Journal of Molecular and Cellular Cardiology , vol.71 , pp. 71-80
    • Ouyang, C.1    You, J.2    Xie, Z.3
  • 74
    • 84901659445 scopus 로고    scopus 로고
    • Ubiquitination-dependent CARM1 degradation facilitates notch1-mediated podocyte apoptosis in diabetic nephropathy
    • D. Kim, S. Lim, M. Park et al., "Ubiquitination-dependent CARM1 degradation facilitates Notch1-mediated podocyte apoptosis in diabetic nephropathy," Cellular Signalling, Vol. 26, no. 9, pp. 1774-1782, 2014.
    • (2014) Cellular Signalling , vol.26 , Issue.9 , pp. 1774-1782
    • Kim, D.1    Lim, S.2    Park, M.3
  • 75
    • 0022843745 scopus 로고
    • Cathepsin L inactivates α1-proteinase inhibitor by cleavage in the reactive site region
    • D. A. Johnson, A. J. Barrett, and R. W. Mason, "Cathepsin L inactivates α1-proteinase inhibitor by cleavage in the reactive site region," Journal of Biological Chemistry, Vol. 261, no. 31, pp. 14748-14751, 1986.
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.31 , pp. 14748-14751
    • Johnson, D.A.1    Barrett, A.J.2    Mason, R.W.3
  • 76
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • K. Kessenbrock, V. Plaks, and Z. Werb, "Matrix metalloproteinases: regulators of the tumor microenvironment," Cell, Vol. 141, no. 1, pp. 52-67, 2010.
    • (2010) Cell , vol.141 , Issue.1 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 77
    • 1242283880 scopus 로고    scopus 로고
    • Members of the cystatin superfamily interact with MMP-9 and protect it from autolytic degradation without affecting its gelatinolytic activities
    • S. Ray, P. Lukyanov, and J. Ochieng, "Members of the cystatin superfamily interact with MMP-9 and protect it from autolytic degradation without affecting its gelatinolytic activities," Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1652, no. 2, pp. 91-102, 2003.
    • (2003) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1652 , Issue.2 , pp. 91-102
    • Ray, S.1    Lukyanov, P.2    Ochieng, J.3
  • 78
    • 42649117475 scopus 로고    scopus 로고
    • Interplay of angiotensin II and angiotensin(1-7) in the regulation of matrix metalloproteinases of human cardiocytes
    • C. H. Pan, C. H. Wen, and C. S. Lin, "Interplay of angiotensin II and angiotensin(1-7) in the regulation of matrix metalloproteinases of human cardiocytes," Experimental Physiology, Vol. 93, no. 5, pp. 599-612, 2008.
    • (2008) Experimental Physiology , vol.93 , Issue.5 , pp. 599-612
    • Pan, C.H.1    Wen, C.H.2    Lin, C.S.3


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