메뉴 건너뛰기




Volumn 44, Issue 6, 2012, Pages 1040-1050

Distinct role of matrix metalloproteinase-3 in kidney injury molecule-1 shedding by kidney proximal tubular epithelial cells

Author keywords

Ectodomain shedding; Kidney injury molecule; Matrix metalloproteinase; Proximal tubular epithelial cells; Reactive oxygen species

Indexed keywords

ALBUMIN; KIDNEY INJURY MOLECULE 1; REACTIVE OXYGEN METABOLITE; SMALL INTERFERING RNA; STROMELYSIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 84860280763     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2012.03.015     Document Type: Article
Times cited : (35)

References (57)
  • 1
    • 84860202695 scopus 로고    scopus 로고
    • Macrophage infiltration and renal damage are independent of matrix metalloproteinase 12 (MMP-12) in the obstructed kidney
    • JANUARY [Epub ahead of print]
    • A.P. Abraham, F.Y. Ma, W.R. Mulley, E. Ozols, and D.J. Nikolic-Paterson Macrophage infiltration and renal damage are independent of matrix metalloproteinase 12 (MMP-12) in the obstructed kidney Nephrology January 2012 [Epub ahead of print]
    • (2012) Nephrology
    • Abraham, A.P.1    Ma, F.Y.2    Mulley, W.R.3    Ozols, E.4    Nikolic-Paterson, D.J.5
  • 3
    • 0036882397 scopus 로고    scopus 로고
    • Protein ectodomain shedding
    • J. Arribas, and A. Borroto Protein ectodomain shedding Chem Rev 102 2002 4627 4638
    • (2002) Chem Rev , vol.102 , pp. 4627-4638
    • Arribas, J.1    Borroto, A.2
  • 4
    • 0037131165 scopus 로고    scopus 로고
    • Shedding of kidney injury molecule-1, a putative adhesion protein involved in renal regeneration
    • DOI 10.1074/jbc.M200562200
    • V. Bailly, Z. Zhang, W. Meier, R. Cate, M. Sanicola, and J.V. Bonventre Shedding of kidney injury molecule-1, a putative adhesion protein involved in renal regeneration J Biol Chem 277 2002 39739 39748 (Pubitemid 35190957)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39739-39748
    • Bailly, V.1    Zhang, Z.2    Meier, W.3    Cate, R.4    Sanicola, M.5    Bonventre, J.V.6
  • 6
    • 33744995009 scopus 로고    scopus 로고
    • In situ gene expression and localization of metalloproteinases MMP1, MMP2, MMP3, MMP9, and their inhibitors TIMP1 and TIMP2 in human renal cell carcinoma
    • V. Bhuvarahamurthy, G.O. Kristiansen, M. Johannsen, S.A. Loening, D. Schnorr, and K. Jung In situ gene expression and localization of metalloproteinases MMP1, MMP2, MMP3, MMP9, and their inhibitors TIMP1 and TIMP2 in human renal cell carcinoma Oncol Rep 15 2006 1379 1384
    • (2006) Oncol Rep , vol.15 , pp. 1379-1384
    • Bhuvarahamurthy, V.1    Kristiansen, G.O.2    Johannsen, M.3    Loening, S.A.4    Schnorr, D.5    Jung, K.6
  • 9
    • 79958768097 scopus 로고    scopus 로고
    • Albumin overload activates intrarenal renin-angiotensin system through protein kinase C and NADPH oxidase-dependent pathway
    • W. Cao, Q.G. Zhou, J. Nie, G.B. Wang, Y. Liu, and Z.M. Zhou Albumin overload activates intrarenal renin-angiotensin system through protein kinase C and NADPH oxidase-dependent pathway J Hypertens 29 2011 1411 1421
    • (2011) J Hypertens , vol.29 , pp. 1411-1421
    • Cao, W.1    Zhou, Q.G.2    Nie, J.3    Wang, G.B.4    Liu, Y.5    Zhou, Z.M.6
  • 10
    • 25844525721 scopus 로고    scopus 로고
    • Ischemia injury alters endothelial cell properties of kidney cortex: Stimulation of MMP-9
    • DOI 10.1016/j.yexcr.2005.07.004, PII S0014482705003307
    • A. Caron, R.R. Desrosiers, and R. Beliveau Ischemia injury alters endothelial cell properties of kidney cortex: stimulation of MMP-9 Exp Cell Res 310 2005 105 116 (Pubitemid 41393692)
    • (2005) Experimental Cell Research , vol.310 , Issue.1 , pp. 105-116
    • Caron, A.1    Desrosiers, R.R.2    Beliveau, R.3
  • 14
    • 0033573049 scopus 로고    scopus 로고
    • Ectodomain shedding of TGF-α and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades
    • H. Fan, and R. Derynck Ectodomain shedding of TGF-alpha and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades EMBO J 18 1999 6962 6972 (Pubitemid 30000449)
    • (1999) EMBO Journal , vol.18 , Issue.24 , pp. 6962-6972
    • Fan, H.1    Derynck, R.2
  • 15
    • 0034695918 scopus 로고    scopus 로고
    • Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3-sensitive metalloproteinase
    • M.L. Fitzgerald, Z. Wang, P.W. Park, G. Murphy, and M. Bernfield Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3-sensitive metalloproteinase J Cell Biol 148 2000 811 824
    • (2000) J Cell Biol , vol.148 , pp. 811-824
    • Fitzgerald, M.L.1    Wang, Z.2    Park, P.W.3    Murphy, G.4    Bernfield, M.5
  • 16
    • 0042093741 scopus 로고    scopus 로고
    • Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin). An oxidative mechanism for restraining proteolytic activity during inflammation
    • DOI 10.1074/jbc.M304739200
    • X. Fu, S.Y. Kassim, W.C. Parks, and J.W. Heinecke Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation J Biol Chem 278 2003 28403 28409 (Pubitemid 36935741)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28403-28409
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 18
    • 0036314217 scopus 로고    scopus 로고
    • Kidney Injury Molecule-1 (KIM-1): A novel biomarker for human renal proximal tubule injury
    • DOI 10.1046/j.1523-1755.2002.00433.x
    • W.K. Han, V. Bailly, R. Abichandani, R. Thadhani, and J.V. Bonventre Kidney injury molecule-1 (KIM-1): a novel biomarker for human renal proximal tubule injury Kidney Int 62 2002 237 244 (Pubitemid 34754067)
    • (2002) Kidney International , vol.62 , Issue.1 , pp. 237-244
    • Han, W.K.1    Bailly, V.2    Abichandani, R.3    Thadhani, R.4    Bonventre, J.V.5
  • 22
    • 0032512724 scopus 로고    scopus 로고
    • Kidney injury molecule-1 (KIM-1), a putative epithelial cell adhesion molecule containing a novel immunoglobulin domain, is up-regulated in renal cells after injury
    • DOI 10.1074/jbc.273.7.4135
    • T. Ichimura, J.V. Bonventre, V. Bailly, H. Wei, C.A. Hession, and R.L. Cate Kidney injury molecule-1 (KIM-1), a putative epithelial cell adhesion molecule containing a novel immunoglobulin domain, is up-regulated in renal cells after injury J Biol Chem 273 1998 4135 4142 (Pubitemid 28103282)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.7 , pp. 4135-4142
    • Ichimura, T.1    Bonventre, J.V.2    Bailly, V.3    Wei, H.4    Hession, C.A.5    Cate, R.L.6    Sanicola, M.7
  • 24
    • 33847203614 scopus 로고    scopus 로고
    • Effect of combining ACE inhibition with aldosterone blockade on proteinuria and renal damage in experimental nephrosis
    • A.B. Kramer, E.F. van der Meulen, I. Hamming, H. van Goor, and G. Navis Effect of combining ACE inhibition with aldosterone blockade on proteinuria and renal damage in experimental nephrosis Kidney Int 71 2007 417 424
    • (2007) Kidney Int , vol.71 , pp. 417-424
    • Kramer, A.B.1    Van Der Meulen, E.F.2    Hamming, I.3    Van Goor, H.4    Navis, G.5
  • 25
    • 66049115451 scopus 로고    scopus 로고
    • Reduction of proteinuria in adriamycin-induced nephropathy is associated with reduction of renal kidney injury molecule (Kim-1) over time
    • A.B. Kramer, M.M. van Timmeren, T.A. Schuurs, V.S. Vaidya, J.V. Bonventre, and H. van Goor Reduction of proteinuria in adriamycin-induced nephropathy is associated with reduction of renal kidney injury molecule (Kim-1) over time Am J Physiol Renal Physiol 296 2009 F1136 F1145
    • (2009) Am J Physiol Renal Physiol , vol.296
    • Kramer, A.B.1    Van Timmeren, M.M.2    Schuurs, T.A.3    Vaidya, V.S.4    Bonventre, J.V.5    Van Goor, H.6
  • 28
    • 0021984681 scopus 로고
    • Oxygen-derived free radicals in postischemic tissue injury
    • J.M. McCord Oxygen-derived free radicals in postischemic tissue injury N Engl J Med 312 1985 159 163 (Pubitemid 15192863)
    • (1985) New England Journal of Medicine , vol.312 , Issue.3 , pp. 159-163
    • McCord, J.M.1
  • 29
    • 21644431566 scopus 로고    scopus 로고
    • Overproduction of reactive oxygen species in end-stage renal disease patients: A potential component of hemodialysis-associated inflammation
    • DOI 10.1111/j.1492-7535.2005.01116.x
    • M. Morena, S. Delbosc, A.M. Dupuy, B. Canaud, and J.P. Cristol Overproduction of reactive oxygen species in end-stage renal disease patients: a potential component of hemodialysis-associated inflammation Hemodial Int 9 2005 37 46 (Pubitemid 40932774)
    • (2005) Hemodialysis International , vol.9 , Issue.1 , pp. 37-46
    • Morena, M.1    Delbosc, S.2    Dupuy, A.-M.3    Canaud, B.4    Cristol, J.-P.5
  • 30
    • 0025095795 scopus 로고
    • Induction of renal growth and injury in the intact rat kidney by dietary deficiency of antioxidants
    • K.A. Nath, and A.K. Salahudeen Induction of renal growth and injury in the intact rat kidney by dietary deficiency of antioxidants J Clin Invest 86 1990 1179 1192 (Pubitemid 20370424)
    • (1990) Journal of Clinical Investigation , vol.86 , Issue.4 , pp. 1179-1192
    • Nath, K.A.1    Salahudeen, A.K.2
  • 31
    • 4644310412 scopus 로고    scopus 로고
    • TNF-α and IL-1β-mediated regulation of MMP-9 and TIMP-1 in renal proximal tubular cells
    • DOI 10.1111/j.1523-1755.2004.00900.x
    • L.E. Nee, T. McMorrow, E. Campbell, C. Slattery, and M.P. Ryan TNF-alpha and IL-1beta-mediated regulation of MMP-9 and TIMP-1 in renal proximal tubular cells Kidney Int 66 2004 1376 1386 (Pubitemid 39298369)
    • (2004) Kidney International , vol.66 , Issue.4 , pp. 1376-1386
    • Nee, L.E.1    McMorrow, T.2    Campbell, E.3    Slattery, C.4    Ryan, M.P.5
  • 33
    • 0031570730 scopus 로고    scopus 로고
    • Activation of human neutrophil procollagenase by nitrogen dioxide and peroxynitrite: A novel mechanism for procollagenase activation involving nitric oxide
    • DOI 10.1006/abbi.1997.0127
    • T. Okamoto, T. Akaike, T. Nagano, S. Miyajima, M. Suga, and M. Ando Activation of human neutrophil procollagenase by nitrogen dioxide and peroxynitrite: a novel mechanism for procollagenase activation involving nitric oxide Arch Biochem Biophys 342 1997 261 274 (Pubitemid 27251247)
    • (1997) Archives of Biochemistry and Biophysics , vol.342 , Issue.2 , pp. 261-274
    • Okamoto, T.1    Akaike, T.2    Nagano, T.3    Miyajima, S.4    Suga, M.5    Ando, M.6    Ichimori, K.7    Maeda, H.8
  • 34
  • 37
    • 36549085160 scopus 로고    scopus 로고
    • Control of matrix metalloproteinase catalytic activity
    • DOI 10.1016/j.matbio.2007.07.001, PII S0945053X0700090X
    • H.J. Ra, and W.C. Parks Control of matrix metalloproteinase catalytic activity Matrix Biol 26 2007 587 596 (Pubitemid 350180394)
    • (2007) Matrix Biology , vol.26 , Issue.8 , pp. 587-596
    • Ra, H.-J.1    Parks, W.C.2
  • 38
    • 0021203006 scopus 로고
    • Evidence for the role of oxygen radicals in acute nephrotoxic nephritis
    • A. Rehan, K.J. Johnson, R.C. Wiggins, R.G. Kunkel, and P.A. Ward Evidence for the role of oxygen radicals in acute nephrotoxic nephritis Lab Invest 51 1984 396 403 (Pubitemid 14021012)
    • (1984) Laboratory Investigation , vol.51 , Issue.4 , pp. 396-403
    • Rehan, A.1    Johnson, K.J.2    Wiggins, R.C.3
  • 39
    • 0033646195 scopus 로고    scopus 로고
    • Circulating levels of matrix metalloproteinases MMP-3 and MMP-2 in renal transplant recipients with chronic transplant nephropathy
    • E. Rodrigo, M. Lopez-Hoyos, R. Escallada, G. Fernandez-Fresnedo, J.C. Ruiz, and C. Pinera Circulating levels of matrix metalloproteinases MMP-3 and MMP-2 in renal transplant recipients with chronic transplant nephropathy Nephrol Dial Transplant 15 2000 2041 2045
    • (2000) Nephrol Dial Transplant , vol.15 , pp. 2041-2045
    • Rodrigo, E.1    Lopez-Hoyos, M.2    Escallada, R.3    Fernandez-Fresnedo, G.4    Ruiz, J.C.5    Pinera, C.6
  • 40
    • 0030064690 scopus 로고    scopus 로고
    • Tubular gelatinase A (MMP-2) and its tissue inhibitors in polycystic kidney disease in the Han:SPRD rat
    • L. Schaefer, X. Han, N. Gretz, C. Hafner, K. Meier, and F. Matzkies Tubular gelatinase A (MMP-2) and its tissue inhibitors in polycystic kidney disease in the Han:SPRD rat Kidney Int 49 1996 75 81 (Pubitemid 26024229)
    • (1996) Kidney International , vol.49 , Issue.1 , pp. 75-81
    • Schaefer, L.1    Han, X.2    Gretz, N.3    Hafner, C.4    Meier, K.5    Matzkies, F.6    Schaefer, R.M.7
  • 42
    • 0030818120 scopus 로고    scopus 로고
    • In situ hybridization studies of matrix metalloproteinase-3, tissue inhibitor of metalloproteinase-1 and type IV collagen in diabetic nephropathy
    • D. Suzuki, M. Miyazaki, K. Jinde, T. Koji, M. Yagame, and M. Endoh In situ hybridization studies of matrix metalloproteinase-3, tissue inhibitor of metalloproteinase-1 and type IV collagen in diabetic nephropathy Kidney Int 52 1997 111 119 (Pubitemid 27321821)
    • (1997) Kidney International , vol.52 , Issue.1 , pp. 111-119
    • Suzuki, D.1    Miyazaki, M.2    Jinde, K.3    Koji, T.4    Yagame, M.5    Endoh, M.6    Nomoto, Y.7    Sakai, H.8
  • 43
  • 44
    • 0038486911 scopus 로고    scopus 로고
    • Antioxidant ameliorates cisplatin-induced renal tubular cell death through inhibition of death receptor-mediated pathways
    • K. Tsuruya, M. Tokumoto, T. Ninomiya, M. Hirakawa, K. Masutani, and M. Taniguchi Antioxidant ameliorates cisplatin-induced renal tubular cell death through inhibition of death receptor-mediated pathways Am J Physiol Renal Physiol 285 2003 F208 F218
    • (2003) Am J Physiol Renal Physiol , vol.285
    • Tsuruya, K.1    Tokumoto, M.2    Ninomiya, T.3    Hirakawa, M.4    Masutani, K.5    Taniguchi, M.6
  • 45
    • 77952160766 scopus 로고    scopus 로고
    • Kidney injury molecule-1 outperforms traditional biomarkers of kidney injury in preclinical biomarker qualification studies
    • V.S. Vaidya, J.S. Ozer, F. Dieterle, F.B. Collings, V. Ramirez, and S. Troth Kidney injury molecule-1 outperforms traditional biomarkers of kidney injury in preclinical biomarker qualification studies Nat Biotechnol 28 2010 478 485
    • (2010) Nat Biotechnol , vol.28 , pp. 478-485
    • Vaidya, V.S.1    Ozer, J.S.2    Dieterle, F.3    Collings, F.B.4    Ramirez, V.5    Troth, S.6
  • 46
    • 33644870877 scopus 로고    scopus 로고
    • Urinary kidney injury molecule-1: A sensitive quantitative biomarker for early detection of kidney tubular injury
    • V.S. Vaidya, V. Ramirez, T. Ichimura, N.A. Bobadilla, and J.V. Bonventre Urinary kidney injury molecule-1: a sensitive quantitative biomarker for early detection of kidney tubular injury Am J Physiol Renal Physiol 290 2006 F517 F529
    • (2006) Am J Physiol Renal Physiol , vol.290
    • Vaidya, V.S.1    Ramirez, V.2    Ichimura, T.3    Bobadilla, N.A.4    Bonventre, J.V.5
  • 50
    • 57649144008 scopus 로고    scopus 로고
    • Effect of renin-angiotensin-aldosterone system inhibition, dietary sodium restriction, and/or diuretics on urinary kidney injury molecule 1 excretion in nondiabetic proteinuric kidney disease: A post hoc analysis of a randomized controlled trial
    • F. Waanders, V.S. Vaidya, H. van Goor, H. Leuvenink, K. Damman, and I. Hamming Effect of renin-angiotensin-aldosterone system inhibition, dietary sodium restriction, and/or diuretics on urinary kidney injury molecule 1 excretion in nondiabetic proteinuric kidney disease: a post hoc analysis of a randomized controlled trial Am J Kidney Dis 53 2009 16 25
    • (2009) Am J Kidney Dis , vol.53 , pp. 16-25
    • Waanders, F.1    Vaidya, V.S.2    Van Goor, H.3    Leuvenink, H.4    Damman, K.5    Hamming, I.6
  • 52
    • 0021961153 scopus 로고
    • Oxidative autoactivation of latent collagenase by human neutrophils
    • S.J. Weiss, G. Peppin, X. Ortiz, C. Ragsdale, and S.T. Test Oxidative autoactivation of latent collagenase by human neutrophils Science 227 1985 747 749 (Pubitemid 15168259)
    • (1985) Science , vol.227 , Issue.4688 , pp. 747-749
    • Weiss, S.J.1    Peppin, G.2    Ortiz, X.3
  • 53
    • 0141918880 scopus 로고    scopus 로고
    • Protein kinase Cε is linked to 12-O-tetradecanoylphorbol-13-acetate- induced tumor necrosis factor-α ectodomain shedding and the development of metastatic squamous cell carcinoma in protein kinase Cε transgenic mice
    • D.L. Wheeler, K.J. Ness, T.D. Oberley, and A.K. Verma Protein kinase Cepsilon is linked to 12-O-tetradecanoylphorbol-13-acetate-induced tumor necrosis factor-alpha ectodomain shedding and the development of metastatic squamous cell carcinoma in protein kinase Cepsilon transgenic mice Cancer Res 63 2003 6547 6555 (Pubitemid 37255210)
    • (2003) Cancer Research , vol.63 , Issue.19 , pp. 6547-6555
    • Wheeler, D.L.1    Ness, K.J.2    Oberley, T.D.3    Verma, A.K.4
  • 54
    • 48549095293 scopus 로고    scopus 로고
    • Immunolocalization of Kim-1, RPA-1, and RPA-2 in kidney of gentamicin-, mercury-, or chromium-treated rats: Relationship to renal distributions of iNOS and nitrotyrosine
    • J. Zhang, R.P. Brown, M. Shaw, V.S. Vaidya, Y. Zhou, and P. Espandiari Immunolocalization of Kim-1, RPA-1, and RPA-2 in kidney of gentamicin-, mercury-, or chromium-treated rats: relationship to renal distributions of iNOS and nitrotyrosine Toxicol Pathol 36 2008 397 409
    • (2008) Toxicol Pathol , vol.36 , pp. 397-409
    • Zhang, J.1    Brown, R.P.2    Shaw, M.3    Vaidya, V.S.4    Zhou, Y.5    Espandiari, P.6
  • 55
    • 70350453660 scopus 로고    scopus 로고
    • Differences in immunolocalization of Kim-1, RPA-1, and RPA-2 in kidneys of gentamicin-, cisplatin-, and valproic acid-treated rats: Potential role of iNOS and nitrotyrosine
    • J. Zhang, P.L. Goering, P. Espandiari, M. Shaw, J.V. Bonventre, and V.S. Vaidya Differences in immunolocalization of Kim-1, RPA-1, and RPA-2 in kidneys of gentamicin-, cisplatin-, and valproic acid-treated rats: potential role of iNOS and nitrotyrosine Toxicol Pathol 37 2009 629 643
    • (2009) Toxicol Pathol , vol.37 , pp. 629-643
    • Zhang, J.1    Goering, P.L.2    Espandiari, P.3    Shaw, M.4    Bonventre, J.V.5    Vaidya, V.S.6
  • 56
    • 34948814501 scopus 로고    scopus 로고
    • Shedding of the urinary biomarker kidney injury molecule-1 (KIM-1) is regulated by MAP kinases and juxtamembrane region
    • DOI 10.1681/ASN.2007030325
    • Z. Zhang, B.D. Humphreys, and J.V. Bonventre Shedding of the urinary biomarker kidney injury molecule-1 (KIM-1) is regulated by MAP kinases and juxtamembrane region J Am Soc Nephrol 18 2007 2704 2714 (Pubitemid 47531197)
    • (2007) Journal of the American Society of Nephrology , vol.18 , Issue.10 , pp. 2704-2714
    • Zhang, Z.1    Humphreys, B.D.2    Bonventre, J.V.3
  • 57
    • 36949014801 scopus 로고    scopus 로고
    • Comparison of kidney injury molecule-1 and other nephrotoxicity biomarkers in urine and kidney following acute exposure to gentamicin, mercury, and chromium
    • DOI 10.1093/toxsci/kfm260
    • Y. Zhou, V.S. Vaidya, R.P. Brown, J. Zhang, B.A. Rosenzweig, and K.L. Thompson Comparison of kidney injury molecule-1 and other nephrotoxicity biomarkers in urine and kidney following acute exposure to gentamicin, mercury, and chromium Toxicol Sci 101 2008 159 170 (Pubitemid 350239020)
    • (2008) Toxicological Sciences , vol.101 , Issue.1 , pp. 159-170
    • Zhou, Y.1    Vaidya, V.S.2    Brown, R.P.3    Zhang, J.4    Rosenzweig, B.A.5    Thompson, K.L.6    Miller, T.J.7    Bonventre, J.V.8    Goering, P.I.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.