메뉴 건너뛰기




Volumn 302, Issue 11, 2012, Pages

Matrix metalloproteinases in kidney homeostasis and diseases

Author keywords

Apoptosis; Epithelial mesenchymal transition; Fibrosis; Inflammation; MMP

Indexed keywords

CARTILAGE OLIGOMERIC MATRIX PROTEIN; CASEIN; COLLAGEN TYPE 4; COLLAGENASE 3; FIBRIN; FIBRONECTIN; GELATIN; GELATINASE A; GELATINASE B; INTERSTITIAL COLLAGENASE; MACROPHAGE ELASTASE; MATRILYSIN; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE 15; MATRIX METALLOPROTEINASE 16; MATRIX METALLOPROTEINASE 17; MATRIX METALLOPROTEINASE 18; MATRIX METALLOPROTEINASE 19; MATRIX METALLOPROTEINASE 20; MATRIX METALLOPROTEINASE 21; MATRIX METALLOPROTEINASE 23; MATRIX METALLOPROTEINASE 24; MATRIX METALLOPROTEINASE 25; MATRIX METALLOPROTEINASE 26; MATRIX METALLOPROTEINASE 27; MATRIX METALLOPROTEINASE 28; STROMELYSIN 2; STROMELYSIN 3; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84861850705     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.00037.2012     Document Type: Review
Times cited : (204)

References (154)
  • 2
    • 77955928306 scopus 로고    scopus 로고
    • Evaluation of role of doxycycline (a matrix metalloproteinase inhibitor) on renal functions in patients of diabetic nephropathy
    • Aggarwal HK, Jain D, Talapatra P, Yadav RK, Gupta T, Kathuria KL. Evaluation of role of doxycycline (a matrix metalloproteinase inhibitor) on renal functions in patients of diabetic nephropathy. Ren Fail 32: 941-946, 2010.
    • (2010) Ren Fail , vol.32 , pp. 941-946
    • Aggarwal, H.K.1    Jain, D.2    Talapatra, P.3    Yadav, R.K.4    Gupta, T.5    Kathuria, K.L.6
  • 3
    • 2142860186 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 expression in renal biopsies of patients with HIV-associated nephropathy
    • Ahuja TS, Gopalani A, Davies P, Ahuja H. Matrix metalloproteinase-9 expression in renal biopsies of patients with HIV-associated nephropathy. Nephron Clin Pract 95: c100-c104, 2003.
    • (2003) Nephron Clin Pract , vol.95
    • Ahuja, T.S.1    Gopalani, A.2    Davies, P.3    Ahuja, H.4
  • 4
    • 0344152902 scopus 로고    scopus 로고
    • Local delivery of matrix metalloproteinase gene prevents the onset of renal sclerosis in streptozotocin-induced diabetic mice
    • Aoyama T, Yamamoto S, Kanematsu A, Ogawa O, Tabata Y. Local delivery of matrix metalloproteinase gene prevents the onset of renal sclerosis in streptozotocin-induced diabetic mice. Tissue Eng 9: 1289-1299, 2003.
    • (2003) Tissue Eng , vol.9 , pp. 1289-1299
    • Aoyama, T.1    Yamamoto, S.2    Kanematsu, A.3    Ogawa, O.4    Tabata, Y.5
  • 6
    • 0035199934 scopus 로고    scopus 로고
    • Renal ischemic injury results in permanent damage to peritubular capillaries and influences long-term function
    • Basile DP, Donohoe D, Roethe K, Osborn JL. Renal ischemic injury results in permanent damage to peritubular capillaries and influences long-term function. Am J Physiol Renal Physiol 281: F887-F899, 2001.
    • (2001) Am J Physiol Renal Physiol , vol.281
    • Basile, D.P.1    Donohoe, D.2    Roethe, K.3    Osborn, J.L.4
  • 7
    • 0037303729 scopus 로고    scopus 로고
    • Chronic renal hypoxia after acute ischemic injury: Effects of L-arginine on hypoxia and secondary damage
    • Basile DP, Donohoe DL, Roethe K, Mattson DL. Chronic renal hypoxia after acute ischemic injury: effects of L-arginine on hypoxia and secondary damage. Am J Physiol Renal Physiol 284: F338-F348, 2003.
    • (2003) Am J Physiol Renal Physiol , vol.284
    • Basile, D.P.1    Donohoe, D.L.2    Roethe, K.3    Mattson, D.L.4
  • 9
    • 34047174848 scopus 로고    scopus 로고
    • Specific changes in plasma concentrations of matrix metalloproteinase-2 and-9, TIMP-1 and TGF-beta1 in patients with distinct types of primary glomerulonephritis
    • Bauvois B, Mothu N, Nguyen J, Nguyen-Khoa T, Noel LH, Jungers P. Specific changes in plasma concentrations of matrix metalloproteinase-2 and-9, TIMP-1 and TGF-beta1 in patients with distinct types of primary glomerulonephritis. Nephrol Dial Transplant 22: 1115-1122, 2007.
    • (2007) Nephrol Dial Transplant , vol.22 , pp. 1115-1122
    • Bauvois, B.1    Mothu, N.2    Nguyen, J.3    Nguyen-Khoa, T.4    Noel, L.H.5    Jungers, P.6
  • 16
    • 40849133852 scopus 로고    scopus 로고
    • Circulating matrix metalloproteinase-2 is associated with cystatin C level, posttransplant duration, and diabetes mellitus in kidney transplant recipients
    • Chang HR, Kuo WH, Hsieh YS, Yang SF, Lin CC, Lee ML, Lian JD, Chu SC. Circulating matrix metalloproteinase-2 is associated with cystatin C level, posttransplant duration, and diabetes mellitus in kidney transplant recipients. Transl Res 151: 217-223, 2008.
    • (2008) Transl Res , vol.151 , pp. 217-223
    • Chang, H.R.1    Kuo, W.H.2    Hsieh, Y.S.3    Yang, S.F.4    Lin, C.C.5    Lee, M.L.6    Lian, J.D.7    Chu, S.C.8
  • 17
    • 0038582623 scopus 로고    scopus 로고
    • Gelatinase A (MMP-2) is necessary and sufficient for renal tubular cell epithelial-mesenchymal transformation
    • Cheng S, Lovett DH. Gelatinase A (MMP-2) is necessary and sufficient for renal tubular cell epithelial-mesenchymal transformation. Am J Pathol 162: 1937-1949, 2003.
    • (2003) Am J Pathol , vol.162 , pp. 1937-1949
    • Cheng, S.1    Lovett, D.H.2
  • 18
    • 33845576431 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 and basement membrane integrity: A unifying mechanism for progressive renal injury
    • Cheng S, Pollock AS, Mahimkar R, Olson JL, Lovett DH. Matrix metalloproteinase 2 and basement membrane integrity: a unifying mechanism for progressive renal injury. FASEB J 20: 1898-1900, 2006.
    • (2006) FASEB J , vol.20 , pp. 1898-1900
    • Cheng, S.1    Pollock, A.S.2    Mahimkar, R.3    Olson, J.L.4    Lovett, D.H.5
  • 19
    • 70349317144 scopus 로고    scopus 로고
    • Upregulation of matrix metalloproteinase-2 in the arterial vasculature contributes to stiffening and vasomotor dysfunction in patients with chronic kidney disease
    • Chung AW, Yang HH, Kim JM, Sigrist MK, Chum E, Gourlay WA, Levin A. Upregulation of matrix metalloproteinase-2 in the arterial vasculature contributes to stiffening and vasomotor dysfunction in patients with chronic kidney disease. Circulation 120: 792-801, 2009.
    • (2009) Circulation , vol.120 , pp. 792-801
    • Chung, A.W.1    Yang, H.H.2    Kim, J.M.3    Sigrist, M.K.4    Chum, E.5    Gourlay, W.A.6    Levin, A.7
  • 20
    • 70749162074 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and-9 exacerbate arterial stiffening and angiogenesis in diabetes and chronic kidney disease
    • Chung AW, Yang HH, Sigrist MK, Brin G, Chum E, Gourlay WA, Levin A. Matrix metalloproteinase-2 and-9 exacerbate arterial stiffening and angiogenesis in diabetes and chronic kidney disease. Cardiovasc Res 84: 494-504, 2009.
    • (2009) Cardiovasc Res , vol.84 , pp. 494-504
    • Chung, A.W.1    Yang, H.H.2    Sigrist, M.K.3    Brin, G.4    Chum, E.5    Gourlay, W.A.6    Levin, A.7
  • 21
    • 70449727044 scopus 로고    scopus 로고
    • Glomerular protein levels of matrix metalloproteinase-1 and tissue inhibitor of metalloproteinase-1 are lower in diabetic subjects
    • Cornish TC, Bagnasco SM, Macgregor AM, Lu J, Selvin E, Halushka MK. Glomerular protein levels of matrix metalloproteinase-1 and tissue inhibitor of metalloproteinase-1 are lower in diabetic subjects. J Histochem Cytochem 57: 995-1001, 2009.
    • (2009) J Histochem Cytochem , vol.57 , pp. 995-1001
    • Cornish, T.C.1    Bagnasco, S.M.2    McGregor, A.M.3    Lu, J.4    Selvin, E.5    Halushka, M.K.6
  • 22
    • 40449098083 scopus 로고    scopus 로고
    • Integrin alpha1beta1 regulates matrix metalloproteinases via P38 mitogen-activated protein kinase in mesangial cells: Implications for Alport syndrome
    • Cosgrove D, Meehan DT, Delimont D, Pozzi A, Chen X, Rodgers KD, Tempero RM, Zallocchi M, Rao VH. Integrin alpha1beta1 regulates matrix metalloproteinases via P38 mitogen-activated protein kinase in mesangial cells: implications for Alport syndrome. Am J Pathol 172: 761-773, 2008.
    • (2008) Am J Pathol , vol.172 , pp. 761-773
    • Cosgrove, D.1    Meehan, D.T.2    Delimont, D.3    Pozzi, A.4    Chen, X.5    Rodgers, K.D.6    Tempero, R.M.7    Zallocchi, M.8    Rao, V.H.9
  • 23
    • 78649881267 scopus 로고    scopus 로고
    • Matrix metalloproteinase 8 deficiency in mice exacerbates inflammatory arthritis through delayed neutrophil apoptosis and reduced caspase 11 expression
    • Cox JH, Starr AE, Kappelhoff R, Yan R, Roberts CR, Overall CM. Matrix metalloproteinase 8 deficiency in mice exacerbates inflammatory arthritis through delayed neutrophil apoptosis and reduced caspase 11 expression. Arthritis Rheum 62: 3645-3655, 2010.
    • (2010) Arthritis Rheum , vol.62 , pp. 3645-3655
    • Cox, J.H.1    Starr, A.E.2    Kappelhoff, R.3    Yan, R.4    Roberts, C.R.5    Overall, C.M.6
  • 24
    • 83055181483 scopus 로고    scopus 로고
    • Distinct metalloproteinase excretion patterns in focal segmental glomerulosclerosis
    • Czech KA, Bennett M, Devarajan P. Distinct metalloproteinase excretion patterns in focal segmental glomerulosclerosis. Pediatr Nephrol 26: 2179-2184, 2011.
    • (2011) Pediatr Nephrol , vol.26 , pp. 2179-2184
    • Czech, K.A.1    Bennett, M.2    Devarajan, P.3
  • 28
    • 45449115351 scopus 로고    scopus 로고
    • Pervanadate-induced shedding of the intercellular adhesion molecule (ICAM)-1 ectodomain is mediated by membrane type-1 matrix metalloproteinase (MT1-MMP)
    • Essick E, Sithu S, Dean W, D'Souza S. Pervanadate-induced shedding of the intercellular adhesion molecule (ICAM)-1 ectodomain is mediated by membrane type-1 matrix metalloproteinase (MT1-MMP). Mol Cell Biochem 314: 151-159, 2008.
    • (2008) Mol Cell Biochem , vol.314 , pp. 151-159
    • Essick, E.1    Sithu, S.2    Dean, W.3    D'Souza, S.4
  • 29
    • 77149137406 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Evolution, gene regulation and functional analysis in mouse models
    • Fanjul-Fernandez M, Folgueras AR, Cabrera S, Lopez-Otin C. Matrix metalloproteinases: evolution, gene regulation and functional analysis in mouse models. Biochim Biophys Acta 1803: 3-19, 2010.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 3-19
    • Fanjul-Fernandez, M.1    Folgueras, A.R.2    Cabrera, S.3    Lopez-Otin, C.4
  • 31
    • 1342346608 scopus 로고    scopus 로고
    • Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: Specific structural motifs control protein oxidation
    • Fu X, Kao JL, Bergt C, Kassim SY, Huq NP, d'Avignon A, Parks WC, Mecham RP, Heinecke JW. Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: specific structural motifs control protein oxidation. J Biol Chem 279: 6209-6212, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 6209-6212
    • Fu, X.1    Kao, J.L.2    Bergt, C.3    Kassim, S.Y.4    Huq, N.P.5    d'Avignon, A.6    Parks, W.C.7    Mecham, R.P.8    Heinecke, J.W.9
  • 32
    • 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
    • Fu X, Kassim SY, Parks WC, Heinecke JW. 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: 28403-28409, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 28403-28409
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 35
    • 77951719523 scopus 로고    scopus 로고
    • Dendritic cell podosomes are protrusive and invade the extracellular matrix using metalloproteinase MMP-14
    • Gawden-Bone C, Zhou Z, King E, Prescott A, Watts C, Lucocq J. Dendritic cell podosomes are protrusive and invade the extracellular matrix using metalloproteinase MMP-14. J Cell Sci 123: 1427-1437, 2010.
    • (2010) J Cell Sci , vol.123 , pp. 1427-1437
    • Gawden-Bone, C.1    Zhou, Z.2    King, E.3    Prescott, A.4    Watts, C.5    Lucocq, J.6
  • 37
    • 78650424066 scopus 로고    scopus 로고
    • Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting
    • Gialeli C, Theocharis AD, Karamanos NK. Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting. FEBS J 278: 16-27, 2011.
    • (2011) FEBS J , vol.278 , pp. 16-27
    • Gialeli, C.1    Theocharis, A.D.2    Karamanos, N.K.3
  • 38
    • 2542483387 scopus 로고    scopus 로고
    • How tadpoles lose their tails: Path to discovery of the first matrix metalloproteinase
    • Gross J. How tadpoles lose their tails: path to discovery of the first matrix metalloproteinase. Matrix Biol 23: 3-13, 2004.
    • (2004) Matrix Biol , vol.23 , pp. 3-13
    • Gross, J.1
  • 39
    • 20544438078 scopus 로고    scopus 로고
    • Tumstatin, the NC1 domain of alpha3 chain of type IV collagen, is an endogenous inhibitor of pathological angiogenesis and suppresses tumor growth
    • Hamano Y, Kalluri R. Tumstatin, the NC1 domain of alpha3 chain of type IV collagen, is an endogenous inhibitor of pathological angiogenesis and suppresses tumor growth. Biochem Biophys Res Commun 333: 292-298, 2005.
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 292-298
    • Hamano, Y.1    Kalluri, R.2
  • 41
    • 80052335469 scopus 로고    scopus 로고
    • Targeted inhibition of β-catenin/CBP signaling ameliorates renal interstitial fibrosis
    • Hao S, He W, Li Y, Ding H, Hou Y, Nie J, Hou FF, Kahn M, Liu Y. Targeted inhibition of β-catenin/CBP signaling ameliorates renal interstitial fibrosis. J Am Soc Nephrol 22: 1642-1653, 2011.
    • (2011) J Am Soc Nephrol , vol.22 , pp. 1642-1653
    • Hao, S.1    He, W.2    Li, Y.3    Ding, H.4    Hou, Y.5    Nie, J.6    Hou, F.F.7    Kahn, M.8    Liu, Y.9
  • 42
    • 77956547718 scopus 로고    scopus 로고
    • tPA is a potent mitogen for renal interstitial fibroblasts: Role of beta1 integrin/focal adhesion kinase signaling
    • Hao S, Shen H, Hou Y, Mars WM, Liu Y. tPA is a potent mitogen for renal interstitial fibroblasts: role of beta1 integrin/focal adhesion kinase signaling. Am J Pathol 177: 1164-1175, 2010.
    • (2010) Am J Pathol , vol.177 , pp. 1164-1175
    • Hao, S.1    Shen, H.2    Hou, Y.3    Mars, W.M.4    Liu, Y.5
  • 43
    • 0033966350 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7-dependent release of tumor necrosis factor-alpha in a model of herniated disc resorption
    • Haro H, Crawford HC, Fingleton B, Shinomiya K, Spengler DM, Matrisian LM. Matrix metalloproteinase-7-dependent release of tumor necrosis factor-alpha in a model of herniated disc resorption. J Clin Invest 105: 143-150, 2000.
    • (2000) J Clin Invest , vol.105 , pp. 143-150
    • Haro, H.1    Crawford, H.C.2    Fingleton, B.3    Shinomiya, K.4    Spengler, D.M.5    Matrisian, L.M.6
  • 44
    • 65249134946 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling promotes renal interstitial fibrosis
    • He W, Dai C, Li Y, Zeng G, Monga SP, Liu Y. Wnt/β-catenin signaling promotes renal interstitial fibrosis. J Am Soc Nephrol 20: 765-776, 2009.
    • (2009) J Am Soc Nephrol , vol.20 , pp. 765-776
    • He, W.1    Dai, C.2    Li, Y.3    Zeng, G.4    Monga, S.P.5    Liu, Y.6
  • 45
    • 84863115179 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7 as a surrogate marker predicts renal Wnt/β-catenin activity in CKD
    • He W, Tan RJ, Li Y, Wang D, Nie J, Hou FF, Liu Y. Matrix metalloproteinase-7 as a surrogate marker predicts renal Wnt/β-catenin activity in CKD. J Am Soc Nephrol 23: 294-304, 2012.
    • (2012) J Am Soc Nephrol , vol.23 , pp. 294-304
    • He, W.1    Tan, R.J.2    Li, Y.3    Wang, D.4    Nie, J.5    Hou, F.F.6    Liu, Y.7
  • 47
    • 40449129202 scopus 로고    scopus 로고
    • tPA protects renal interstitial fibroblasts and myofibroblasts from apoptosis
    • Hu K, Lin L, Tan X, Yang J, Bu G, Mars WM, Liu Y. tPA protects renal interstitial fibroblasts and myofibroblasts from apoptosis. J Am Soc Nephrol 19: 503-514, 2008.
    • (2008) J Am Soc Nephrol , vol.19 , pp. 503-514
    • Hu, K.1    Lin, L.2    Tan, X.3    Yang, J.4    Bu, G.5    Mars, W.M.6    Liu, Y.7
  • 48
    • 36849007621 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator promotes murine myofibroblast activation through LDL receptor-related protein 1-mediated integrin signaling
    • Hu K, Wu C, Mars WM, Liu Y. Tissue-type plasminogen activator promotes murine myofibroblast activation through LDL receptor-related protein 1-mediated integrin signaling. J Clin Invest 117: 3821-3832, 2007.
    • (2007) J Clin Invest , vol.117 , pp. 3821-3832
    • Hu, K.1    Wu, C.2    Mars, W.M.3    Liu, Y.4
  • 49
    • 33644869414 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator acts as a cytokine that triggers intracellular signal transduction and induces matrix metalloproteinase-9 gene expression
    • Hu K, Yang J, Tanaka S, Gonias SL, Mars WM, Liu Y. Tissue-type plasminogen activator acts as a cytokine that triggers intracellular signal transduction and induces matrix metalloproteinase-9 gene expression. J Biol Chem 281: 2120-2127, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 2120-2127
    • Hu, K.1    Yang, J.2    Tanaka, S.3    Gonias, S.L.4    Mars, W.M.5    Liu, Y.6
  • 50
    • 33646532452 scopus 로고    scopus 로고
    • Costimulation of chemokine receptor signaling by matrix metalloproteinase-9 mediates enhanced migration of IFN-alpha dendritic cells
    • Hu Y, Ivashkiv LB. Costimulation of chemokine receptor signaling by matrix metalloproteinase-9 mediates enhanced migration of IFN-alpha dendritic cells. J Immunol 176: 6022-6033, 2006.
    • (2006) J Immunol , vol.176 , pp. 6022-6033
    • Hu, Y.1    Ivashkiv, L.B.2
  • 51
    • 79953046160 scopus 로고    scopus 로고
    • Effects of doxycycline on renal ischemia reperfusion injury induced by abdominal compartment syndrome
    • Ihtiyar E, Yasar NF, Erkasap N, Koken T, Tosun M, Oner S, Erkasap S. Effects of doxycycline on renal ischemia reperfusion injury induced by abdominal compartment syndrome. J Surg Res 167: 113-120, 2011.
    • (2011) J Surg Res , vol.167 , pp. 113-120
    • Ihtiyar, E.1    Yasar, N.F.2    Erkasap, N.3    Koken, T.4    Tosun, M.5    Oner, S.6    Erkasap, S.7
  • 52
    • 79952714520 scopus 로고    scopus 로고
    • Decrease in claudin-2 expression enhances cell migration in renal epithelial Madin-Darby canine kidney cells
    • Ikari A, Takiguchi A, Atomi K, Sato T, Sugatani J. Decrease in claudin-2 expression enhances cell migration in renal epithelial Madin-Darby canine kidney cells. J Cell Physiol 226: 1471-1478, 2011.
    • (2011) J Cell Physiol , vol.226 , pp. 1471-1478
    • Ikari, A.1    Takiguchi, A.2    Atomi, K.3    Sato, T.4    Sugatani, J.5
  • 53
    • 54049130859 scopus 로고    scopus 로고
    • Epilysin (MMP-28)-structure, expression and potential functions
    • Illman SA, Lohi J, Keski-Oja J. Epilysin (MMP-28)-structure, expression and potential functions. Exp Dermatol 17: 897-907, 2008.
    • (2008) Exp Dermatol , vol.17 , pp. 897-907
    • Illman, S.A.1    Lohi, J.2    Keski-Oja, J.3
  • 54
    • 33747610734 scopus 로고    scopus 로고
    • Crystal structure of an active form of human MMP-1
    • Iyer S, Visse R, Nagase H, Acharya KR. Crystal structure of an active form of human MMP-1. J Mol Biol 362: 78-88, 2006.
    • (2006) J Mol Biol , vol.362 , pp. 78-88
    • Iyer, S.1    Visse, R.2    Nagase, H.3    Acharya, K.R.4
  • 56
    • 78650099684 scopus 로고    scopus 로고
    • Role of matrix metalloproteinase-3 in neurodegeneration
    • Kim EM, Hwang O. Role of matrix metalloproteinase-3 in neurodegeneration. J Neurochem 116: 22-32, 2011.
    • (2011) J Neurochem , vol.116 , pp. 22-32
    • Kim, E.M.1    Hwang, O.2
  • 58
    • 70249085914 scopus 로고    scopus 로고
    • Altered apoptosis of inflammatory neutrophils in MMP-9-deficient mice is due to lower expression and activity of caspase-3
    • Kolaczkowska E, Koziol A, Plytycz B, Arnold B, Opdenakker G. Altered apoptosis of inflammatory neutrophils in MMP-9-deficient mice is due to lower expression and activity of caspase-3. Immunol Lett 126: 73-82, 2009.
    • (2009) Immunol Lett , vol.126 , pp. 73-82
    • Kolaczkowska, E.1    Koziol, A.2    Plytycz, B.3    Arnold, B.4    Opdenakker, G.5
  • 62
    • 0036063760 scopus 로고    scopus 로고
    • The structure, regulation, and function of human matrix metalloproteinase-13
    • Leeman MF, Curran S, Murray GI. The structure, regulation, and function of human matrix metalloproteinase-13. Crit Rev Biochem Mol Biol 37: 149-166, 2002.
    • (2002) Crit Rev Biochem Mol Biol , vol.37 , pp. 149-166
    • Leeman, M.F.1    Curran, S.2    Murray, G.I.3
  • 64
    • 18744383614 scopus 로고    scopus 로고
    • Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury
    • Li Q, Park PW, Wilson CL, Parks WC. Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 111: 635-646, 2002.
    • (2002) Cell , vol.111 , pp. 635-646
    • Li, Q.1    Park, P.W.2    Wilson, C.L.3    Parks, W.C.4
  • 65
    • 39549098861 scopus 로고    scopus 로고
    • Epithelial-tomesenchymal transition is a potential pathway leading to podocyte dysfunction and proteinuria
    • Li Y, Kang YS, Dai C, Kiss LP, Wen X, Liu Y. Epithelial-tomesenchymal transition is a potential pathway leading to podocyte dysfunction and proteinuria. Am J Pathol 172: 299-308, 2008.
    • (2008) Am J Pathol , vol.172 , pp. 299-308
    • Li, Y.1    Kang, Y.S.2    Dai, C.3    Kiss, L.P.4    Wen, X.5    Liu, Y.6
  • 66
    • 17844383733 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1 associates with intracellular organelles and confers resistance to lamin A/C degradation during apoptosis
    • Limb GA, Matter K, Murphy G, Cambrey AD, Bishop PN, Morris GE, Khaw PT. Matrix metalloproteinase-1 associates with intracellular organelles and confers resistance to lamin A/C degradation during apoptosis. Am J Pathol 166: 1555-1563, 2005.
    • (2005) Am J Pathol , vol.166 , pp. 1555-1563
    • Limb, G.A.1    Matter, K.2    Murphy, G.3    Cambrey, A.D.4    Bishop, P.N.5    Morris, G.E.6    Khaw, P.T.7
  • 67
    • 0036310677 scopus 로고    scopus 로고
    • Inhibition of apoptosis in rat mesangial cells by tissue inhibitor of metalloproteinase-1
    • Lin H, Chen X, Wang J, Yu Z. Inhibition of apoptosis in rat mesangial cells by tissue inhibitor of metalloproteinase-1. Kidney Int 62: 60-69, 2002.
    • (2002) Kidney Int , vol.62 , pp. 60-69
    • Lin, H.1    Chen, X.2    Wang, J.3    Yu, Z.4
  • 68
    • 77950615625 scopus 로고    scopus 로고
    • Integrative urinary peptidomics in renal transplantation identifies biomarkers for acute rejection
    • Ling XB, Sigdel TK, Lau K, Ying L, Lau I, Schilling J, Sarwal MM. Integrative urinary peptidomics in renal transplantation identifies biomarkers for acute rejection. J Am Soc Nephrol 21: 646-653, 2010.
    • (2010) J Am Soc Nephrol , vol.21 , pp. 646-653
    • Ling, X.B.1    Sigdel, T.K.2    Lau, K.3    Ying, L.4    Lau, I.5    Schilling, J.6    Sarwal, M.M.7
  • 69
    • 33745876549 scopus 로고    scopus 로고
    • Increase in extracellular cross-linking by tissue transglutaminase and reduction in expression of MMP-9 contribute differentially to focal segmental glomerulosclerosis in rats
    • Liu S, Li Y, Zhao H, Chen D, Huang Q, Wang S, Zou W, Zhang Y, Li X, Huang H. Increase in extracellular cross-linking by tissue transglutaminase and reduction in expression of MMP-9 contribute differentially to focal segmental glomerulosclerosis in rats. Mol Cell Biochem 284: 9-17, 2006.
    • (2006) Mol Cell Biochem , vol.284 , pp. 9-17
    • Liu, S.1    Li, Y.2    Zhao, H.3    Chen, D.4    Huang, Q.5    Wang, S.6    Zou, W.7    Zhang, Y.8    Li, X.9    Huang, H.10
  • 70
    • 82355190219 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of renal fibrosis
    • Liu Y. Cellular and molecular mechanisms of renal fibrosis. Nat Rev Nephrol 7: 684-696, 2011.
    • (2011) Nat Rev Nephrol , vol.7 , pp. 684-696
    • Liu, Y.1
  • 71
    • 77949351029 scopus 로고    scopus 로고
    • New insights into epithelial-mesenchymal transition in kidney fibrosis
    • Liu Y. New insights into epithelial-mesenchymal transition in kidney fibrosis. J Am Soc Nephrol 21: 212-222, 2010.
    • (2010) J Am Soc Nephrol , vol.21 , pp. 212-222
    • Liu, Y.1
  • 72
    • 79960027287 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 promotes NIH3T3 fibroblast proliferation by activating p-Akt and cell cycle progression
    • Lu Y, Liu S, Zhang S, Cai G, Jiang H, Su H, Li X, Hong Q, Zhang X, Chen X. Tissue inhibitor of metalloproteinase-1 promotes NIH3T3 fibroblast proliferation by activating p-Akt and cell cycle progression. Mol Cells 31: 225-230, 2011.
    • (2011) Mol Cells , vol.31 , pp. 225-230
    • Lu, Y.1    Liu, S.2    Zhang, S.3    Cai, G.4    Jiang, H.5    Su, H.6    Li, X.7    Hong, Q.8    Zhang, X.9    Chen, X.10
  • 74
    • 32844457706 scopus 로고    scopus 로고
    • Transcriptional regulation of matrix metalloprotease gene expression in health and disease
    • Mancini A, Di Battista JA. Transcriptional regulation of matrix metalloprotease gene expression in health and disease. Front Biosci 11: 423-446, 2006.
    • (2006) Front Biosci , vol.11 , pp. 423-446
    • Mancini, A.1    di Battista, J.A.2
  • 75
    • 73549094456 scopus 로고    scopus 로고
    • Matrilysin (Matrix Metalloproteinase-7) regulates anti-inflammatory and antifibrotic pulmonary dendritic cells that express CD103 (alpha(E)beta(7)-integrin)
    • Manicone AM, Huizar I, McGuire JK. Matrilysin (Matrix Metalloproteinase-7) regulates anti-inflammatory and antifibrotic pulmonary dendritic cells that express CD103 (alpha(E)beta(7)-integrin). Am J Pathol 175: 2319-2331, 2009.
    • (2009) Am J Pathol , vol.175 , pp. 2319-2331
    • Manicone, A.M.1    Huizar, I.2    McGuire, J.K.3
  • 76
    • 0038676949 scopus 로고    scopus 로고
    • The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein
    • Marchenko GN, Marchenko ND, Strongin AY. The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein. Biochem J 372: 503-515, 2003.
    • (2003) Biochem J , vol.372 , pp. 503-515
    • Marchenko, G.N.1    Marchenko, N.D.2    Strongin, A.Y.3
  • 77
    • 0035168304 scopus 로고    scopus 로고
    • Induction of metalloproteinases by glomerular mesangial cells stimulated by proteins of the extracellular matrix
    • Martin J, Eynstone L, Davies M, Steadman R. Induction of metalloproteinases by glomerular mesangial cells stimulated by proteins of the extracellular matrix. J Am Soc Nephrol 12: 88-96, 2001.
    • (2001) J Am Soc Nephrol , vol.12 , pp. 88-96
    • Martin, J.1    Eynstone, L.2    Davies, M.3    Steadman, R.4
  • 78
    • 0037568364 scopus 로고    scopus 로고
    • Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium
    • McGuire JK, Li Q, Parks WC. Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium. Am J Pathol 162: 1831-1843, 2003.
    • (2003) Am J Pathol , vol.162 , pp. 1831-1843
    • McGuire, J.K.1    Li, Q.2    Parks, W.C.3
  • 81
    • 2442642574 scopus 로고    scopus 로고
    • Participation of the matrix metalloproteinase inhibitor in Thy-1 nephritis
    • Mitani O, Katoh M, Shigematsu H. Participation of the matrix metalloproteinase inhibitor in Thy-1 nephritis. Pathol Int 54: 241-250, 2004.
    • (2004) Pathol Int , vol.54 , pp. 241-250
    • Mitani, O.1    Katoh, M.2    Shigematsu, H.3
  • 82
    • 83555168313 scopus 로고    scopus 로고
    • An alternate perspective on the roles of TIMPs and MMPs in Pathology
    • Moore CS, Crocker SJ. An alternate perspective on the roles of TIMPs and MMPs in Pathology. Am J Pathol 180: 12-16, 2012.
    • (2012) Am J Pathol , vol.180 , pp. 12-16
    • Moore, C.S.1    Crocker, S.J.2
  • 84
    • 50849091591 scopus 로고    scopus 로고
    • Cancer cells, adipocytes and matrix metalloproteinase 11: A vicious tumor progression cycle
    • Motrescu ER, Rio MC. Cancer cells, adipocytes and matrix metalloproteinase 11: a vicious tumor progression cycle. Biol Chem 389: 1037-1041, 2008.
    • (2008) Biol Chem , vol.389 , pp. 1037-1041
    • Motrescu, E.R.1    Rio, M.C.2
  • 86
    • 60749109564 scopus 로고    scopus 로고
    • Characterization of the transcriptional regulation of the human MT1-MMP gene and association of risk reduction for focalsegmental glomerulosclerosis with two functional promoter SNPs
    • Munkert A, Helmchen U, Kemper MJ, Bubenheim M, Stahl RA, Harendza S. Characterization of the transcriptional regulation of the human MT1-MMP gene and association of risk reduction for focalsegmental glomerulosclerosis with two functional promoter SNPs. Nephrol Dial Transplant 24: 735-742, 2009.
    • (2009) Nephrol Dial Transplant , vol.24 , pp. 735-742
    • Munkert, A.1    Helmchen, U.2    Kemper, M.J.3    Bubenheim, M.4    Stahl, R.A.5    Harendza, S.6
  • 87
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H, Visse R, Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 69: 562-573, 2006.
    • (2006) Cardiovasc Res , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 88
    • 0033957602 scopus 로고    scopus 로고
    • Elevation of serum levels of metalloproteinase-1, tissue inhibitor of metalloproteinase-1 and type IV collagen, and plasma levels of metalloproteinase-9 in polycystic kidney disease
    • Nakamura T, Ushiyama C, Suzuki S, Ebihara I, Shimada N, Koide H. Elevation of serum levels of metalloproteinase-1, tissue inhibitor of metalloproteinase-1 and type IV collagen, and plasma levels of metalloproteinase-9 in polycystic kidney disease. Am J Nephrol 20: 32-36, 2000.
    • (2000) Am J Nephrol , vol.20 , pp. 32-36
    • Nakamura, T.1    Ushiyama, C.2    Suzuki, S.3    Ebihara, I.4    Shimada, N.5    Koide, H.6
  • 89
    • 4644310412 scopus 로고    scopus 로고
    • TNF-alpha and IL-1beta-mediated regulation of MMP-9 and TIMP-1 in renal proximal tubular cells
    • Nee LE, McMorrow T, Campbell E, Slattery C, Ryan MP. TNF-alpha and IL-1beta-mediated regulation of MMP-9 and TIMP-1 in renal proximal tubular cells. Kidney Int 66: 1376-1386, 2004.
    • (2004) Kidney Int , vol.66 , pp. 1376-1386
    • Nee, L.E.1    McMorrow, T.2    Campbell, E.3    Slattery, C.4    Ryan, M.P.5
  • 95
    • 0036741135 scopus 로고    scopus 로고
    • Molecular determinants of metalloproteinase substrate specificity: Matrix metalloproteinase substrate binding domains, modules, and exosites
    • Overall CM. Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites. Mol Biotechnol 22: 51-86, 2002.
    • (2002) Mol Biotechnol , vol.22 , pp. 51-86
    • Overall, C.M.1
  • 97
    • 33744938426 scopus 로고    scopus 로고
    • Matrix metalloproteases in aberrant fibrotic tissue remodeling
    • Pardo A, Selman M. Matrix metalloproteases in aberrant fibrotic tissue remodeling. Proc Am Thorac Soc 3: 383-388, 2006.
    • (2006) Proc Am Thorac Soc , vol.3 , pp. 383-388
    • Pardo, A.1    Selman, M.2
  • 98
    • 70449726460 scopus 로고    scopus 로고
    • Effects of detergents on catalytic activity of human endometase/matrilysin 2, a putative cancer biomarker
    • Park HI, Lee S, Ullah A, Cao Q, Sang QX. Effects of detergents on catalytic activity of human endometase/matrilysin 2, a putative cancer biomarker. Anal Biochem 396: 262-268, 2010.
    • (2010) Anal Biochem , vol.396 , pp. 262-268
    • Park, H.I.1    Lee, S.2    Ullah, A.3    Cao, Q.4    Sang, Q.X.5
  • 99
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • Parks WC, Wilson CL, Lopez-Boado YS. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat Rev Immunol 4: 617-629, 2004.
    • (2004) Nat Rev Immunol , vol.4 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    Lopez-Boado, Y.S.3
  • 100
    • 80051788293 scopus 로고    scopus 로고
    • Matrix metalloprotease-9 induces transforming growth factor-beta(1) production in airway epithelium via activation of epidermal growth factor receptors
    • Perng DW, Chang KT, Su KC, Wu YC, Chen CS, Hsu WH, Tsai CM, Lee YC. Matrix metalloprotease-9 induces transforming growth factor-beta(1) production in airway epithelium via activation of epidermal growth factor receptors. Life Sci 89: 204-212, 2011.
    • (2011) Life Sci , vol.89 , pp. 204-212
    • Perng, D.W.1    Chang, K.T.2    Su, K.C.3    Wu, Y.C.4    Chen, C.S.5    Hsu, W.H.6    Tsai, C.M.7    Lee, Y.C.8
  • 101
    • 0033576645 scopus 로고    scopus 로고
    • The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis
    • Powell WC, Fingleton B, Wilson CL, Boothby M, Matrisian LM. The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis. Curr Biol 9: 1441-1447, 1999.
    • (1999) Curr Biol , vol.9 , pp. 1441-1447
    • Powell, W.C.1    Fingleton, B.2    Wilson, C.L.3    Boothby, M.4    Matrisian, L.M.5
  • 102
    • 79958779687 scopus 로고    scopus 로고
    • Scar wars: Mapping the fate of epithelialmesenchymal-myofibroblast transition
    • Quaggin SE, Kapus A. Scar wars: mapping the fate of epithelialmesenchymal-myofibroblast transition. Kidney Int 80: 41-50, 2011.
    • (2011) Kidney Int , vol.80 , pp. 41-50
    • Quaggin, S.E.1    Kapus, A.2
  • 103
    • 33745686157 scopus 로고    scopus 로고
    • Role for macrophage metalloelastase in glomerular basement membrane damage associated with Alport syndrome
    • Rao VH, Meehan DT, Delimont D, Nakajima M, Wada T, Gratton MA, Cosgrove D. Role for macrophage metalloelastase in glomerular basement membrane damage associated with Alport syndrome. Am J Pathol 169: 32-46, 2006.
    • (2006) Am J Pathol , vol.169 , pp. 32-46
    • Rao, V.H.1    Meehan, D.T.2    Delimont, D.3    Nakajima, M.4    Wada, T.5    Gratton, M.A.6    Cosgrove, D.7
  • 108
  • 109
    • 36049045015 scopus 로고    scopus 로고
    • Serum matrix metalloproteinases MMP-2 and MMP-9 and metalloproteinase tissue inhibitors TIMP-1 and TIMP-2 in diabetic nephropathy
    • Rysz J, Banach M, Stolarek RA, Pasnik J, Cialkowska-Rysz A, Koktysz R, Piechota M, Baj Z. Serum matrix metalloproteinases MMP-2 and MMP-9 and metalloproteinase tissue inhibitors TIMP-1 and TIMP-2 in diabetic nephropathy. J Nephrol 20: 444-452, 2007.
    • (2007) J Nephrol , vol.20 , pp. 444-452
    • Rysz, J.1    Banach, M.2    Stolarek, R.A.3    Pasnik, J.4    Cialkowska-Rysz, A.5    Koktysz, R.6    Piechota, M.7    Baj, Z.8
  • 114
    • 57049099165 scopus 로고    scopus 로고
    • Ciglitazone, a PPARgamma agonist, ameliorates diabetic nephropathy in part through homocysteine clearance
    • Sen U, Rodriguez WE, Tyagi N, Kumar M, Kundu S, Tyagi SC. Ciglitazone, a PPARgamma agonist, ameliorates diabetic nephropathy in part through homocysteine clearance. Am J Physiol Endocrinol Metab 295: E1205-E1212, 2008.
    • (2008) Am J Physiol Endocrinol Metab , vol.295
    • Sen, U.1    Rodriguez, W.E.2    Tyagi, N.3    Kumar, M.4    Kundu, S.5    Tyagi, S.C.6
  • 115
    • 79957600358 scopus 로고    scopus 로고
    • The gene expression profile of matrix metalloproteinases and their inhibitors in children with Henoch-Schonlein purpura
    • Shin JI, Song KS, Kim H, Cho NH, Kim J, Kim HS, Lee JS. The gene expression profile of matrix metalloproteinases and their inhibitors in children with Henoch-Schonlein purpura. Br J Dermatol 164: 1348-1355, 2011.
    • (2011) Br J Dermatol , vol.164 , pp. 1348-1355
    • Shin, J.I.1    Song, K.S.2    Kim, H.3    Cho, N.H.4    Kim, J.5    Kim, H.S.6    Lee, J.S.7
  • 116
    • 77957226350 scopus 로고    scopus 로고
    • Matrix metalloproteinase (MMP-9 and MMP-2) gene polymorphisms influence allograft survival in renal transplant recipients
    • Singh R, Srivastava P, Srivastava A, Mittal RD. Matrix metalloproteinase (MMP-9 and MMP-2) gene polymorphisms influence allograft survival in renal transplant recipients. Nephrol Dial Transplant 25: 3393-3401, 2010.
    • (2010) Nephrol Dial Transplant , vol.25 , pp. 3393-3401
    • Singh, R.1    Srivastava, P.2    Srivastava, A.3    Mittal, R.D.4
  • 118
    • 43049084341 scopus 로고    scopus 로고
    • MT4-(MMP17) and MT6-MMP (MMP25), A unique set of membraneanchored matrix metalloproteinases: Properties and expression in cancer
    • Sohail A, Sun Q, Zhao H, Bernardo MM, Cho JA, Fridman R. MT4-(MMP17) and MT6-MMP (MMP25), A unique set of membraneanchored matrix metalloproteinases: properties and expression in cancer. Cancer Metastasis Rev 27: 289-302, 2008.
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 289-302
    • Sohail, A.1    Sun, Q.2    Zhao, H.3    Bernardo, M.M.4    Cho, J.A.5    Fridman, R.6
  • 119
    • 0031890320 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases attenuates anti-Thy1.1 nephritis
    • Steinmann-Niggli K, Ziswiler R, Kung M, Marti HP. Inhibition of matrix metalloproteinases attenuates anti-Thy1.1 nephritis. J Am Soc Nephrol 9: 397-407, 1998.
    • (1998) J Am Soc Nephrol , vol.9 , pp. 397-407
    • Steinmann-Niggli, K.1    Ziswiler, R.2    Kung, M.3    Marti, H.P.4
  • 120
    • 2442642567 scopus 로고    scopus 로고
    • Matrilysin (MMP-7) expression in renal tubular damage: Association with Wnt4
    • Surendran K, Simon TC, Liapis H, McGuire JK. Matrilysin (MMP-7) expression in renal tubular damage: association with Wnt4. Kidney Int 65: 2212-2222, 2004.
    • (2004) Kidney Int , vol.65 , pp. 2212-2222
    • Surendran, K.1    Simon, T.C.2    Liapis, H.3    McGuire, J.K.4
  • 122
    • 45949086634 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7 (matrilysin) controls neutrophil egress by generating chemokine gradients
    • Swee M, Wilson CL, Wang Y, McGuire JK, Parks WC. Matrix metalloproteinase-7 (matrilysin) controls neutrophil egress by generating chemokine gradients. J Leukoc Biol 83: 1404-1412, 2008.
    • (2008) J Leukoc Biol , vol.83 , pp. 1404-1412
    • Swee, M.1    Wilson, C.L.2    Wang, Y.3    McGuire, J.K.4    Parks, W.C.5
  • 123
    • 77749291745 scopus 로고    scopus 로고
    • Macrophage matrix metalloproteinase-9 mediates epithelial-mesenchymal transition in vitro in murine renal tubular cells
    • Tan TK, Zheng G, Hsu TT, Wang Y, Lee VW, Tian X, Wang Y, Cao Q, Wang Y, Harris DC. Macrophage matrix metalloproteinase-9 mediates epithelial-mesenchymal transition in vitro in murine renal tubular cells. Am J Pathol 176: 1256-1270, 2010.
    • (2010) Am J Pathol , vol.176 , pp. 1256-1270
    • Tan, T.K.1    Zheng, G.2    Hsu, T.T.3    Wang, Y.4    Lee, V.W.5    Tian, X.6    Wang, Y.7    Cao, Q.8    Wang, Y.9    Harris, D.C.10
  • 124
    • 58849101696 scopus 로고    scopus 로고
    • Endothelial nitric oxide deficiency reduces MMP-13-mediated cleavage of ICAM-1 in vascular endothelium: A role in atherosclerosis
    • Tarin C, Gomez M, Calvo E, Lopez JA, Zaragoza C. Endothelial nitric oxide deficiency reduces MMP-13-mediated cleavage of ICAM-1 in vascular endothelium: a role in atherosclerosis. Arterioscler Thromb Vasc Biol 29: 27-32, 2009.
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 27-32
    • Tarin, C.1    Gomez, M.2    Calvo, E.3    Lopez, J.A.4    Zaragoza, C.5
  • 125
    • 2342632543 scopus 로고    scopus 로고
    • Levels of urinary matrix metalloproteinase-9 (MMP-9) and renal injuries in patients with type 2 diabetic nephropathy
    • Tashiro K, Koyanagi I, Ohara I, Ito T, Saitoh A, Horikoshi S, Tomino Y. Levels of urinary matrix metalloproteinase-9 (MMP-9) and renal injuries in patients with type 2 diabetic nephropathy. J Clin Lab Anal 18: 206-210, 2004.
    • (2004) J Clin Lab Anal , vol.18 , pp. 206-210
    • Tashiro, K.1    Koyanagi, I.2    Ohara, I.3    Ito, T.4    Saitoh, A.5    Horikoshi, S.6    Tomino, Y.7
  • 126
    • 63449086757 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Their potential role in the pathogenesis of diabetic nephropathy
    • Thrailkill KM, Clay Bunn R, Fowlkes JL. Matrix metalloproteinases: their potential role in the pathogenesis of diabetic nephropathy. Endocrine 35: 1-10, 2009.
    • (2009) Endocrine , vol.35 , pp. 1-10
    • Thrailkill, K.M.1    Clay Bunn, R.2    Fowlkes, J.L.3
  • 128
    • 1942453449 scopus 로고    scopus 로고
    • Decreased collagen-degrading activity could be a marker of prolonged mesangial matrix expansion
    • Tomita M, Koike H, Han GD, Shimizu F, Kawachi H. Decreased collagen-degrading activity could be a marker of prolonged mesangial matrix expansion. Clin Exp Nephrol 8: 17-26, 2004.
    • (2004) Clin Exp Nephrol , vol.8 , pp. 17-26
    • Tomita, M.1    Koike, H.2    Han, G.D.3    Shimizu, F.4    Kawachi, H.5
  • 129
    • 55249118574 scopus 로고    scopus 로고
    • Three matrix metalloproteinases are required in vivo for macrophage migration during embryonic development
    • Tomlinson ML, Garcia-Morales C, Abu-Elmagd M, Wheeler GN. Three matrix metalloproteinases are required in vivo for macrophage migration during embryonic development. Mech Dev 125: 1059-1070, 2008.
    • (2008) Mech Dev , vol.125 , pp. 1059-1070
    • Tomlinson, M.L.1    Garcia-Morales, C.2    Abu-Elmagd, M.3    Wheeler, G.N.4
  • 130
    • 0034858149 scopus 로고    scopus 로고
    • The human neutrophil lipocalin supports the allosteric activation of matrix metalloproteinases
    • Tschesche H, Zolzer V, Triebel S, Bartsch S. The human neutrophil lipocalin supports the allosteric activation of matrix metalloproteinases. Eur J Biochem 268: 1918-1928, 2001.
    • (2001) Eur J Biochem , vol.268 , pp. 1918-1928
    • Tschesche, H.1    Zolzer, V.2    Triebel, S.3    Bartsch, S.4
  • 131
    • 15844379355 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 (gelatinase A) regulates glomerular mesangial cell proliferation and differentiation
    • Turck J, Pollock AS, Lee LK, Marti HP, Lovett DH. Matrix metalloproteinase 2 (gelatinase A) regulates glomerular mesangial cell proliferation and differentiation. J Biol Chem 271: 15074-15083, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 15074-15083
    • Turck, J.1    Pollock, A.S.2    Lee, L.K.3    Marti, H.P.4    Lovett, D.H.5
  • 132
    • 66749086267 scopus 로고    scopus 로고
    • Glomerular matrix metalloproteinases and their regulators in the pathogenesis of lupus nephritis
    • Tveita A, Rekvig OP, Zykova SN. Glomerular matrix metalloproteinases and their regulators in the pathogenesis of lupus nephritis. Arthritis Res Ther 10: 229, 2008.
    • (2008) Arthritis Res Ther , vol.10 , pp. 229
    • Tveita, A.1    Rekvig, O.P.2    Zykova, S.N.3
  • 133
    • 53949095413 scopus 로고    scopus 로고
    • Increased glomerular matrix metalloproteinase activity in murine lupus nephritis
    • Tveita AA, Rekvig OP, Zykova SN. Increased glomerular matrix metalloproteinase activity in murine lupus nephritis. Kidney Int 74: 1150-1158, 2008.
    • (2008) Kidney Int , vol.74 , pp. 1150-1158
    • Tveita, A.A.1    Rekvig, O.P.2    Zykova, S.N.3
  • 134
    • 0036020910 scopus 로고    scopus 로고
    • Glomerular distribution and gelatinolytic activity of matrix metalloproteinases in human glomerulonephritis
    • Urushihara M, Kagami S, Kuhara T, Tamaki T, Kuroda Y. Glomerular distribution and gelatinolytic activity of matrix metalloproteinases in human glomerulonephritis. Nephrol Dial Transplant 17: 1189-1196, 2002.
    • (2002) Nephrol Dial Transplant , vol.17 , pp. 1189-1196
    • Urushihara, M.1    Kagami, S.2    Kuhara, T.3    Tamaki, T.4    Kuroda, Y.5
  • 136
    • 33745829453 scopus 로고    scopus 로고
    • Matrix metalloproteinase-8: Cleavage can be decisive
    • Van Lint P, Libert C. Matrix metalloproteinase-8: cleavage can be decisive. Cytokine Growth Factor Rev 17: 217-223, 2006.
    • (2006) Cytokine Growth Factor Rev , vol.17 , pp. 217-223
    • van Lint, P.1    Libert, C.2
  • 137
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart HE, Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA 87: 5578-5582, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5578-5582
    • van Wart, H.E.1    Birkedal-Hansen, H.2
  • 138
    • 0033582513 scopus 로고    scopus 로고
    • Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members
    • Velasco G, Pendas AM, Fueyo A, Knauper V, Murphy G, Lopez-Otin C. Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members. J Biol Chem 274: 4570-4576, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 4570-4576
    • Velasco, G.1    Pendas, A.M.2    Fueyo, A.3    Knauper, V.4    Murphy, G.5    Lopez-Otin, C.6
  • 139
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • Visse R, Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res 92: 827-839, 2003.
    • (2003) Circ Res , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 140
    • 81155150123 scopus 로고    scopus 로고
    • Canonical Wnt β-catenin signaling mediates transforming growth factor-β1-driven podocyte injury and proteinuria
    • Wang D, Dai C, Li Y, Liu Y. Canonical Wnt β-catenin signaling mediates transforming growth factor-β1-driven podocyte injury and proteinuria. Kidney Int 80: 1159-1169, 2011.
    • (2011) Kidney Int , vol.80 , pp. 1159-1169
    • Wang, D.1    Dai, C.2    Li, Y.3    Liu, Y.4
  • 141
  • 142
    • 33749234589 scopus 로고    scopus 로고
    • Associations of increases in serum creatinine with mortality and length of hospital stay after coronary angiography
    • Weisbord SD, Chen H, Stone RA, Kip KE, Fine MJ, Saul MI, Palevsky PM. Associations of increases in serum creatinine with mortality and length of hospital stay after coronary angiography. J Am Soc Nephrol 17: 2871-2877, 2006.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 2871-2877
    • Weisbord, S.D.1    Chen, H.2    Stone, R.A.3    Kip, K.E.4    Fine, M.J.5    Saul, M.I.6    Palevsky, P.M.7
  • 143
    • 23944488505 scopus 로고    scopus 로고
    • Endostatin signaling and regulation of endothelial cell-matrix interactions
    • Wickstrom SA, Alitalo K, Keski-Oja J. Endostatin signaling and regulation of endothelial cell-matrix interactions. Adv Cancer Res 94: 197-229, 2005.
    • (2005) Adv Cancer Res , vol.94 , pp. 197-229
    • Wickstrom, S.A.1    Alitalo, K.2    Keski-Oja, J.3
  • 146
  • 148
    • 0036854980 scopus 로고    scopus 로고
    • Disruption of tissue-type plasminogen activator gene in mice reduces renal interstitial fibrosis in obstructive nephropathy
    • Yang J, Shultz RW, Mars WM, Wegner RE, Li Y, Dai C, Nejak K, Liu Y. Disruption of tissue-type plasminogen activator gene in mice reduces renal interstitial fibrosis in obstructive nephropathy. J Clin Invest 110: 1525-1538, 2002.
    • (2002) J Clin Invest , vol.110 , pp. 1525-1538
    • Yang, J.1    Shultz, R.W.2    Mars, W.M.3    Wegner, R.E.4    Li, Y.5    Dai, C.6    Nejak, K.7    Liu, Y.8
  • 149
    • 33750466237 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase is involved in the migration of human monocyte-derived dendritic cells
    • Yang MX, Qu X, Kong BH, Lam QL, Shao QQ, Deng BP, Ko KH, Lu L. Membrane type 1-matrix metalloproteinase is involved in the migration of human monocyte-derived dendritic cells. Immunol Cell Biol 84: 557-562, 2006.
    • (2006) Immunol Cell Biol , vol.84 , pp. 557-562
    • Yang, M.X.1    Qu, X.2    Kong, B.H.3    Lam, Q.L.4    Shao, Q.Q.5    Deng, B.P.6    Ko, K.H.7    Lu, L.8
  • 150
    • 77954195454 scopus 로고    scopus 로고
    • Simvastatin protects diabetic rats against kidney injury through the suppression of renal matrix metalloproteinase-9 expression
    • Yao XM, Ye SD, Zai Z, Chen Y, Li XC, Yang GW, Wang YX, Chen K. Simvastatin protects diabetic rats against kidney injury through the suppression of renal matrix metalloproteinase-9 expression. J Endocrinol Invest 33: 292-296, 2010.
    • (2010) J Endocrinol Invest , vol.33 , pp. 292-296
    • Yao, X.M.1    Ye, S.D.2    Zai, Z.3    Chen, Y.4    Li, X.C.5    Yang, G.W.6    Wang, Y.X.7    Chen, K.8
  • 151
    • 38049156464 scopus 로고    scopus 로고
    • 2-induced metalloproteinase-9 is essential for dendritic cell migration
    • 2-induced metalloproteinase-9 is essential for dendritic cell migration. Blood 111: 260-270, 2008.
    • (2008) Blood , vol.111 , pp. 260-270
    • Yen, J.H.1    Khayrullina, T.2    Ganea, D.3
  • 152
    • 77955602944 scopus 로고    scopus 로고
    • Resolved: EMT produces fibroblasts in the kidney
    • Zeisberg M, Duffield JS. Resolved: EMT produces fibroblasts in the kidney. J Am Soc Nephrol 21: 1247-1253, 2010.
    • (2010) J Am Soc Nephrol , vol.21 , pp. 1247-1253
    • Zeisberg, M.1    Duffield, J.S.2
  • 154
    • 68449094056 scopus 로고    scopus 로고
    • Disruption of E-cadherin by matrix metalloproteinase directly mediates epithelial-mesenchymal transition downstream of transforming growth factor-beta1 in renal tubular epithelial cells
    • Zheng G, Lyons JG, Tan TK, Wang Y, Hsu TT, Min D, Succar L, Rangan GK, Hu M, Henderson BR, Alexander SI, Harris DC. Disruption of E-cadherin by matrix metalloproteinase directly mediates epithelial-mesenchymal transition downstream of transforming growth factor-beta1 in renal tubular epithelial cells. Am J Pathol 175: 580-591, 2009.
    • (2009) Am J Pathol , vol.175 , pp. 580-591
    • Zheng, G.1    Lyons, J.G.2    Tan, T.K.3    Wang, Y.4    Hsu, T.T.5    Min, D.6    Succar, L.7    Rangan, G.K.8    Hu, M.9    Henderson, B.R.10    Alexander, S.I.11    Harris, D.C.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.