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Volumn 228, Issue 1, 2013, Pages 12-17

The role of ADAM17 in metabolic inflammation

Author keywords

Inflammation; Insulin resistance; Macrophages; Metalloproteinase; Obesity; Steatosis

Indexed keywords

ADAM PROTEIN; ADAM17 PROTEIN; UNCLASSIFIED DRUG;

EID: 84876787262     PISSN: 00219150     EISSN: 18791484     Source Type: Journal    
DOI: 10.1016/j.atherosclerosis.2013.01.024     Document Type: Review
Times cited : (90)

References (70)
  • 1
    • 79960923986 scopus 로고    scopus 로고
    • ADAM17: a molecular switch to control inflammation and tissue regeneration
    • Scheller J., Chalaris A., Garbers C., et al. ADAM17: a molecular switch to control inflammation and tissue regeneration. Trends in Immunology 2011, 32:380-387.
    • (2011) Trends in Immunology , vol.32 , pp. 380-387
    • Scheller, J.1    Chalaris, A.2    Garbers, C.3
  • 2
    • 0032515018 scopus 로고    scopus 로고
    • An essential role for ectodomain shedding in mammalian development
    • Peschon J.J., Slack J.L., Reddy P., et al. An essential role for ectodomain shedding in mammalian development. Science (New York, N.Y) 1998, 282:1281-1284.
    • (1998) Science (New York, N.Y) , vol.282 , pp. 1281-1284
    • Peschon, J.J.1    Slack, J.L.2    Reddy, P.3
  • 3
    • 0032846604 scopus 로고    scopus 로고
    • Cutting edge: a dominant negative form of TNF-alpha converting enzyme inhibits proTNF and TNFRII secretion
    • Solomon K.A., Pesti N., Wu G., et al. Cutting edge: a dominant negative form of TNF-alpha converting enzyme inhibits proTNF and TNFRII secretion. Journal of Immunology 1999, 163:4105-4108.
    • (1999) Journal of Immunology , vol.163 , pp. 4105-4108
    • Solomon, K.A.1    Pesti, N.2    Wu, G.3
  • 4
    • 84859896499 scopus 로고    scopus 로고
    • The membrane-proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin-6 receptor and interleukin-1 receptor II
    • Lorenzen I., Lokau J., Dusterhoft S., et al. The membrane-proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin-6 receptor and interleukin-1 receptor II. FEBS Letters 2012, 586:1093-1100.
    • (2012) FEBS Letters , vol.586 , pp. 1093-1100
    • Lorenzen, I.1    Lokau, J.2    Dusterhoft, S.3
  • 5
    • 1842737700 scopus 로고    scopus 로고
    • Expression analysis of the entire MMP and TIMP gene families during mouse tissue development
    • Nuttall R.K., Sampieri C.L., Pennington C.J., et al. Expression analysis of the entire MMP and TIMP gene families during mouse tissue development. FEBS Letters 2004, 563:129-134.
    • (2004) FEBS Letters , vol.563 , pp. 129-134
    • Nuttall, R.K.1    Sampieri, C.L.2    Pennington, C.J.3
  • 6
    • 84860714018 scopus 로고    scopus 로고
    • TACE activation by MAPK-mediated regulation of cell surface dimerization and TIMP3 association
    • Xu P., Liu J., Sakaki-Yumoto M., et al. TACE activation by MAPK-mediated regulation of cell surface dimerization and TIMP3 association. Science Signaling 2012, 5:ra34.
    • (2012) Science Signaling , vol.5
    • Xu, P.1    Liu, J.2    Sakaki-Yumoto, M.3
  • 7
    • 84862909285 scopus 로고    scopus 로고
    • IRhom2 regulation of TACE controls TNF-mediated protection against Listeria and responses to LPS
    • McIlwain D.R., Lang P.A., Maretzky T., et al. iRhom2 regulation of TACE controls TNF-mediated protection against Listeria and responses to LPS. Science (New York, N.Y) 2012, 335:229-232.
    • (2012) Science (New York, N.Y) , vol.335 , pp. 229-232
    • McIlwain, D.R.1    Lang, P.A.2    Maretzky, T.3
  • 8
    • 84855822415 scopus 로고    scopus 로고
    • Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE
    • Adrain C., Zettl M., Christova Y., et al. Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE. Science (New York, N.Y) 2012, 335:225-228.
    • (2012) Science (New York, N.Y) , vol.335 , pp. 225-228
    • Adrain, C.1    Zettl, M.2    Christova, Y.3
  • 9
    • 73949110048 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases 3 regulates resolution of inflammation following acute lung injury
    • Gill S.E., Huizar I., Bench E.M., et al. Tissue inhibitor of metalloproteinases 3 regulates resolution of inflammation following acute lung injury. The American Journal of Pathology 2010, 176:64-73.
    • (2010) The American Journal of Pathology , vol.176 , pp. 64-73
    • Gill, S.E.1    Huizar, I.2    Bench, E.M.3
  • 10
    • 31044437380 scopus 로고    scopus 로고
    • Timp3 deficiency in insulin receptor-haploinsufficient mice promotes diabetes and vascular inflammation via increased TNF-alpha
    • Federici M., Hribal M.L., Menghini R., et al. Timp3 deficiency in insulin receptor-haploinsufficient mice promotes diabetes and vascular inflammation via increased TNF-alpha. The Journal of Clinical Investigation 2005, 115:3494-3505.
    • (2005) The Journal of Clinical Investigation , vol.115 , pp. 3494-3505
    • Federici, M.1    Hribal, M.L.2    Menghini, R.3
  • 11
    • 0038823617 scopus 로고    scopus 로고
    • Matrix metalloproteinases are differentially expressed in adipose tissue during obesity and modulate adipocyte differentiation
    • Chavey C., Mari B., Monthouel M.N., et al. Matrix metalloproteinases are differentially expressed in adipose tissue during obesity and modulate adipocyte differentiation. The Journal of Biological Chemistry 2003, 278:11888-11896.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 11888-11896
    • Chavey, C.1    Mari, B.2    Monthouel, M.N.3
  • 12
    • 82255185823 scopus 로고    scopus 로고
    • Decreased IRS2 and TIMP3 expression in monocytes from offspring of type 2 diabetic patients is correlated with insulin resistance and increased intima-media thickness
    • Cardellini M., Menghini R., Luzi A., et al. Decreased IRS2 and TIMP3 expression in monocytes from offspring of type 2 diabetic patients is correlated with insulin resistance and increased intima-media thickness. Diabetes 2011, 60:3265-3270.
    • (2011) Diabetes , vol.60 , pp. 3265-3270
    • Cardellini, M.1    Menghini, R.2    Luzi, A.3
  • 14
    • 0027459878 scopus 로고
    • Adipose expression of tumor necrosis factor-alpha: direct role in obesity-linked insulin resistance
    • Hotamisligil G.S., Shargill N.S., Spiegelman B.M. Adipose expression of tumor necrosis factor-alpha: direct role in obesity-linked insulin resistance. Science (New York, N.Y) 1993, 259:87-91.
    • (1993) Science (New York, N.Y) , vol.259 , pp. 87-91
    • Hotamisligil, G.S.1    Shargill, N.S.2    Spiegelman, B.M.3
  • 15
    • 8744309820 scopus 로고    scopus 로고
    • Weight reduction, but not a moderate intake of fish oil, lowers concentrations of inflammatory markers and PAI-1 antigen in obese men during the fasting and postprandial state
    • Jellema A., Plat J., Mensink R.P. Weight reduction, but not a moderate intake of fish oil, lowers concentrations of inflammatory markers and PAI-1 antigen in obese men during the fasting and postprandial state. European Journal of Clinical Investigation 2004, 34:766-773.
    • (2004) European Journal of Clinical Investigation , vol.34 , pp. 766-773
    • Jellema, A.1    Plat, J.2    Mensink, R.P.3
  • 17
    • 34547492488 scopus 로고    scopus 로고
    • PPARgamma activation primes human monocytes into alternative M2 macrophages with anti-inflammatory properties
    • Bouhlel M.A., Derudas B., Rigamonti E., et al. PPARgamma activation primes human monocytes into alternative M2 macrophages with anti-inflammatory properties. Cell Metabolism 2007, 6:137-143.
    • (2007) Cell Metabolism , vol.6 , pp. 137-143
    • Bouhlel, M.A.1    Derudas, B.2    Rigamonti, E.3
  • 18
  • 19
    • 80053262767 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme is a key mediator of abdominal aortic aneurysm development
    • Kaneko H., Anzai T., Horiuchi K., et al. Tumor necrosis factor-alpha converting enzyme is a key mediator of abdominal aortic aneurysm development. Atherosclerosis 2011, 218:470-478.
    • (2011) Atherosclerosis , vol.218 , pp. 470-478
    • Kaneko, H.1    Anzai, T.2    Horiuchi, K.3
  • 20
    • 84856551460 scopus 로고    scopus 로고
    • TIMP3 overexpression in macrophages protects from insulin resistance, adipose inflammation, and nonalcoholic fatty liver disease in mice
    • Menghini R., Casagrande V., Menini S., et al. TIMP3 overexpression in macrophages protects from insulin resistance, adipose inflammation, and nonalcoholic fatty liver disease in mice. Diabetes 2012, 61:454-462.
    • (2012) Diabetes , vol.61 , pp. 454-462
    • Menghini, R.1    Casagrande, V.2    Menini, S.3
  • 21
    • 83655167191 scopus 로고    scopus 로고
    • Overexpression of tissue inhibitor of metalloproteinase 3 in macrophages reduces atherosclerosis in low-density lipoprotein receptor knockout mice
    • Casagrande V., Menghini R., Menini S., et al. Overexpression of tissue inhibitor of metalloproteinase 3 in macrophages reduces atherosclerosis in low-density lipoprotein receptor knockout mice. Arteriosclerosis, Thrombosis, and Vascular Biology 2012, 32:74-81.
    • (2012) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.32 , pp. 74-81
    • Casagrande, V.1    Menghini, R.2    Menini, S.3
  • 22
    • 33745866965 scopus 로고    scopus 로고
    • Ectodomain shedding of preadipocyte factor 1 (Pref-1) by tumor necrosis factor alpha converting enzyme (TACE) and inhibition of adipocyte differentiation
    • Wang Y., Sul H.S. Ectodomain shedding of preadipocyte factor 1 (Pref-1) by tumor necrosis factor alpha converting enzyme (TACE) and inhibition of adipocyte differentiation. Molecular and Cellular Biology 2006, 26:5421-5435.
    • (2006) Molecular and Cellular Biology , vol.26 , pp. 5421-5435
    • Wang, Y.1    Sul, H.S.2
  • 23
    • 57349182490 scopus 로고    scopus 로고
    • Deficiency of TNFalpha converting enzyme (TACE/ADAM17) causes a lean, hypermetabolic phenotype in mice
    • Gelling R.W., Yan W., Al-Noori S., et al. Deficiency of TNFalpha converting enzyme (TACE/ADAM17) causes a lean, hypermetabolic phenotype in mice. Endocrinology 2008, 149:6053-6064.
    • (2008) Endocrinology , vol.149 , pp. 6053-6064
    • Gelling, R.W.1    Yan, W.2    Al-Noori, S.3
  • 24
    • 34948846112 scopus 로고    scopus 로고
    • Mice heterozygous for tumor necrosis factor-alpha converting enzyme are protected from obesity-induced insulin resistance and diabetes
    • Serino M., Menghini R., Fiorentino L., et al. Mice heterozygous for tumor necrosis factor-alpha converting enzyme are protected from obesity-induced insulin resistance and diabetes. Diabetes 2007, 56:2541-2546.
    • (2007) Diabetes , vol.56 , pp. 2541-2546
    • Serino, M.1    Menghini, R.2    Fiorentino, L.3
  • 25
    • 80053085356 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme inactivation ameliorates high-fat diet-induced insulin resistance and altered energy homeostasis
    • Kaneko H., Anzai T., Horiuchi K., et al. Tumor necrosis factor-alpha converting enzyme inactivation ameliorates high-fat diet-induced insulin resistance and altered energy homeostasis. Circulation Journal 2011, 75:2482-2490.
    • (2011) Circulation Journal , vol.75 , pp. 2482-2490
    • Kaneko, H.1    Anzai, T.2    Horiuchi, K.3
  • 26
    • 58649105336 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase 3 deficiency causes hepatic steatosis and adipose tissue inflammation in mice
    • Menghini R., Menini S., Amoruso R., et al. Tissue inhibitor of metalloproteinase 3 deficiency causes hepatic steatosis and adipose tissue inflammation in mice. Gastroenterology 2009, 136:663-672 e664.
    • (2009) Gastroenterology , vol.136
    • Menghini, R.1    Menini, S.2    Amoruso, R.3
  • 27
    • 0142053963 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha inhibits insulin's stimulating effect on glucose uptake and endothelium-dependent vasodilation in humans
    • Rask-Madsen C., Dominguez H., Ihlemann N., et al. Tumor necrosis factor-alpha inhibits insulin's stimulating effect on glucose uptake and endothelium-dependent vasodilation in humans. Circulation 2003, 108:1815-1821.
    • (2003) Circulation , vol.108 , pp. 1815-1821
    • Rask-Madsen, C.1    Dominguez, H.2    Ihlemann, N.3
  • 28
    • 0031785508 scopus 로고    scopus 로고
    • Effects of tumor necrosis factor-alpha on glucose metabolism in cultured human muscle cells from nondiabetic and type 2 diabetic subjects
    • Ciaraldi T.P., Carter L., Mudaliar S., et al. Effects of tumor necrosis factor-alpha on glucose metabolism in cultured human muscle cells from nondiabetic and type 2 diabetic subjects. Endocrinology 1998, 139:4793-4800.
    • (1998) Endocrinology , vol.139 , pp. 4793-4800
    • Ciaraldi, T.P.1    Carter, L.2    Mudaliar, S.3
  • 29
    • 0030756346 scopus 로고    scopus 로고
    • Protection from obesity-induced insulin resistance in mice lacking TNF-alpha function
    • Uysal K.T., Wiesbrock S.M., Marino M.W., et al. Protection from obesity-induced insulin resistance in mice lacking TNF-alpha function. Nature 1997, 389:610-614.
    • (1997) Nature , vol.389 , pp. 610-614
    • Uysal, K.T.1    Wiesbrock, S.M.2    Marino, M.W.3
  • 30
    • 0028031569 scopus 로고
    • Reduced tyrosine kinase activity of the insulin receptor in obesity-diabetes. Central role of tumor necrosis factor-alpha
    • Hotamisligil G.S., Budavari A., Murray D., et al. Reduced tyrosine kinase activity of the insulin receptor in obesity-diabetes. Central role of tumor necrosis factor-alpha. The Journal of Clinical Investigation 1994, 94:1543-1549.
    • (1994) The Journal of Clinical Investigation , vol.94 , pp. 1543-1549
    • Hotamisligil, G.S.1    Budavari, A.2    Murray, D.3
  • 31
    • 0035144307 scopus 로고    scopus 로고
    • Insulin/IGF-1 and TNF-alpha stimulate phosphorylation of IRS-1 at inhibitory Ser307 via distinct pathways
    • Rui L., Aguirre V., Kim J.K., et al. Insulin/IGF-1 and TNF-alpha stimulate phosphorylation of IRS-1 at inhibitory Ser307 via distinct pathways. The Journal of Clinical Investigation 2001, 107:181-189.
    • (2001) The Journal of Clinical Investigation , vol.107 , pp. 181-189
    • Rui, L.1    Aguirre, V.2    Kim, J.K.3
  • 32
    • 25844456730 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha induces skeletal muscle insulin resistance in healthy human subjects via inhibition of Akt substrate 160 phosphorylation
    • Plomgaard P., Bouzakri K., Krogh-Madsen R., et al. Tumor necrosis factor-alpha induces skeletal muscle insulin resistance in healthy human subjects via inhibition of Akt substrate 160 phosphorylation. Diabetes 2005, 54:2939-2945.
    • (2005) Diabetes , vol.54 , pp. 2939-2945
    • Plomgaard, P.1    Bouzakri, K.2    Krogh-Madsen, R.3
  • 33
    • 33751552452 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-induced skeletal muscle insulin resistance involves suppression of AMP-kinase signaling
    • Steinberg G.R., Michell B.J., van Denderen B.J., et al. Tumor necrosis factor alpha-induced skeletal muscle insulin resistance involves suppression of AMP-kinase signaling. Cell Metabolism 2006, 4:465-474.
    • (2006) Cell Metabolism , vol.4 , pp. 465-474
    • Steinberg, G.R.1    Michell, B.J.2    van Denderen, B.J.3
  • 34
    • 2342428466 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha produces insulin resistance in skeletal muscle by activation of inhibitor kappaB kinase in a p38 MAPK-dependent manner
    • de Alvaro C., Teruel T., Hernandez R., et al. Tumor necrosis factor alpha produces insulin resistance in skeletal muscle by activation of inhibitor kappaB kinase in a p38 MAPK-dependent manner. The Journal of Biological Chemistry 2004, 279:17070-17078.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 17070-17078
    • de Alvaro, C.1    Teruel, T.2    Hernandez, R.3
  • 35
    • 50949089015 scopus 로고    scopus 로고
    • SiRNA-mediated reduction of inhibitor of nuclear factor-kappaB kinase prevents tumor necrosis factor-alpha-induced insulin resistance in human skeletal muscle
    • Austin R.L., Rune A., Bouzakri K., et al. siRNA-mediated reduction of inhibitor of nuclear factor-kappaB kinase prevents tumor necrosis factor-alpha-induced insulin resistance in human skeletal muscle. Diabetes 2008, 57:2066-2073.
    • (2008) Diabetes , vol.57 , pp. 2066-2073
    • Austin, R.L.1    Rune, A.2    Bouzakri, K.3
  • 36
    • 69949130225 scopus 로고    scopus 로고
    • Impaired regulation of the TNF-alpha converting enzyme/tissue inhibitor of metalloproteinase 3 proteolytic system in skeletal muscle of obese type 2 diabetic patients: a new mechanism of insulin resistance in humans
    • Monroy A., Kamath S., Chavez A.O., et al. Impaired regulation of the TNF-alpha converting enzyme/tissue inhibitor of metalloproteinase 3 proteolytic system in skeletal muscle of obese type 2 diabetic patients: a new mechanism of insulin resistance in humans. Diabetologia 2009, 52:2169-2181.
    • (2009) Diabetologia , vol.52 , pp. 2169-2181
    • Monroy, A.1    Kamath, S.2    Chavez, A.O.3
  • 37
    • 70349633646 scopus 로고    scopus 로고
    • TIMP3 is reduced in atherosclerotic plaques from subjects with type 2 diabetes and increased by SirT1
    • Cardellini M., Menghini R., Martelli E., et al. TIMP3 is reduced in atherosclerotic plaques from subjects with type 2 diabetes and increased by SirT1. Diabetes 2009, 58:2396-2401.
    • (2009) Diabetes , vol.58 , pp. 2396-2401
    • Cardellini, M.1    Menghini, R.2    Martelli, E.3
  • 38
    • 50949088445 scopus 로고    scopus 로고
    • Candidate genes for plasma triglyceride, FFA, and glucose revealed from an intercross between inbred mouse strains NZB/B1NJ and NZW/LacJ
    • Su Z., Tsaih S.W., Szatkiewicz J., et al. Candidate genes for plasma triglyceride, FFA, and glucose revealed from an intercross between inbred mouse strains NZB/B1NJ and NZW/LacJ. Journal of Lipid Research 2008, 49:1500-1510.
    • (2008) Journal of Lipid Research , vol.49 , pp. 1500-1510
    • Su, Z.1    Tsaih, S.W.2    Szatkiewicz, J.3
  • 39
    • 73149086166 scopus 로고    scopus 로고
    • Genes and gene expression modules associated with caloric restriction and aging in the laboratory mouse
    • Swindell W.R. Genes and gene expression modules associated with caloric restriction and aging in the laboratory mouse. BMC Genomics 2009, 10:585.
    • (2009) BMC Genomics , vol.10 , pp. 585
    • Swindell, W.R.1
  • 40
    • 73449086315 scopus 로고    scopus 로고
    • Increased tumor necrosis factor alpha-converting enzyme activity induces insulin resistance and hepatosteatosis in mice
    • Fiorentino L., Vivanti A., Cavalera M., et al. Increased tumor necrosis factor alpha-converting enzyme activity induces insulin resistance and hepatosteatosis in mice. Hepatology (Baltimore, Md) 2010, 51:103-110.
    • (2010) Hepatology (Baltimore, Md) , vol.51 , pp. 103-110
    • Fiorentino, L.1    Vivanti, A.2    Cavalera, M.3
  • 41
    • 40549135297 scopus 로고    scopus 로고
    • Contribution of de novo fatty acid synthesis to hepatic steatosis and insulin resistance: lessons from genetically engineered mice
    • Postic C., Girard J. Contribution of de novo fatty acid synthesis to hepatic steatosis and insulin resistance: lessons from genetically engineered mice. The Journal of Clinical Investigation 2008, 118:829-838.
    • (2008) The Journal of Clinical Investigation , vol.118 , pp. 829-838
    • Postic, C.1    Girard, J.2
  • 42
    • 3042824524 scopus 로고    scopus 로고
    • Free fatty acids promote hepatic lipotoxicity by stimulating TNF-alpha expression via a lysosomal pathway
    • Feldstein A.E., Werneburg N.W., Canbay A., et al. Free fatty acids promote hepatic lipotoxicity by stimulating TNF-alpha expression via a lysosomal pathway. Hepatology (Baltimore, Md) 2004, 40:185-194.
    • (2004) Hepatology (Baltimore, Md) , vol.40 , pp. 185-194
    • Feldstein, A.E.1    Werneburg, N.W.2    Canbay, A.3
  • 44
    • 80053187053 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-converting enzyme inhibition reverses hepatic steatosis and improves insulin sensitivity markers and surgical outcome in mice
    • de Meijer V.E., Le H.D., Meisel J.A., et al. Tumor necrosis factor alpha-converting enzyme inhibition reverses hepatic steatosis and improves insulin sensitivity markers and surgical outcome in mice. PloS One 2011, 6:e25587.
    • (2011) PloS One , vol.6
    • de Meijer, V.E.1    Le, H.D.2    Meisel, J.A.3
  • 45
    • 0345900899 scopus 로고    scopus 로고
    • Paracrine regulation of angiogenesis and adipocyte differentiation during in vivo adipogenesis
    • Fukumura D., Ushiyama A., Duda D.G., et al. Paracrine regulation of angiogenesis and adipocyte differentiation during in vivo adipogenesis. Circulation Research 2003, 93:e88-97.
    • (2003) Circulation Research , vol.93
    • Fukumura, D.1    Ushiyama, A.2    Duda, D.G.3
  • 46
    • 0037393850 scopus 로고    scopus 로고
    • A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2
    • Qi J.H., Ebrahem Q., Moore N., et al. A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2. Nature Medicine 2003, 9:407-415.
    • (2003) Nature Medicine , vol.9 , pp. 407-415
    • Qi, J.H.1    Ebrahem, Q.2    Moore, N.3
  • 47
    • 77955284154 scopus 로고    scopus 로고
    • Ectodomain shedding of EGFR ligands and TNFR1 dictates hepatocyte apoptosis during fulminant hepatitis in mice
    • Murthy A., Defamie V., Smookler D.S., et al. Ectodomain shedding of EGFR ligands and TNFR1 dictates hepatocyte apoptosis during fulminant hepatitis in mice. The Journal of Clinical Investigation 2010, 120:2731-2744.
    • (2010) The Journal of Clinical Investigation , vol.120 , pp. 2731-2744
    • Murthy, A.1    Defamie, V.2    Smookler, D.S.3
  • 48
    • 55449114832 scopus 로고    scopus 로고
    • VEGF-A stimulates ADAM17-dependent shedding of VEGFR2 and crosstalk between VEGFR2 and ERK signaling
    • Swendeman S., Mendelson K., Weskamp G., et al. VEGF-A stimulates ADAM17-dependent shedding of VEGFR2 and crosstalk between VEGFR2 and ERK signaling. Circulation Research 2008, 103:916-918.
    • (2008) Circulation Research , vol.103 , pp. 916-918
    • Swendeman, S.1    Mendelson, K.2    Weskamp, G.3
  • 49
    • 38449086094 scopus 로고    scopus 로고
    • Cutting edge: TNF-alpha-converting enzyme (TACE/ADAM17) inactivation in mouse myeloid cells prevents lethality from endotoxin shock
    • Horiuchi K., Kimura T., Miyamoto T., et al. Cutting edge: TNF-alpha-converting enzyme (TACE/ADAM17) inactivation in mouse myeloid cells prevents lethality from endotoxin shock. Journal of Immunology 2007, 179:2686-2689.
    • (2007) Journal of Immunology , vol.179 , pp. 2686-2689
    • Horiuchi, K.1    Kimura, T.2    Miyamoto, T.3
  • 50
    • 77950889362 scopus 로고    scopus 로고
    • Pathological neovascularization is reduced by inactivation of ADAM17 in endothelial cells but not in pericytes
    • Weskamp G., Mendelson K., Swendeman S., et al. Pathological neovascularization is reduced by inactivation of ADAM17 in endothelial cells but not in pericytes. Circulation Research 2010, 106:932-940.
    • (2010) Circulation Research , vol.106 , pp. 932-940
    • Weskamp, G.1    Mendelson, K.2    Swendeman, S.3
  • 51
    • 33845685599 scopus 로고    scopus 로고
    • Network analysis of human in-stent restenosis
    • Ashley E.A., Ferrara R., King J.Y., et al. Network analysis of human in-stent restenosis. Circulation 2006, 114:2644-2654.
    • (2006) Circulation , vol.114 , pp. 2644-2654
    • Ashley, E.A.1    Ferrara, R.2    King, J.Y.3
  • 52
    • 33744797970 scopus 로고    scopus 로고
    • The TNF alpha converting enzyme (TACE/ADAM17) is expressed in the atherosclerotic lesions of apolipoprotein E-deficient mice: possible contribution to elevated plasma levels of soluble TNF alpha receptors
    • Canault M., Peiretti F., Kopp F., et al. The TNF alpha converting enzyme (TACE/ADAM17) is expressed in the atherosclerotic lesions of apolipoprotein E-deficient mice: possible contribution to elevated plasma levels of soluble TNF alpha receptors. Atherosclerosis 2006, 187:82-91.
    • (2006) Atherosclerosis , vol.187 , pp. 82-91
    • Canault, M.1    Peiretti, F.2    Kopp, F.3
  • 53
    • 36349026433 scopus 로고    scopus 로고
    • Microparticles of human atherosclerotic plaques enhance the shedding of the tumor necrosis factor-alpha converting enzyme/ADAM17 substrates, tumor necrosis factor and tumor necrosis factor receptor-1
    • Canault M., Leroyer A.S., Peiretti F., et al. Microparticles of human atherosclerotic plaques enhance the shedding of the tumor necrosis factor-alpha converting enzyme/ADAM17 substrates, tumor necrosis factor and tumor necrosis factor receptor-1. The American Journal of Pathology 2007, 171:1713-1723.
    • (2007) The American Journal of Pathology , vol.171 , pp. 1713-1723
    • Canault, M.1    Leroyer, A.S.2    Peiretti, F.3
  • 54
    • 78149283545 scopus 로고    scopus 로고
    • A disintegrin and metalloprotease 10 is a novel mediator of vascular endothelial growth factor-induced endothelial cell function in angiogenesis and is associated with atherosclerosis
    • Donners M.M., Wolfs I.M., Olieslagers S., et al. A disintegrin and metalloprotease 10 is a novel mediator of vascular endothelial growth factor-induced endothelial cell function in angiogenesis and is associated with atherosclerosis. Arteriosclerosis, Thrombosis, and Vascular Biology 2010, 30:2188-2195.
    • (2010) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.30 , pp. 2188-2195
    • Donners, M.M.1    Wolfs, I.M.2    Olieslagers, S.3
  • 55
    • 67649713385 scopus 로고    scopus 로고
    • ADAM-9, ADAM-15, and ADAM-17 are upregulated in macrophages in advanced human atherosclerotic plaques in aorta and carotid and femoral arteries-Tampere vascular study
    • Oksala N., Levula M., Airla N., et al. ADAM-9, ADAM-15, and ADAM-17 are upregulated in macrophages in advanced human atherosclerotic plaques in aorta and carotid and femoral arteries-Tampere vascular study. Annals of Medicine 2009, 41:279-290.
    • (2009) Annals of Medicine , vol.41 , pp. 279-290
    • Oksala, N.1    Levula, M.2    Airla, N.3
  • 56
    • 51649101109 scopus 로고    scopus 로고
    • Low tissue inhibitor of metalloproteinases 3 and high matrix metalloproteinase 14 levels defines a subpopulation of highly invasive foam-cell macrophages
    • Johnson J.L., Sala-Newby G.B., Ismail Y., et al. Low tissue inhibitor of metalloproteinases 3 and high matrix metalloproteinase 14 levels defines a subpopulation of highly invasive foam-cell macrophages. Arteriosclerosis, Thrombosis, and Vascular Biology 2008, 28:1647-1653.
    • (2008) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.28 , pp. 1647-1653
    • Johnson, J.L.1    Sala-Newby, G.B.2    Ismail, Y.3
  • 58
    • 84870300659 scopus 로고    scopus 로고
    • Metalloproteinases and advanced glycation end products: coupled navigation in atherosclerotic plaque pathophysiology?
    • Furfaro A.L., Sanguineti R., Storace D., et al. Metalloproteinases and advanced glycation end products: coupled navigation in atherosclerotic plaque pathophysiology?. Experimental and Clinical Endocrinology and Diabetes 2012, 120:586-590.
    • (2012) Experimental and Clinical Endocrinology and Diabetes , vol.120 , pp. 586-590
    • Furfaro, A.L.1    Sanguineti, R.2    Storace, D.3
  • 59
    • 80052735881 scopus 로고    scopus 로고
    • Sustained reduction of vein graft neointima formation by ex vivo TIMP-3 gene therapy
    • George S.J., Wan S., Hu J., et al. Sustained reduction of vein graft neointima formation by ex vivo TIMP-3 gene therapy. Circulation 2011, 124:S135-S142.
    • (2011) Circulation , vol.124
    • George, S.J.1    Wan, S.2    Hu, J.3
  • 60
    • 79960674990 scopus 로고    scopus 로고
    • Unsaturated fatty acids drive disintegrin and metalloproteinase (ADAM)-dependent cell adhesion, proliferation, and migration by modulating membrane fluidity
    • Reiss K., Cornelsen I., Husmann M., et al. Unsaturated fatty acids drive disintegrin and metalloproteinase (ADAM)-dependent cell adhesion, proliferation, and migration by modulating membrane fluidity. The Journal of Biological Chemistry 2011, 286:26931-26942.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 26931-26942
    • Reiss, K.1    Cornelsen, I.2    Husmann, M.3
  • 61
    • 0035908941 scopus 로고    scopus 로고
    • Circulating cell adhesion molecules and death in patients with coronary artery disease
    • Blankenberg S., Rupprecht H.J., Bickel C., et al. Circulating cell adhesion molecules and death in patients with coronary artery disease. Circulation 2001, 104:1336-1342.
    • (2001) Circulation , vol.104 , pp. 1336-1342
    • Blankenberg, S.1    Rupprecht, H.J.2    Bickel, C.3
  • 62
    • 0037072452 scopus 로고    scopus 로고
    • Soluble intercellular adhesion molecule-1, soluble vascular adhesion molecule-1, and the development of symptomatic peripheral arterial disease in men
    • Pradhan A.D., Rifai N., Ridker P.M. Soluble intercellular adhesion molecule-1, soluble vascular adhesion molecule-1, and the development of symptomatic peripheral arterial disease in men. Circulation 2002, 106:820-825.
    • (2002) Circulation , vol.106 , pp. 820-825
    • Pradhan, A.D.1    Rifai, N.2    Ridker, P.M.3
  • 63
    • 33748747486 scopus 로고    scopus 로고
    • Relation between soluble intercellular adhesion molecule-1, statin therapy, and long-term risk of clinical cardiovascular events in patients with previous acute coronary syndrome (from PROVE IT-TIMI 22)
    • Ray K.K., Morrow D.A., Shui A., et al. Relation between soluble intercellular adhesion molecule-1, statin therapy, and long-term risk of clinical cardiovascular events in patients with previous acute coronary syndrome (from PROVE IT-TIMI 22). The American Journal of Cardiology 2006, 98:861-865.
    • (2006) The American Journal of Cardiology , vol.98 , pp. 861-865
    • Ray, K.K.1    Morrow, D.A.2    Shui, A.3
  • 64
    • 77954232611 scopus 로고    scopus 로고
    • Transmembrane TNF-alpha: structure, function and interaction with anti-TNF agents
    • Horiuchi T., Mitoma H., Harashima S., et al. Transmembrane TNF-alpha: structure, function and interaction with anti-TNF agents. Rheumatology (Oxford) 2010, 49:1215-1228.
    • (2010) Rheumatology (Oxford) , vol.49 , pp. 1215-1228
    • Horiuchi, T.1    Mitoma, H.2    Harashima, S.3
  • 65
    • 84863845567 scopus 로고    scopus 로고
    • Anti-tumour effects of a specific anti-ADAM17 antibody in an ovarian cancer model in vivo
    • Richards F.M., Tape C.J., Jodrell D.I., et al. Anti-tumour effects of a specific anti-ADAM17 antibody in an ovarian cancer model in vivo. PloS One 2012, 7:e40597.
    • (2012) PloS One , vol.7
    • Richards, F.M.1    Tape, C.J.2    Jodrell, D.I.3
  • 66
    • 36749087548 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
    • Milne J.C., Lambert P.D., Schenk S., et al. Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature 2007, 450:712-716.
    • (2007) Nature , vol.450 , pp. 712-716
    • Milne, J.C.1    Lambert, P.D.2    Schenk, S.3
  • 67
    • 38749142898 scopus 로고    scopus 로고
    • Clipping, shedding and RIPping keep immunity on cue
    • Murphy G., Murthy A., Khokha R. Clipping, shedding and RIPping keep immunity on cue. Trends in Immunology 2008, 29:75-82.
    • (2008) Trends in Immunology , vol.29 , pp. 75-82
    • Murphy, G.1    Murthy, A.2    Khokha, R.3
  • 68
    • 84869749821 scopus 로고    scopus 로고
    • Mesenchymal stem cells regulate blood-brain barrier integrity through TIMP3 release after traumatic brain injury
    • Menge T., Zhao Y., Zhao J., et al. Mesenchymal stem cells regulate blood-brain barrier integrity through TIMP3 release after traumatic brain injury. Science Translational Medicine 2012, 4:161ra150.
    • (2012) Science Translational Medicine , vol.4
    • Menge, T.1    Zhao, Y.2    Zhao, J.3
  • 69
    • 84876812168 scopus 로고    scopus 로고
    • Loss of TIMP3 underlies diabetic nephropathy via FoxO1/STAT1 interplay
    • Embo Molecular Medicine, in press.
    • Fiorentino L. Loss of TIMP3 underlies diabetic nephropathy via FoxO1/STAT1 interplay. Embo Molecular Medicine, in press.
    • Fiorentino, L.1
  • 70
    • 84868115043 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-3 regulates inflammation in human and mouse intestine
    • e1271-1274
    • Monteleone I., Federici M., Sarra M., et al. Tissue inhibitor of metalloproteinase-3 regulates inflammation in human and mouse intestine. Gastroenterology 2012, 143:1277-1287. e1271-1274.
    • (2012) Gastroenterology , vol.143 , pp. 1277-1287
    • Monteleone, I.1    Federici, M.2    Sarra, M.3


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