메뉴 건너뛰기




Volumn 49, Issue 6, 2013, Pages 875-884

ADAM8 in asthma: Friend or foe to airway inflammation?

Author keywords

A disintegrin and metalloprotease 8 (ADAM8); Adhesion molecules; Airway inflammation; Asthma; Leukocytes recruitment

Indexed keywords

A DISINTEGRIN AND METALLOPROTEASE 8; ADAM PROTEIN; CELL ADHESION MOLECULE; EOTAXIN; INTERLEUKIN 13; INTERLEUKIN 4; L SELECTIN; P SELECTIN GLYCOPROTEIN LIGAND 1; UNCLASSIFIED DRUG; VASCULAR CELL ADHESION MOLECULE 1;

EID: 84890055160     PISSN: 10441549     EISSN: 15354989     Source Type: Journal    
DOI: 10.1165/rcmb.2013-0168TR     Document Type: Review
Times cited : (13)

References (119)
  • 1
    • 0034872296 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of allergic disease
    • Broide DH. Molecular and cellular mechanisms of allergic disease. J Allergy Clin Immunol 2001;108:S65-S71.
    • (2001) J Allergy Clin Immunol , vol.108
    • Broide, D.H.1
  • 2
    • 21744458277 scopus 로고    scopus 로고
    • Modulation of airway inflammation and resistance in mice by a nicotinic receptor agonist
    • Blanchet MR, Israël-Assayag E, Cormier Y. Modulation of airway inflammation and resistance in mice by a nicotinic receptor agonist. Eur Respir J 2005;26:21-27.
    • (2005) Eur Respir J , vol.26 , pp. 21-27
    • Blanchet, M.R.1    Israël-Assayag, E.2    Cormier, Y.3
  • 4
    • 52249093960 scopus 로고    scopus 로고
    • Lung dendritic cells: Targets for therapy in allergic disease
    • Lambrecht BN, Hammad H. Lung dendritic cells: targets for therapy in allergic disease. Chem Immunol Allergy 2008;94:189-200.
    • (2008) Chem Immunol Allergy , vol.94 , pp. 189-200
    • Lambrecht, B.N.1    Hammad, H.2
  • 5
    • 3042838551 scopus 로고    scopus 로고
    • The alveolar macrophage: The forgotten cell in asthma
    • Peters-Golden M. The alveolar macrophage: the forgotten cell in asthma. Am J Respir Cell Mol Biol 2004;31:3-7.
    • (2004) Am J Respir Cell Mol Biol , vol.31 , pp. 3-7
    • Peters-Golden, M.1
  • 6
    • 0034080842 scopus 로고    scopus 로고
    • Airway neutrophils and interleukin-17
    • Lindén A, Hoshino H, Laan M. Airway neutrophils and interleukin-17. Eur Respir J 2000;15:973-977.
    • (2000) Eur Respir J , vol.15 , pp. 973-977
    • Lindén, A.1    Hoshino, H.2    Laan, M.3
  • 8
    • 0031918920 scopus 로고    scopus 로고
    • Interleukin-5-producing CD4+ T cells play a pivotal role in aeroallergen-induced eosinophilia, bronchial hyperreactivity, and lung damage in mice
    • Hogan SP, Koskinen A, Matthaei KI, Young IG, Foster PS. Interleukin-5-producing CD4+ T cells play a pivotal role in aeroallergen-induced eosinophilia, bronchial hyperreactivity, and lung damage in mice. Am J Respir Crit Care Med 1998;157:210-218.
    • (1998) Am J Respir Crit Care Med , vol.157 , pp. 210-218
    • Hogan, S.P.1    Koskinen, A.2    Matthaei, K.I.3    Young, I.G.4    Foster, P.S.5
  • 9
    • 0032750835 scopus 로고    scopus 로고
    • Th2 cells and GATA-3 in asthma: New insights into the regulation of airway inflammation
    • Ray A, Cohn L. Th2 cells and GATA-3 in asthma: new insights into the regulation of airway inflammation. J Clin Invest 1999;104:985-993.
    • (1999) J Clin Invest , vol.104 , pp. 985-993
    • Ray, A.1    Cohn, L.2
  • 11
    • 55849148482 scopus 로고    scopus 로고
    • The cytokine network in asthma and chronic obstructive pulmonary disease
    • Barnes PJ. The cytokine network in asthma and chronic obstructive pulmonary disease. J Clin Invest 2008;118:3546-3556.
    • (2008) J Clin Invest , vol.118 , pp. 3546-3556
    • Barnes, P.J.1
  • 12
    • 0032699213 scopus 로고    scopus 로고
    • IgE in asthma and atopy: Cellular and molecular connections
    • Oettgen HC, Geha RS. IgE in asthma and atopy: cellular and molecular connections. J Clin Invest 1999;104:829-835.
    • (1999) J Clin Invest , vol.104 , pp. 829-835
    • Oettgen, H.C.1    Geha, R.S.2
  • 14
    • 0037336954 scopus 로고    scopus 로고
    • Airway hyperresponsiveness
    • O'Byrne PM, Inman MD. Airway hyperresponsiveness. Chest 2003;123 (3, Suppl) 411S-416S.
    • (2003) Chest , vol.123 , Issue.3 SUPPL.
    • O'Byrne, P.M.1    Inman, M.D.2
  • 16
    • 33749261118 scopus 로고    scopus 로고
    • Airway remodelling in asthma: Current understanding and implications for future therapies
    • Tang ML, Wilson JW, Stewart AG, Royce SG. Airway remodelling in asthma: current understanding and implications for future therapies. Pharmacol Ther 2006;112:474-488.
    • (2006) Pharmacol Ther , vol.112 , pp. 474-488
    • Tang, M.L.1    Wilson, J.W.2    Stewart, A.G.3    Royce, S.G.4
  • 17
    • 23044493210 scopus 로고    scopus 로고
    • Airway smooth muscle tone modulates mechanically induced cytoskeletal stiffening and remodeling
    • Deng L, Fairbank NJ, Cole DJ, Fredberg JJ, Maksym GN. Airway smooth muscle tone modulates mechanically induced cytoskeletal stiffening and remodeling. J Appl Physiol 2005;99:634-641.
    • (2005) J Appl Physiol , vol.99 , pp. 634-641
    • Deng, L.1    Fairbank, N.J.2    Cole, D.J.3    Fredberg, J.J.4    Maksym, G.N.5
  • 18
    • 3242695224 scopus 로고    scopus 로고
    • Localized mechanical stress induces time-dependent actin cytoskeletal remodeling and stiffening in cultured airway smooth muscle cells
    • Deng L, Fairbank NJ, Fabry B, Smith PG, Maksym GN. Localized mechanical stress induces time-dependent actin cytoskeletal remodeling and stiffening in cultured airway smooth muscle cells. Am J Physiol Cell Physiol 2004;287:C440-C448.
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Deng, L.1    Fairbank, N.J.2    Fabry, B.3    Smith, P.G.4    Maksym, G.N.5
  • 20
    • 0026342111 scopus 로고
    • Leukocyte-endothelial cell recognition: Three (or more) steps to specificity and diversity
    • Butcher EC. Leukocyte-endothelial cell recognition: three (or more) steps to specificity and diversity. Cell 1991;67:1033-1036.
    • (1991) Cell , vol.67 , pp. 1033-1036
    • Butcher, E.C.1
  • 21
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer TA. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 1994;76:301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 22
    • 68549130679 scopus 로고    scopus 로고
    • Proteolytic interstitial cell migration: A five-step process
    • Friedl P, Wolf K. Proteolytic interstitial cell migration: a five-step process. Cancer Metastasis Rev 2009;28:129-135.
    • (2009) Cancer Metastasis Rev , vol.28 , pp. 129-135
    • Friedl, P.1    Wolf, K.2
  • 23
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger DA, Horwitz AF. Cell migration: a physically integrated molecular process. Cell 1996;84:359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 24
    • 0033768928 scopus 로고    scopus 로고
    • Cell migration in the immune system: The evolving inter-related roles of adhesion molecules and proteinases
    • Madri JA, Graesser D. Cell migration in the immune system: the evolving inter-related roles of adhesion molecules and proteinases. Dev Immunol 2000;7:103-116.
    • (2000) Dev Immunol , vol.7 , pp. 103-116
    • Madri, J.A.1    Graesser, D.2
  • 32
    • 67349241968 scopus 로고    scopus 로고
    • Upregulation of ADAM8 in the airways of mice with allergic bronchial asthma
    • Chiba Y, Onoda S, Hattori Y, Maitani Y, Sakai H, Misawa M. Upregulation of ADAM8 in the airways of mice with allergic bronchial asthma. Lung 2009;187:179-185.
    • (2009) Lung , vol.187 , pp. 179-185
    • Chiba, Y.1    Onoda, S.2    Hattori, Y.3    Maitani, Y.4    Sakai, H.5    Misawa, M.6
  • 33
    • 0025284795 scopus 로고
    • Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface antigen strongly expressed in murine monocytic lineage
    • Yoshida S, Setoguchi M, Higuchi Y, Akizuki S, Yamamoto S. Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface antigen strongly expressed in murine monocytic lineage. Int Immunol 1990;2:585-591.
    • (1990) Int Immunol , vol.2 , pp. 585-591
    • Yoshida, S.1    Setoguchi, M.2    Higuchi, Y.3    Akizuki, S.4    Yamamoto, S.5
  • 34
    • 0031128165 scopus 로고    scopus 로고
    • CD156 (human ADAM8): Expression, primary amino acid sequence, and gene location
    • Yoshiyama K, Higuchi Y, Kataoka M, Matsuura K, Yamamoto S. CD156 (human ADAM8): expression, primary amino acid sequence, and gene location. Genomics 1997;41:56-62.
    • (1997) Genomics , vol.41 , pp. 56-62
    • Yoshiyama, K.1    Higuchi, Y.2    Kataoka, M.3    Matsuura, K.4    Yamamoto, S.5
  • 35
    • 33846509794 scopus 로고    scopus 로고
    • The detection of ADAM8 protein on cells of the human immune system and the demonstration of its expression on peripheral blood B cells, dendritic cells and monocyte subsets
    • Richens J, Fairclough L, Ghaemmaghami AM, Mahdavi J, Shakib F, Sewell HF. The detection of ADAM8 protein on cells of the human immune system and the demonstration of its expression on peripheral blood B cells, dendritic cells and monocyte subsets. Immunobiology 2007;212:29-38.
    • (2007) Immunobiology , vol.212 , pp. 29-38
    • Richens, J.1    Fairclough, L.2    Ghaemmaghami, A.M.3    Mahdavi, J.4    Shakib, F.5    Sewell, H.F.6
  • 36
    • 0034332481 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha induces a metalloproteasedisintegrin, ADAM8 (CD 156): Implications for neuron-glia interactions during neurodegeneration
    • Schlomann U, Rathke-Hartlieb S, Yamamoto S, Jockusch H, Bartsch JW. Tumor necrosis factor alpha induces a metalloproteasedisintegrin, ADAM8 (CD 156): implications for neuron-glia interactions during neurodegeneration. J Neurosci 2000;20:7964-7971.
    • (2000) J Neurosci , vol.20 , pp. 7964-7971
    • Schlomann, U.1    Rathke-Hartlieb, S.2    Yamamoto, S.3    Jockusch, H.4    Bartsch, J.W.5
  • 38
    • 43049139847 scopus 로고    scopus 로고
    • Leukocyte cell surface proteinases: Regulation of expression, functions, and mechanisms of surface localization
    • Owen CA. Leukocyte cell surface proteinases: regulation of expression, functions, and mechanisms of surface localization. Int J Biochem Cell Biol 2008;40:1246-1272.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1246-1272
    • Owen, C.A.1
  • 40
    • 44349121755 scopus 로고    scopus 로고
    • Regulated expression of ADAM8 (a disintegrin and metalloprotease domain 8) in the mouse ovary: Evidence for a regulatory role of luteinizing hormone, progesterone receptor, and epidermal growth factor-like growth factors
    • Sriraman V, Eichenlaub-Ritter U, Bartsch JW, Rittger A, Mulders SM, Richards JS. Regulated expression of ADAM8 (a disintegrin and metalloprotease domain 8) in the mouse ovary: evidence for a regulatory role of luteinizing hormone, progesterone receptor, and epidermal growth factor-like growth factors. Biol Reprod 2008;78:1038-1048.
    • (2008) Biol Reprod , vol.78 , pp. 1038-1048
    • Sriraman, V.1    Eichenlaub-Ritter, U.2    Bartsch, J.W.3    Rittger, A.4    Mulders, S.M.5    Richards, J.S.6
  • 41
    • 58249084386 scopus 로고    scopus 로고
    • ADAM8 is selectively up-regulated in endothelial cells and is associated with angiogenesis after spinal cord injury in adult mice
    • Mahoney ET, Benton RL, Maddie MA, Whittemore SR, Hagg T. ADAM8 is selectively up-regulated in endothelial cells and is associated with angiogenesis after spinal cord injury in adult mice. J Comp Neurol 2009;512:243-255.
    • (2009) J Comp Neurol , vol.512 , pp. 243-255
    • Mahoney, E.T.1    Benton, R.L.2    Maddie, M.A.3    Whittemore, S.R.4    Hagg, T.5
  • 42
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding
    • Schlöndorff J, Blobel CP. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding. J Cell Sci 1999;112:3603-3617.
    • (1999) J Cell Sci , vol.112 , pp. 3603-3617
    • Schlöndorff, J.1    Blobel, C.P.2
  • 43
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals DF, Courtneidge SA. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 2003;17:7-30.
    • (2003) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 44
    • 0141533033 scopus 로고    scopus 로고
    • ADAMs: Modulators of cell-cell and cell-matrix interactions
    • White JM. ADAMs: modulators of cell-cell and cell-matrix interactions. Curr Opin Cell Biol 2003;15:598-606.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 598-606
    • White, J.M.1
  • 49
    • 0035059212 scopus 로고    scopus 로고
    • ADAM8: A novel osteoclast stimulating factor
    • Choi SJ, Han JH, Roodman GD. ADAM8: a novel osteoclast stimulating factor. J Bone Miner Res 2001;16:814-822.
    • (2001) J Bone Miner Res , vol.16 , pp. 814-822
    • Choi, S.J.1    Han, J.H.2    Roodman, G.D.3
  • 55
    • 0033120966 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases prevents allergen-induced airway inflammation in a murine model of asthma
    • Kumagai K, Ohno I, Okada S, Ohkawara Y, Suzuki K, Shinya T, Nagase H, Iwata K, Shirato K. Inhibition of matrix metalloproteinases prevents allergen-induced airway inflammation in a murine model of asthma. J Immunol 1999;162:4212-4219.
    • (1999) J Immunol , vol.162 , pp. 4212-4219
    • Kumagai, K.1    Ohno, I.2    Okada, S.3    Ohkawara, Y.4    Suzuki, K.5    Shinya, T.6    Nagase, H.7    Iwata, K.8    Shirato, K.9
  • 56
    • 69249132152 scopus 로고    scopus 로고
    • ADAM8/MS2/CD156, an emerging drug target in the treatment of inflammatory and invasive pathologies
    • Koller G, Schlomann U, Golfi P, Ferdous T, Naus S, Bartsch JW. ADAM8/MS2/CD156, an emerging drug target in the treatment of inflammatory and invasive pathologies. Curr Pharm Des 2009;15:2272-2281.
    • (2009) Curr Pharm Des , vol.15 , pp. 2272-2281
    • Koller, G.1    Schlomann, U.2    Golfi, P.3    Ferdous, T.4    Naus, S.5    Bartsch, J.W.6
  • 57
    • 61449142644 scopus 로고    scopus 로고
    • Involvement of a disintegrin and a metalloproteinase 8 (ADAM8) in osteoclastogenesis and pathological bone destruction
    • Ainola M, Li TF, Mandelin J, Hukkanen M, Choi SJ, Salo J, Konttinen YT. Involvement of a disintegrin and a metalloproteinase 8 (ADAM8) in osteoclastogenesis and pathological bone destruction. Ann Rheum Dis 2009;68:427-434.
    • (2009) Ann Rheum Dis , vol.68 , pp. 427-434
    • Ainola, M.1    Li, T.F.2    Mandelin, J.3    Hukkanen, M.4    Choi, S.J.5    Salo, J.6    Konttinen, Y.T.7
  • 59
    • 0034729369 scopus 로고    scopus 로고
    • The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrindependent cell spreading
    • Iba K, Albrechtsen R, Gilpin B, Fröhlich C, Loechel F, Zolkiewska A, Ishiguro K, Kojima T, Liu W, Langford JK, et al. The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrindependent cell spreading. J Cell Biol 2000;149:1143-1156.
    • (2000) J Cell Biol , vol.149 , pp. 1143-1156
    • Iba, K.1    Albrechtsen, R.2    Gilpin, B.3    Fröhlich, C.4    Loechel, F.5    Zolkiewska, A.6    Ishiguro, K.7    Kojima, T.8    Liu, W.9    Langford, J.K.10
  • 60
    • 0037189557 scopus 로고    scopus 로고
    • ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin
    • Gaultier A, Cousin H, Darribère T, Alfandari D. ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin. J Biol Chem 2002;277:23336-23344.
    • (2002) J Biol Chem , vol.277 , pp. 23336-23344
    • Gaultier, A.1    Cousin, H.2    Darribère, T.3    Alfandari, D.4
  • 61
    • 0034672264 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells
    • Kang Q, Cao Y, Zolkiewska A. Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells. Biochem J 2000;352:883-892.
    • (2000) Biochem J , vol.352 , pp. 883-892
    • Kang, Q.1    Cao, Y.2    Zolkiewska, A.3
  • 62
    • 0034608081 scopus 로고    scopus 로고
    • Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion
    • Galliano MF, Huet C, Frygelius J, Polgren A, Wewer UM, Engvall E. Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion. J Biol Chem 2000;275:13933-13939.
    • (2000) J Biol Chem , vol.275 , pp. 13933-13939
    • Galliano, M.F.1    Huet, C.2    Frygelius, J.3    Polgren, A.4    Wewer, U.M.5    Engvall, E.6
  • 64
    • 1942533555 scopus 로고    scopus 로고
    • Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death
    • Naus S, Richter M, Wildeboer D, Moss M, Schachner M, Bartsch JW. Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death. J Biol Chem 2004;279:16083-16090.
    • (2004) J Biol Chem , vol.279 , pp. 16083-16090
    • Naus, S.1    Richter, M.2    Wildeboer, D.3    Moss, M.4    Schachner, M.5    Bartsch, J.W.6
  • 66
    • 33745689524 scopus 로고    scopus 로고
    • Metalloproteinase disintegrins ADAM8 and ADAM19 are highly regulated in human primary brain tumors and their expression levels and activities are associated with invasiveness
    • Wildeboer D, Naus S, Amy Sang QX, Bartsch JW, Pagenstecher A. Metalloproteinase disintegrins ADAM8 and ADAM19 are highly regulated in human primary brain tumors and their expression levels and activities are associated with invasiveness. J Neuropathol Exp Neurol 2006;65:516-527.
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 516-527
    • Wildeboer, D.1    Naus, S.2    Amy Sang, Q.X.3    Bartsch, J.W.4    Pagenstecher, A.5
  • 68
    • 73749084745 scopus 로고    scopus 로고
    • Increased serum ADAM8 concentration in patients with drug-induced eosinophilic pneumonia-ADAM8 expression depends on a the allergen route of entry
    • Matsuno O, Ono E, Ueno T, Takenaka R, Nishitake T, Hiroshige S, Miyazaki E, Kumamoto T, Higuchi Y. Increased serum ADAM8 concentration in patients with drug-induced eosinophilic pneumonia-ADAM8 expression depends on a the allergen route of entry. Respir Med 2010;104:34-39.
    • (2010) Respir Med , vol.104 , pp. 34-39
    • Matsuno, O.1    Ono, E.2    Ueno, T.3    Takenaka, R.4    Nishitake, T.5    Hiroshige, S.6    Miyazaki, E.7    Kumamoto, T.8    Higuchi, Y.9
  • 69
    • 77954242611 scopus 로고    scopus 로고
    • Novel alternatively spliced ADAM8 isoforms contribute to the aggressive bone metastatic phenotype of lung cancer
    • Hernández I, Moreno JL, Zandueta C, Montuenga L, Lecanda F. Novel alternatively spliced ADAM8 isoforms contribute to the aggressive bone metastatic phenotype of lung cancer. Oncogene 2010;29:3758-3769.
    • (2010) Oncogene , vol.29 , pp. 3758-3769
    • Hernández, I.1    Moreno, J.L.2    Zandueta, C.3    Montuenga, L.4    Lecanda, F.5
  • 72
    • 84867886232 scopus 로고    scopus 로고
    • Overexpression of a disintegrin and metalloprotease 8 in human gliomas is implicated in tumor progression and prognosis
    • He S, Ding L, Cao Y, Li G, Deng J, Tu Y, Wang B. Overexpression of a disintegrin and metalloprotease 8 in human gliomas is implicated in tumor progression and prognosis. Med Oncol 2012;29:2032-2037.
    • (2012) Med Oncol , vol.29 , pp. 2032-2037
    • He, S.1    Ding, L.2    Cao, Y.3    Li, G.4    Deng, J.5    Tu, Y.6    Wang, B.7
  • 74
    • 0030850182 scopus 로고    scopus 로고
    • Structure of the murine CD156 gene, characterization of its promoter, and chromosomal location
    • Kataoka M, Yoshiyama K, Matsuura K, Hijiya N, Higuchi Y, Yamamoto S. Structure of the murine CD156 gene, characterization of its promoter, and chromosomal location. J Biol Chem 1997;272:18209-18215.
    • (1997) J Biol Chem , vol.272 , pp. 18209-18215
    • Kataoka, M.1    Yoshiyama, K.2    Matsuura, K.3    Hijiya, N.4    Higuchi, Y.5    Yamamoto, S.6
  • 75
    • 0042666789 scopus 로고    scopus 로고
    • Microarray analysis of peroxisome proliferatoractivated receptor-gamma induced changes in gene expression in macrophages
    • Hodgkinson CP, Ye S. Microarray analysis of peroxisome proliferatoractivated receptor-gamma induced changes in gene expression in macrophages. Biochem Biophys Res Commun 2003;308:505-510.
    • (2003) Biochem Biophys Res Commun , vol.308 , pp. 505-510
    • Hodgkinson, C.P.1    Ye, S.2
  • 76
    • 2942567828 scopus 로고    scopus 로고
    • Therapeutic benefits from targeting of ADAM family members
    • Moss ML, Bartsch JW. Therapeutic benefits from targeting of ADAM family members. Biochemistry 2004;43:7227-7235.
    • (2004) Biochemistry , vol.43 , pp. 7227-7235
    • Moss, M.L.1    Bartsch, J.W.2
  • 78
    • 0042232590 scopus 로고    scopus 로고
    • Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23
    • Fourie AM, Coles F, Moreno V, Karlsson L. Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23. J Biol Chem 2003;278:30469-30477.
    • (2003) J Biol Chem , vol.278 , pp. 30469-30477
    • Fourie, A.M.1    Coles, F.2    Moreno, V.3    Karlsson, L.4
  • 79
    • 67649598621 scopus 로고    scopus 로고
    • ADAM8: A new therapeutic target for asthma
    • Knolle MD, Owen CA. ADAM8: a new therapeutic target for asthma. Expert Opin Ther Targets 2009;13:523-540.
    • (2009) Expert Opin Ther Targets , vol.13 , pp. 523-540
    • Knolle, M.D.1    Owen, C.A.2
  • 80
    • 82255164228 scopus 로고    scopus 로고
    • Regulating inflammation: ADAM8-a new player in the game
    • Zarbock A, Rossaint J. Regulating inflammation: ADAM8-a new player in the game. Eur J Immunol 2011;41:3419-3422.
    • (2011) Eur J Immunol , vol.41 , pp. 3419-3422
    • Zarbock, A.1    Rossaint, J.2
  • 81
    • 0036972233 scopus 로고    scopus 로고
    • CD156 transgenic mice. Different responses between inflammatory types
    • Higuchi Y, Yasui A, Matsuura K, Yamamoto S. CD156 transgenic mice. Different responses between inflammatory types. Pathobiology 2002;70:47-54.
    • (2002) Pathobiology , vol.70 , pp. 47-54
    • Higuchi, Y.1    Yasui, A.2    Matsuura, K.3    Yamamoto, S.4
  • 82
    • 34147105872 scopus 로고    scopus 로고
    • ADAMs in cancer cell proliferation and progression
    • Mochizuki S, Okada Y. ADAMs in cancer cell proliferation and progression. Cancer Sci 2007;98:621-628.
    • (2007) Cancer Sci , vol.98 , pp. 621-628
    • Mochizuki, S.1    Okada, Y.2
  • 83
    • 2942707947 scopus 로고    scopus 로고
    • ADAM gene expression and regulation during human osteoclast formation
    • Verrier S, Hogan A, McKie N, Horton M. ADAM gene expression and regulation during human osteoclast formation. Bone 2004;35:34-46.
    • (2004) Bone , vol.35 , pp. 34-46
    • Verrier, S.1    Hogan, A.2    McKie, N.3    Horton, M.4
  • 84
    • 44349089740 scopus 로고    scopus 로고
    • TNF-alpha-induced up-regulation of intercellular adhesion molecule-1 is regulated by a Rac-ROS-dependent cascade in human airway epithelial cells
    • Kim H, Hwang JS, Woo CH, Kim EY, Kim TH, Cho KJ, Kim JH, Seo JM, Lee SS. TNF-alpha-induced up-regulation of intercellular adhesion molecule-1 is regulated by a Rac-ROS-dependent cascade in human airway epithelial cells. Exp Mol Med 2008;40:167-175.
    • (2008) Exp Mol Med , vol.40 , pp. 167-175
    • Kim, H.1    Hwang, J.S.2    Woo, C.H.3    Kim, E.Y.4    Kim, T.H.5    Cho, K.J.6    Kim, J.H.7    Seo, J.M.8    Lee, S.S.9
  • 85
    • 0042237924 scopus 로고    scopus 로고
    • The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion
    • Hundhausen C, Misztela D, Berkhout TA, Broadway N, Saftig P, Reiss K, Hartmann D, Fahrenholz F, Postina R, Matthews V, et al. The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion. Blood 2003;102:1186-1195.
    • (2003) Blood , vol.102 , pp. 1186-1195
    • Hundhausen, C.1    Misztela, D.2    Berkhout, T.A.3    Broadway, N.4    Saftig, P.5    Reiss, K.6    Hartmann, D.7    Fahrenholz, F.8    Postina, R.9    Matthews, V.10
  • 86
    • 0035976986 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-converting enzyme mediates the inducible cleavage of fractalkine
    • Tsou CL, Haskell CA, Charo IF. Tumor necrosis factor-alpha-converting enzyme mediates the inducible cleavage of fractalkine. J Biol Chem 2001;276:44622-44626.
    • (2001) J Biol Chem , vol.276 , pp. 44622-44626
    • Tsou, C.L.1    Haskell, C.A.2    Charo, I.F.3
  • 87
    • 0032926171 scopus 로고    scopus 로고
    • Stem cell factorinduced airway hyperreactivity in allergic and normal mice
    • Campbell E, Hogaboam C, Lincoln P, Lukacs NW. Stem cell factorinduced airway hyperreactivity in allergic and normal mice. Am J Pathol 1999;154:1259-1265.
    • (1999) Am J Pathol , vol.154 , pp. 1259-1265
    • Campbell, E.1    Hogaboam, C.2    Lincoln, P.3    Lukacs, N.W.4
  • 94
    • 0035030551 scopus 로고    scopus 로고
    • L-selectin and intercellular adhesion molecule 1 mediate lymphocyte migration to the inflamed airway/lung during an allergic inflammatory response in an animal model of asthma
    • Keramidaris E, Merson TD, Steeber DA, Tedder TF, Tang ML. L-selectin and intercellular adhesion molecule 1 mediate lymphocyte migration to the inflamed airway/lung during an allergic inflammatory response in an animal model of asthma. J Allergy Clin Immunol 2001;107:734-738.
    • (2001) J Allergy Clin Immunol , vol.107 , pp. 734-738
    • Keramidaris, E.1    Merson, T.D.2    Steeber, D.A.3    Tedder, T.F.4    Tang, M.L.5
  • 95
    • 24044469049 scopus 로고    scopus 로고
    • L-selectin: Mechanisms and physiological significance of ectodomain cleavage
    • Smalley DM, Ley K. L-selectin: mechanisms and physiological significance of ectodomain cleavage. J Cell Mol Med 2005;9:255-266.
    • (2005) J Cell Mol Med , vol.9 , pp. 255-266
    • Smalley, D.M.1    Ley, K.2
  • 98
    • 33748879109 scopus 로고    scopus 로고
    • Adenovirus expressing interleukin-1 receptor antagonist alleviates allergic airway inflammation in a murine model of asthma
    • Wang CC, Fu CL, Yang YH, Lo YC, Wang LC, Chuang YH, Chang DM, Chiang BL. Adenovirus expressing interleukin-1 receptor antagonist alleviates allergic airway inflammation in a murine model of asthma. Gene Ther 2006;13:1414-1421.
    • (2006) Gene Ther , vol.13 , pp. 1414-1421
    • Wang, C.C.1    Fu, C.L.2    Yang, Y.H.3    Lo, Y.C.4    Wang, L.C.5    Chuang, Y.H.6    Chang, D.M.7    Chiang, B.L.8
  • 99
    • 0031572518 scopus 로고    scopus 로고
    • Cell type-specific glycoforms of Fc gamma RIIIa (CD16): Differential ligand binding
    • Edberg JC, Kimberly RP. Cell type-specific glycoforms of Fc gamma RIIIa (CD16): differential ligand binding. J Immunol 1997;159:3849-3857.
    • (1997) J Immunol , vol.159 , pp. 3849-3857
    • Edberg, J.C.1    Kimberly, R.P.2
  • 101
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe DJ. Folding proteins in fatal ways. Nature 2003;426:900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 102
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White SH, Wimley WC. Membrane protein folding and stability: physical principles. Annu Rev Biophys Biomol Struct 1999;28:319-365.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 103
    • 36849015809 scopus 로고    scopus 로고
    • Crystal structure of RVV-X: An example of evolutionary gain of specificity by ADAM proteinases
    • Takeda S, Igarashi T, Mori H. Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases. FEBS Lett 2007;581:5859-5864.
    • (2007) FEBS Lett , vol.581 , pp. 5859-5864
    • Takeda, S.1    Igarashi, T.2    Mori, H.3
  • 104
    • 17444373968 scopus 로고    scopus 로고
    • A metalloproteasedisintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor
    • Izumi Y, Hirata M, Hasuwa H, Iwamoto R, Umata T, Miyado K, Tamai Y, Kurisaki T, Sehara-Fujisawa A, Ohno S, et al. A metalloproteasedisintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J 1998;17:7260-7272.
    • (1998) EMBO J , vol.17 , pp. 7260-7272
    • Izumi, Y.1    Hirata, M.2    Hasuwa, H.3    Iwamoto, R.4    Umata, T.5    Miyado, K.6    Tamai, Y.7    Kurisaki, T.8    Sehara-Fujisawa, A.9    Ohno, S.10
  • 106
    • 34247198835 scopus 로고    scopus 로고
    • Shedding of the p75NTR neurotrophin receptor is modulated by lipid rafts
    • Gil C, Cubí R, Aguilera J. Shedding of the p75NTR neurotrophin receptor is modulated by lipid rafts. FEBS Lett 2007;581:1851-1858.
    • (2007) FEBS Lett , vol.581 , pp. 1851-1858
    • Gil, C.1    Cubí, R.2    Aguilera, J.3
  • 107
    • 78751479184 scopus 로고    scopus 로고
    • Low cholesterol triggers membrane microdomain-dependent CD44 shedding and suppresses tumor cell migration
    • Murai T, Maruyama Y, Mio K, Nishiyama H, Suga M, Sato C. Low cholesterol triggers membrane microdomain-dependent CD44 shedding and suppresses tumor cell migration. J Biol Chem 2011;286:1999-2007.
    • (2011) J Biol Chem , vol.286 , pp. 1999-2007
    • Murai, T.1    Maruyama, Y.2    Mio, K.3    Nishiyama, H.4    Suga, M.5    Sato, C.6
  • 111
    • 74849084373 scopus 로고    scopus 로고
    • Airway structural components drive airway smooth muscle remodeling in asthma
    • Dekkers BG, Maarsingh H, Meurs H, Gosens R. Airway structural components drive airway smooth muscle remodeling in asthma. Proc Am Thorac Soc 2009;6:683-692.
    • (2009) Proc Am Thorac Soc , vol.6 , pp. 683-692
    • Dekkers, B.G.1    Maarsingh, H.2    Meurs, H.3    Gosens, R.4
  • 112
  • 113
    • 84863275752 scopus 로고    scopus 로고
    • Differential effects of extracellular matrix and mechanical strain on airway smooth muscle cells from ovalbumin-vs. Salinechallenged Brown Norway rats
    • Pasternyk SM, D'Antoni ML, Venkatesan N, Siddiqui S, Martin JG, Ludwig MS. Differential effects of extracellular matrix and mechanical strain on airway smooth muscle cells from ovalbumin-vs. salinechallenged Brown Norway rats. Respir Physiol Neurobiol 2012;181:36-43.
    • (2012) Respir Physiol Neurobiol , vol.181 , pp. 36-43
    • Pasternyk, S.M.1    D'Antoni, M.L.2    Venkatesan, N.3    Siddiqui, S.4    Martin, J.G.5    Ludwig, M.S.6
  • 115
    • 34848855175 scopus 로고    scopus 로고
    • Inhibition of airway smooth muscle adhesion and migration by the disintegrin domain of ADAM-15
    • Lu D, Xie S, Sukkar MB, Lu X, Scully MF, Chung KF. Inhibition of airway smooth muscle adhesion and migration by the disintegrin domain of ADAM-15. Am J Respir Cell Mol Biol 2007;37:494-500.
    • (2007) Am J Respir Cell Mol Biol , vol.37 , pp. 494-500
    • Lu, D.1    Xie, S.2    Sukkar, M.B.3    Lu, X.4    Scully, M.F.5    Chung, K.F.6
  • 116
    • 26244444813 scopus 로고    scopus 로고
    • Selective modulation of integrinmediated cell migration by distinct ADAM family members
    • Huang J, Bridges LC, White JM. Selective modulation of integrinmediated cell migration by distinct ADAM family members. Mol Biol Cell 2005;16:4982-4991.
    • (2005) Mol Biol Cell , vol.16 , pp. 4982-4991
    • Huang, J.1    Bridges, L.C.2    White, J.M.3
  • 117
    • 0035878794 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin ADAM 12 interacts with alpha-actinin-1
    • Cao Y, Kang Q, Zolkiewska A. Metalloprotease-disintegrin ADAM 12 interacts with alpha-actinin-1. Biochem J 2001;357:353-361.
    • (2001) Biochem J , vol.357 , pp. 353-361
    • Cao, Y.1    Kang, Q.2    Zolkiewska, A.3
  • 118
    • 70449701458 scopus 로고    scopus 로고
    • ADAM12 localizes with c-Src to actin-rich structures at the cell periphery and regulates Src kinase activity
    • Stautz D, Sanjay A, Hansen MT, Albrechtsen R, Wewer UM, Kveiborg M. ADAM12 localizes with c-Src to actin-rich structures at the cell periphery and regulates Src kinase activity. Exp Cell Res 2010;316:55-67.
    • (2010) Exp Cell Res , vol.316 , pp. 55-67
    • Stautz, D.1    Sanjay, A.2    Hansen, M.T.3    Albrechtsen, R.4    Wewer, U.M.5    Kveiborg, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.