메뉴 건너뛰기




Volumn 90, Issue 3, 2006, Pages 185-196

Relevance of tenascin-C and matrix metalloproteinases in vascular abnormalities in murine hypoplastic lungs

Author keywords

Angiogenesis; Lung development; Zymography

Indexed keywords

GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE; TENASCIN; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TISSUE INHIBITOR OF METALLOPROTEINASE 4;

EID: 33748907717     PISSN: 00063126     EISSN: None     Source Type: Journal    
DOI: 10.1159/000093308     Document Type: Article
Times cited : (8)

References (27)
  • 1
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner JF Jr: Matrix metalloproteinases. J Biol Chem 1999;274:21491-21494.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner Jr., J.F.2
  • 2
    • 0036786987 scopus 로고    scopus 로고
    • S-nitrosothiols inhibit cytokine-mediated induction of matrix metalloproteinase-9 in airway epithelial cells
    • Okamoto T, Valacchi G, Gohil K, Akaike A, van der Vliet A: S-nitrosothiols inhibit cytokine-mediated induction of matrix metalloproteinase-9 in airway epithelial cells. Am J Respir Cell Mol Biol 2002;27:463-473.
    • (2002) Am J Respir Cell Mol Biol , vol.27 , pp. 463-473
    • Okamoto, T.1    Valacchi, G.2    Gohil, K.3    Akaike, A.4    Van Der Vliet, A.5
  • 3
    • 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 1990;87:5578-5582.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 4
    • 0035254648 scopus 로고    scopus 로고
    • Angiogenesis: Regulators and clinical applications
    • Liekens S, De Clercq E, Neyts J: Angiogenesis: regulators and clinical applications. Biochem Pharmacol 2000;61:253-270.
    • (2000) Biochem Pharmacol , vol.61 , pp. 253-270
    • Liekens, S.1    De Clercq, E.2    Neyts, J.3
  • 5
    • 0034117025 scopus 로고    scopus 로고
    • The tenascin family of ECM glycoproteins: Structure, function, and regulation during embryonic development and tissue remodeling
    • Jones FS, Jones PL: The tenascin family of ECM glycoproteins: structure, function, and regulation during embryonic development and tissue remodeling. Dev Dyn 2000;218:235-259.
    • (2000) Dev Dyn , vol.218 , pp. 235-259
    • Jones, F.S.1    Jones, P.L.2
  • 6
    • 0024454215 scopus 로고
    • Stimulation of tenascin expression in mesenchyme by epithelial- mesenchymal interactions
    • Ekblom P, Aufderheide E: Stimulation of tenascin expression in mesenchyme by epithelial-mesenchymal interactions. Int J Dev Biol 1989;33:71-79.
    • (1989) Int J Dev Biol , vol.33 , pp. 71-79
    • Ekblom, P.1    Aufderheide, E.2
  • 7
    • 0032844899 scopus 로고    scopus 로고
    • The fibrinogen globe of tenascin-C promotes basic fibroblast growth factor-induced endothelial cell elongation
    • Schenk S, Chiquet-Ehrismann R, Battegay EJ: The fibrinogen globe of tenascin-C promotes basic fibroblast growth factor-induced endothelial cell elongation. Mol Biol Cell 1999;10:2933-2943.
    • (1999) Mol Biol Cell , vol.10 , pp. 2933-2943
    • Schenk, S.1    Chiquet-Ehrismann, R.2    Battegay, E.J.3
  • 8
    • 0034902894 scopus 로고    scopus 로고
    • Down-regulation of regulatory proteins for differentiation and proliferation in murine fetal hypoplastic lungs: Altered mesenchymal-epithelial interactions
    • Chinoy MR, Chi X, Cilley RE: Down-regulation of regulatory proteins for differentiation and proliferation in murine fetal hypoplastic lungs: altered mesenchymal-epithelial interactions. Pediatr Pulmonol 2001;32:129-141.
    • (2001) Pediatr Pulmonol , vol.32 , pp. 129-141
    • Chinoy, M.R.1    Chi, X.2    Cilley, R.E.3
  • 9
    • 0036375902 scopus 로고    scopus 로고
    • Pulmonary hypoplasia and congenital diaphragmatic hernia: Advances in the pathogenetics and regulation of lung development
    • Chinoy MR: Pulmonary hypoplasia and congenital diaphragmatic hernia: advances in the pathogenetics and regulation of lung development. J Surg Res 2002;106:209-223.
    • (2002) J Surg Res , vol.106 , pp. 209-223
    • Chinoy, M.R.1
  • 10
    • 0012142487 scopus 로고    scopus 로고
    • Lung growth and development. A review article
    • Chinoy MR: Lung growth and development. A review article. Front Biosci 2003;8:392-415.
    • (2003) Front Biosci , vol.8 , pp. 392-415
    • Chinoy, M.R.1
  • 11
  • 12
    • 0037084399 scopus 로고    scopus 로고
    • Signaling through the EGF receptor controls lung morphogenesis in part by regulating MT1-MMP-mediated activation of gelatinase A/MMP2
    • Kheradmand F, Rishi K, Werb Z: Signaling through the EGF receptor controls lung morphogenesis in part by regulating MT1-MMP-mediated activation of gelatinase A/MMP2. J Cell Sci 2002;115:839-848.
    • (2002) J Cell Sci , vol.115 , pp. 839-848
    • Kheradmand, F.1    Rishi, K.2    Werb, Z.3
  • 13
    • 0031024924 scopus 로고    scopus 로고
    • Quantitative reverse zymography: Analysis of picogram amounts of metalloproteinase inhibitors using gelatinase A and B reverse zymograms
    • Oliver GW, Leferson JD, Stetler-Stevenson WG, Kleiner DE: Quantitative reverse zymography: analysis of picogram amounts of metalloproteinase inhibitors using gelatinase A and B reverse zymograms. Anal Biochem 1997;244:161-166.
    • (1997) Anal Biochem , vol.244 , pp. 161-166
    • Oliver, G.W.1    Leferson, J.D.2    Stetler-Stevenson, W.G.3    Kleiner, D.E.4
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0021918104 scopus 로고
    • Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase
    • Hibbs MS, Hasty KA, Seyer JM, Kang AH, Mainardi CL: Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J Bio Chem 1985;260:2493-2500.
    • (1985) J Bio Chem , vol.260 , pp. 2493-2500
    • Hibbs, M.S.1    Hasty, K.A.2    Seyer, J.M.3    Kang, A.H.4    Mainardi, C.L.5
  • 18
    • 0031241538 scopus 로고    scopus 로고
    • Molecules in focus: Tenascin-C
    • Mackie EJ: Molecules in focus: tenascin-C. Int J Biochem Cell Biol 1997;29:1133-1137.
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 1133-1137
    • Mackie, E.J.1
  • 19
    • 0033612184 scopus 로고    scopus 로고
    • Regression of hypertrophied rat pulmonary arteries in organ culture is associated with suppression of proteolytic activity, inhibition of tenascin-C, and smooth muscle cell apoptosis
    • Cowan KN, Jones PL, Rabinovitch M: Regression of hypertrophied rat pulmonary arteries in organ culture is associated with suppression of proteolytic activity, inhibition of tenascin-C, and smooth muscle cell apoptosis. Circ Res 1999;84:1223-1233.
    • (1999) Circ Res , vol.84 , pp. 1223-1233
    • Cowan, K.N.1    Jones, P.L.2    Rabinovitch, M.3
  • 20
    • 0030860609 scopus 로고    scopus 로고
    • Regulation of tenascin-C, a vascular smooth muscle cell survival factor that interacts with the alpha v beta 3 integrin to promote epidermal growth factor receptor phosphorylation and growth
    • Jones PL, Crack J, Rabinovitch M: Regulation of tenascin-C, a vascular smooth muscle cell survival factor that interacts with the alpha v beta 3 integrin to promote epidermal growth factor receptor phosphorylation and growth. J Cell Biol 1997;139:279-293.
    • (1997) J Cell Biol , vol.139 , pp. 279-293
    • Jones, P.L.1    Crack, J.2    Rabinovitch, M.3
  • 21
    • 0010712792 scopus 로고    scopus 로고
    • Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity
    • Brooks PC, Silletti S, von Schalscha TL, Friedlander M, Cheresh DA: Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity. Cell 1998;92:391-400.
    • (1998) Cell , vol.92 , pp. 391-400
    • Brooks, P.C.1    Silletti, S.2    Von Schalscha, T.L.3    Friedlander, M.4    Cheresh, D.A.5
  • 22
    • 0033989282 scopus 로고    scopus 로고
    • Elastase and matrix metalloproteinase inhibitors induce regression, and tenascin-C antisense prevents progression of vascular disease
    • Cowan KN, Jones PL, Rabinovitch M: Elastase and matrix metalloproteinase inhibitors induce regression, and tenascin-C antisense prevents progression of vascular disease. J Clin Invest 2000;105:21-34.
    • (2000) J Clin Invest , vol.105 , pp. 21-34
    • Cowan, K.N.1    Jones, P.L.2    Rabinovitch, M.3
  • 23
    • 0030764771 scopus 로고    scopus 로고
    • Matrix metalloproteinases MMP2 and MMP9 are produced in early stages of kidney morphogenesis but only MMP9 is required for renal organogenesis in vitro
    • Lelongt B, Trugnan G, Murphy G, Ronco PM: Matrix metalloproteinases MMP2 and MMP9 are produced in early stages of kidney morphogenesis but only MMP9 is required for renal organogenesis in vitro. J Cell Biol 1997;136:1363-1373.
    • (1997) J Cell Biol , vol.136 , pp. 1363-1373
    • Lelongt, B.1    Trugnan, G.2    Murphy, G.3    Ronco, P.M.4
  • 24
    • 0030717692 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions
    • Gomez DE, Alonso DF, Yoshiji H, Thorgeirsson UP: Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol 1997;74:11-122.
    • (1997) Eur J Cell Biol , vol.74 , pp. 11-122
    • Gomez, D.E.1    Alonso, D.F.2    Yoshiji, H.3    Thorgeirsson, U.P.4
  • 26
    • 0032160033 scopus 로고    scopus 로고
    • Complex role of matrix metalloproteinases in angiogenesis
    • Sang QX: Complex role of matrix metalloproteinases in angiogenesis. Cell Res 1998;8:171-177.
    • (1998) Cell Res , vol.8 , pp. 171-177
    • Sang, Q.X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.