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Volumn 1455, Issue 1, 1999, Pages 12-22

Induction of TIMP-1 expression in rat hepatic stellate cells and hepatocytes: A new role for homocysteine in liver fibrosis

Author keywords

Extracellular matrix; Fibrosis; Hyperhomocysteinemia; Liver; Risk factor

Indexed keywords

COMPLEMENTARY DNA; HOMOCYSTEINE; MESSENGER RNA; METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1;

EID: 0345035265     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0925-4439(99)00049-6     Document Type: Article
Times cited : (71)

References (56)
  • 2
    • 0000167774 scopus 로고
    • Disorders of transsulfuration
    • in: C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.) McGraw-Hill, New York
    • S.H. Mudd, H.L. Levy, F. Skovby, Disorders of transsulfuration, in: C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.), The Metabolic and Molecular Basis of Inherited Disease, McGraw-Hill, New York, 1995, pp. 693-734.
    • (1995) The Metabolic and Molecular Basis of Inherited Disease , pp. 693-734
    • Mudd, S.H.1    Levy, H.L.2    Skovby, F.3
  • 3
    • 0027382008 scopus 로고
    • Vitamin status and intake as primary determinants of homocysteinemia in an elderly populations
    • Selhub J., Jacques P.F., Wilson P.W., Rush D., Rosenberg I.H. Vitamin status and intake as primary determinants of homocysteinemia in an elderly populations. J. Am. Med. Assoc. 270:1993;2693-2698.
    • (1993) J. Am. Med. Assoc. , vol.270 , pp. 2693-2698
    • Selhub, J.1    Jacques, P.F.2    Wilson, P.W.3    Rush, D.4    Rosenberg, I.H.5
  • 4
    • 0029120110 scopus 로고
    • Carbon tetrachloride-induced hepatic injury is associated with global DNA hypomethylation and homocysteinemia. Effect of S-adenosylmethionine treatment
    • Varela-Moreiras G., Alonso-Aperte E., Rubio M., Gasso M., Deulofeu R., Alvarez L., Caballeria J., Rodes J., Mato J.M. Carbon tetrachloride-induced hepatic injury is associated with global DNA hypomethylation and homocysteinemia. Effect of S-adenosylmethionine treatment. Hepatology. 22:1995;1310-1315.
    • (1995) Hepatology , vol.22 , pp. 1310-1315
    • Varela-Moreiras, G.1    Alonso-Aperte, E.2    Rubio, M.3    Gasso, M.4    Deulofeu, R.5    Alvarez, L.6    Caballeria, J.7    Rodes, J.8    Mato, J.M.9
  • 8
    • 0021220516 scopus 로고
    • Methionine metabolism in mammals: Distribution of homocysteine between competitive pathways
    • Finkelstein J.D., Martin J.J. Methionine metabolism in mammals: distribution of homocysteine between competitive pathways. J. Biol. Chem. 259:1984;9508-9513.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9508-9513
    • Finkelstein, J.D.1    Martin, J.J.2
  • 9
    • 0031748093 scopus 로고    scopus 로고
    • The metabolism of homocysteine: Pathways and regulation
    • Finkelstein J.D. The metabolism of homocysteine: pathways and regulation. Eur. J. Pediatr. 157:1998;S40-S44.
    • (1998) Eur. J. Pediatr. , vol.157
    • Finkelstein, J.D.1
  • 10
    • 0027531427 scopus 로고
    • Adverse vascular effects of homocysteine are modulated by endothelium-derived relaxing factor and related oxides of nitrogen
    • Stamler J.S., Osborne J.A., Jakaki O., Rabbani L.E., Mullins M., Singel D., Loscalzo J. Adverse vascular effects of homocysteine are modulated by endothelium-derived relaxing factor and related oxides of nitrogen. J. Clin. Invest. 91:1993;308-318.
    • (1993) J. Clin. Invest. , vol.91 , pp. 308-318
    • Stamler, J.S.1    Osborne, J.A.2    Jakaki, O.3    Rabbani, L.E.4    Mullins, M.5    Singel, D.6    Loscalzo, J.7
  • 11
    • 0030610779 scopus 로고    scopus 로고
    • Homocysteine and vascular disfunction
    • Lentz S.R. Homocysteine and vascular disfunction. Life Sci. 61:1997;1205-1215.
    • (1997) Life Sci. , vol.61 , pp. 1205-1215
    • Lentz, S.R.1
  • 14
    • 17344368557 scopus 로고    scopus 로고
    • Homocysteine as a risk factor for vascular disease. Enhanced collagen production and accumulation by smooth muscle cells
    • Majors A., Ehrhart L.A., Pezacka E.H. Homocysteine as a risk factor for vascular disease. Enhanced collagen production and accumulation by smooth muscle cells. Arterioscler. Thromb. Vasc. Biol. 17:1997;2074-2081.
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 2074-2081
    • Majors, A.1    Ehrhart, L.A.2    Pezacka, E.H.3
  • 15
    • 0031935068 scopus 로고    scopus 로고
    • Homocysteine redox receptor and regulation of extracellular matrix components in vascular cells
    • Tyagi S.C. Homocysteine redox receptor and regulation of extracellular matrix components in vascular cells. Am. J. Physiol. 274:1998;C396-C405.
    • (1998) Am. J. Physiol. , vol.274
    • Tyagi, S.C.1
  • 17
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woesner J.F. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5:1991;2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woesner, J.F.1
  • 18
    • 0029024766 scopus 로고
    • Collagenases and liver fibrosis
    • Arthur M.J.P. Collagenases and liver fibrosis. J. Hepatol. 22:1995;43-48.
    • (1995) J. Hepatol. , vol.22 , pp. 43-48
    • Arthur, M.J.P.1
  • 20
    • 0030030039 scopus 로고    scopus 로고
    • Expression of tissue inhibitor of metalloproteinases 1 and 2 is increased in fibrotic human liver
    • Benyon R.C., Iredale J.P., Goddard S., Winwood P.J., Arthur M.J.P. Expression of tissue inhibitor of metalloproteinases 1 and 2 is increased in fibrotic human liver. Gastroenterology. 110:1996;821-831.
    • (1996) Gastroenterology , vol.110 , pp. 821-831
    • Benyon, R.C.1    Iredale, J.P.2    Goddard, S.3    Winwood, P.J.4    Arthur, M.J.P.5
  • 21
    • 0029888478 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 messenger RNA expression is enhanced relative to interstitial collagenase messenger RNA in experimental liver injury and fibrosis
    • Iredale J.P., Benyon C., Arthur M.J.P., Ferris W.F., Alcolado R., Winwood P.J., Clark N., Murphy G. Tissue inhibitor of metalloproteinase-1 messenger RNA expression is enhanced relative to interstitial collagenase messenger RNA in experimental liver injury and fibrosis. Hepatology. 24:1996;176-184.
    • (1996) Hepatology , vol.24 , pp. 176-184
    • Iredale, J.P.1    Benyon, C.2    Arthur, M.J.P.3    Ferris, W.F.4    Alcolado, R.5    Winwood, P.J.6    Clark, N.7    Murphy, G.8
  • 23
    • 0027251069 scopus 로고
    • 4-cirrhotic rats are heterogeneous with regard to proliferation, expression of extracellular matrix components, interleukin-6 and connexin 43
    • 4-cirrhotic rats are heterogeneous with regard to proliferation, expression of extracellular matrix components, interleukin-6 and connexin 43. Lab. Invest. 69:1993;210-216.
    • (1993) Lab. Invest. , vol.69 , pp. 210-216
    • Greenwel, P.1    Rubin, J.2    Schwarzt, M.3    Hertzberg, E.L.4    Rojkind, M.5
  • 25
    • 0031915443 scopus 로고    scopus 로고
    • Regulation by hypoxia of methionine adenosyltransferase activity and gene expression in rat hepatocytes
    • Avila M.A., Carretero M.V., Rodriguez E.N., Mato J.M. Regulation by hypoxia of methionine adenosyltransferase activity and gene expression in rat hepatocytes. Gastroenterology. 114:1998;364-371.
    • (1998) Gastroenterology , vol.114 , pp. 364-371
    • Avila, M.A.1    Carretero, M.V.2    Rodriguez, E.N.3    Mato, J.M.4
  • 26
    • 0031408980 scopus 로고    scopus 로고
    • Altered processing of precursor transcripts and increased levels of the subunit I of mitochondrial cytochrome c oxidase in syrian hamster fetal cells initiated with ionizing radiation
    • Otero G., Avila M.A., de la Peña L., Emfietzoglou D., Cansado J., Popescu G.F., Notario V. Altered processing of precursor transcripts and increased levels of the subunit I of mitochondrial cytochrome c oxidase in syrian hamster fetal cells initiated with ionizing radiation. Carcinogenesis. 18:1997;1569-1575.
    • (1997) Carcinogenesis , vol.18 , pp. 1569-1575
    • Otero, G.1    Avila, M.A.2    De La Peña, L.3    Emfietzoglou, D.4    Cansado, J.5    Popescu, G.F.6    Notario, V.7
  • 27
    • 0026674886 scopus 로고
    • Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction
    • Liang P., Pardee A.B. Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction. Science. 257:1992;967-971.
    • (1992) Science , vol.257 , pp. 967-971
    • Liang, P.1    Pardee, A.B.2
  • 30
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson W.R., Lipmann D.J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:1988;2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipmann, D.J.2
  • 31
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 32
    • 0019061278 scopus 로고
    • Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose
    • Thomas P.S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. USA. 77:1980;5201-5205.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5201-5205
    • Thomas, P.S.1
  • 33
    • 0021731952 scopus 로고
    • Construction of DNA squences complementary to rat alpha 1 and alpha 2 collagen mRNA and their use in studying the regulation of type I collagen synthesis by 1,25-dihydroxyvitamin D
    • Genovese G., Rowe D., Kream B. Construction of DNA squences complementary to rat alpha 1 and alpha 2 collagen mRNA and their use in studying the regulation of type I collagen synthesis by 1,25-dihydroxyvitamin D. Biochemistry. 23:1984;6210-6216.
    • (1984) Biochemistry , vol.23 , pp. 6210-6216
    • Genovese, G.1    Rowe, D.2    Kream, B.3
  • 34
    • 0024380087 scopus 로고
    • Rapid detection of octamers binding proteins with miniextracts prepared from a small number of cells
    • Schreiber E., Matthias P., Muller M.M., Schaffner W. Rapid detection of octamers binding proteins with miniextracts prepared from a small number of cells. Nucleic Acids Res. 17:1989;6419.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 35
    • 0022382006 scopus 로고
    • Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity
    • Docherty A.J.P., Lyons A., Smith B.J., Wright E.M., Stephens P.E., Harris T.J.R. Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity. Nature. 318:1985;66-69.
    • (1985) Nature , vol.318 , pp. 66-69
    • Docherty, A.J.P.1    Lyons, A.2    Smith, B.J.3    Wright, E.M.4    Stephens, P.E.5    Harris, T.J.R.6
  • 36
    • 0024534977 scopus 로고
    • Independent regulation of collagenase72 KD progelatinase, and metalloendoproteinase inhibitor expression in human fibroblast by transforming growth factor-β
    • Overall C.M., Wrana J.L., Sudek J. Independent regulation of collagenase72 KD progelatinase, and metalloendoproteinase inhibitor expression in human fibroblast by transforming growth factor-β J. Biol. Chem. 264:1989;1860-1869.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1860-1869
    • Overall, C.M.1    Wrana, J.L.2    Sudek, J.3
  • 37
    • 2442724379 scopus 로고
    • Transforming growth factor beta modulates expression of collagenase and metalloproteinase inhibitor
    • Edwards D.R., Murphy G., Reynolds J.J., Whitham S.E., Docherty A.J., Angel P., Heath J.K. Transforming growth factor beta modulates expression of collagenase and metalloproteinase inhibitor. EMBO J. 6:1987;1899-1904.
    • (1987) EMBO J. , vol.6 , pp. 1899-1904
    • Edwards, D.R.1    Murphy, G.2    Reynolds, J.J.3    Whitham, S.E.4    Docherty, A.J.5    Angel, P.6    Heath, J.K.7
  • 38
    • 33746521801 scopus 로고
    • The cellular basis of hepatic fibrosis
    • Friedman S.L. The cellular basis of hepatic fibrosis. New Engl. J. Med. 328:1993;1828-1835.
    • (1993) New Engl. J. Med. , vol.328 , pp. 1828-1835
    • Friedman, S.L.1
  • 40
    • 0030741845 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 in the liver of patients with chronic liver disease
    • Murawaki Y., Ikuta Y., Idobe Y., Kitamura Y., Kawasaki H. Tissue inhibitor of metalloproteinase-1 in the liver of patients with chronic liver disease. J. Hepatol. 26:1997;1213-1219.
    • (1997) J. Hepatol. , vol.26 , pp. 1213-1219
    • Murawaki, Y.1    Ikuta, Y.2    Idobe, Y.3    Kitamura, Y.4    Kawasaki, H.5
  • 41
    • 0027375854 scopus 로고
    • Regulation of tissue inhibitor of metalloproteinases-1 gene expression by cytokines and dexametasone in rat hepatocytes primary cultures
    • Roeb E., Graeve L., Hoffmann R., Decker K., Edwards D.R., Heinrich P.C. Regulation of tissue inhibitor of metalloproteinases-1 gene expression by cytokines and dexametasone in rat hepatocytes primary cultures. Hepatology. 18:1993;1437-1442.
    • (1993) Hepatology , vol.18 , pp. 1437-1442
    • Roeb, E.1    Graeve, L.2    Hoffmann, R.3    Decker, K.4    Edwards, D.R.5    Heinrich, P.C.6
  • 43
    • 0030021433 scopus 로고    scopus 로고
    • Synergistic transcriptional activation of the tissue inhibitor of metalloproteinases-1 promoter via functional interaction of AP-1 and Ets-1 transcription factors
    • Logan S.K., Garabedian M.J., Campbell C.E., Werb Z. Synergistic transcriptional activation of the tissue inhibitor of metalloproteinases-1 promoter via functional interaction of AP-1 and Ets-1 transcription factors. J. Biol. Chem. 271:1996;774-782.
    • (1996) J. Biol. Chem. , vol.271 , pp. 774-782
    • Logan, S.K.1    Garabedian, M.J.2    Campbell, C.E.3    Werb, Z.4
  • 44
    • 0032570573 scopus 로고    scopus 로고
    • Oncostatin stimulates c-fos to bind a transcriptionally responsive AP-1 element within the tissue inhibitor of metalloproteinase-1 promoter
    • Botelho F.M., Edwards D.R., Richards C.D. Oncostatin stimulates c-fos to bind a transcriptionally responsive AP-1 element within the tissue inhibitor of metalloproteinase-1 promoter. J. Biol. Chem. 273:1998;5211-5218.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5211-5218
    • Botelho, F.M.1    Edwards, D.R.2    Richards, C.D.3
  • 45
    • 0030789201 scopus 로고    scopus 로고
    • Homocysteine signal cascade: Production of phospholipids, activation of protein kinase C, and the induction of c-fos and c-myb in smooth muscle cells
    • Dalton M.L., Gadson P.F., Wrenn R.W., Rosenquist T.H. Homocysteine signal cascade: production of phospholipids, activation of protein kinase C, and the induction of c-fos and c-myb in smooth muscle cells. FASEB J. 11:1997;703-711.
    • (1997) FASEB J. , vol.11 , pp. 703-711
    • Dalton, M.L.1    Gadson, P.F.2    Wrenn, R.W.3    Rosenquist, T.H.4
  • 47
    • 0014545138 scopus 로고
    • Vascular pathology of homocysteinemia: Implications for the pathogenesis of arteriosclerosis
    • Mc Cully K.S. Vascular pathology of homocysteinemia: implications for the pathogenesis of arteriosclerosis. Am. J. Pathol. 56:1969;111-121.
    • (1969) Am. J. Pathol. , vol.56 , pp. 111-121
    • Mc Cully, K.S.1
  • 49
    • 84989552729 scopus 로고
    • Tissue inhibitor of metalloproteinase is increased in the serum of precirrhotic and cirrhotic alcoholic patients and can serve as a marker of fibrosis
    • Li J., Rosman A.S., Leo M.A., Nagai Y., Lieber C.S. Tissue inhibitor of metalloproteinase is increased in the serum of precirrhotic and cirrhotic alcoholic patients and can serve as a marker of fibrosis. Hepatology. 19:1994;1418-1423.
    • (1994) Hepatology , vol.19 , pp. 1418-1423
    • Li, J.1    Rosman, A.S.2    Leo, M.A.3    Nagai, Y.4    Lieber, C.S.5
  • 50
    • 0344937496 scopus 로고
    • Hepatic lesions in disorders of protein and amino acid metabolism
    • Oxford University Press, New York
    • G. Klastin, H.O. Conn, Hepatic lesions in disorders of protein and amino acid metabolism, in: Histopathology of the Liver, Oxford University Press, New York, 1993, pp. 241-245.
    • (1993) In: Histopathology of the Liver , pp. 241-245
    • Klastin, G.1    Conn, H.O.2
  • 51
    • 0032480790 scopus 로고    scopus 로고
    • Hyperhomocysteinemia after an oral methionine load acutely impairs endothelial function in healthy adults
    • Bellamy M.F., McDowell I.F., Ramsey M.W., Brownlee M., Bones C., Newcombe R.G., Lewis M.J. Hyperhomocysteinemia after an oral methionine load acutely impairs endothelial function in healthy adults. Circulation. 98:1998;1848-1852.
    • (1998) Circulation , vol.98 , pp. 1848-1852
    • Bellamy, M.F.1    McDowell, I.F.2    Ramsey, M.W.3    Brownlee, M.4    Bones, C.5    Newcombe, R.G.6    Lewis, M.J.7
  • 52
    • 0030728675 scopus 로고    scopus 로고
    • Acute methionine load-induced hyperhomocysteinemia enhances platelet aggregation, thromboxane biosynthesis, and macrophage-derived tissue factor activity in rats
    • Durand P., Lussier-Cacan S., Blache D. Acute methionine load-induced hyperhomocysteinemia enhances platelet aggregation, thromboxane biosynthesis, and macrophage-derived tissue factor activity in rats. FASEB J. 11:1997;1157-1168.
    • (1997) FASEB J. , vol.11 , pp. 1157-1168
    • Durand, P.1    Lussier-Cacan, S.2    Blache, D.3
  • 53
    • 9244222705 scopus 로고    scopus 로고
    • Reduction-oxidation (redox) state regulation of extracellular matrix metalloproteinases and tissue inhibitors in cardiac normal and transformed fibroblast cells
    • Tyagi S.C., Kumar G.S., Borders S. Reduction-oxidation (redox) state regulation of extracellular matrix metalloproteinases and tissue inhibitors in cardiac normal and transformed fibroblast cells. J. Cell. Biochem. 61:1996;139-151.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 139-151
    • Tyagi, S.C.1    Kumar, G.S.2    Borders, S.3
  • 55
    • 0027269781 scopus 로고
    • 2 and antioxidants have opposite effects on activation of NF-kB and AP-1 in intact cells: AP-1 as a secondary antioxidant-responsive factor
    • 2 and antioxidants have opposite effects on activation of NF-kB and AP-1 in intact cells: AP-1 as a secondary antioxidant-responsive factor. EMBO J. 12:1993;2005-2015.
    • (1993) EMBO J. , vol.12 , pp. 2005-2015
    • Meyer, M.1    Schreck, R.2    Bauerle, P.A.3
  • 56
    • 85025055449 scopus 로고
    • Peptide hormone and cytokine regulation of matrix synthesis
    • in: M.A. Zern, L.M. Reid (Eds.) Marcel Dekker, New York
    • S. Degli Esposti, M.A. Zern, Peptide hormone and cytokine regulation of matrix synthesis, in: M.A. Zern, L.M. Reid (Eds.), Extracellular matrix, Marcel Dekker, New York, 1993, pp. 331-349.
    • (1993) Extracellular Matrix , pp. 331-349
    • Degli Esposti, S.1    Zern, M.A.2


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