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Volumn 38, Issue 3, 1997, Pages 437-446

Modulation of LDL receptor mRNA stability by phorbol esters in human liver cell culture models

Author keywords

colchicine; cytochalasin D; cytoskeleton; polyribosomes; posttranscriptional regulation

Indexed keywords

BILE SALT; COLCHICINE; CYTOCHALASIN B; LOW DENSITY LIPOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; MESSENGER RNA; PHORBOL ESTER;

EID: 0030941695     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (36)

References (43)
  • 1
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown, M. S., and J. L. Goldstein. 1986. A receptor-mediated pathway for cholesterol homeostasis. Science. 232: 34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 2
    • 0019813096 scopus 로고
    • Characterization of the major lipoproteins secreted by two human hepatoma cell lines
    • Zannis, V. I., J. L. Breslow, T. R. SanGiacomo, D. P. Aden, and B. B. Knowles. 1981. Characterization of the major lipoproteins secreted by two human hepatoma cell lines. Biochemistty. 20: 7089-7096.
    • (1981) Biochemistty. , vol.20 , pp. 7089-7096
    • Zannis, V.I.1    Breslow, J.L.2    Sangiacomo, T.R.3    Aden, D.P.4    Knowles, B.B.5
  • 3
    • 0021720294 scopus 로고
    • Regulation of low-density lipoprotein receptors in the human hepatoma cell line HepG2
    • Illingworth, D. R., S. Lindsey, and F. C. Hagemenas. 1984. Regulation of low-density lipoprotein receptors in the human hepatoma cell line HepG2. Exp. Cell Res. 155:518-526.
    • (1984) Exp. Cell Res. , vol.155 , pp. 518-526
    • Illingworth, D.R.1    Lindsey, S.2    Hagemenas, F.C.3
  • 4
    • 0025165019 scopus 로고
    • HepG2 cells as a resource for metabolic studies: Lipoprotein, cholesterol, and bile acids
    • Javitt, N. B. 1990. HepG2 cells as a resource for metabolic studies: lipoprotein, cholesterol, and bile acids. FASEB J. 4: 161-168.
    • (1990) FASEB J. , vol.4 , pp. 161-168
    • Javitt, N.B.1
  • 5
    • 0026661808 scopus 로고
    • Regulation of LDL receptor, apoB, and apoE protein and mRNA in HepG2 cells
    • Kraft, H. G., S. J. Demosky, K. Schumacher, H. B. Brewer, and J. M. Hoeg. 1992. Regulation of LDL receptor, apoB, and apoE protein and mRNA in HepG2 cells. DNA Cell Biol. 11: 291-300.
    • (1992) DNA Cell Biol. , vol.11 , pp. 291-300
    • Kraft, H.G.1    Demosky, S.J.2    Schumacher, K.3    Brewer, H.B.4    Hoeg, J.M.5
  • 6
    • 0025993049 scopus 로고
    • Differences between the regulation of 3-hydroxy-3-methylglutaryl-coenzyme a reductase and low density lipoprotein receptor in human hepatoma cells and fibroblasts reside primarily at the translational and post-translational levels
    • Tam, S-P., L. Brisette, R. Ramharack, and R. G. Deeley. 1991. Differences between the regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and low density lipoprotein receptor in human hepatoma cells and fibroblasts reside primarily at the translational and post-translational levels. J. Biol. Chem. 266: 16764-16773.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16764-16773
    • Tam, S.-P.1    Brisette, L.2    Ramharack, R.3    Deeley, R.G.4
  • 7
    • 0019332750 scopus 로고
    • Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis B surface antigen
    • Knowles, B. B., C. C. Howe, and D. P. Aden. 1980. Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis B surface antigen. Science. 209: 497-499.
    • (1980) Science , vol.209 , pp. 497-499
    • Knowles, B.B.1    Howe, C.C.2    Aden, D.P.3
  • 8
    • 84989558379 scopus 로고
    • Characterization of human hepatocyte lines derived from normal liver tissue
    • Roberts, E. A., M. Le tarte, J. Squire, and S. Yang. 1994. Characterization of human hepatocyte lines derived from normal liver tissue. Hepatology. 19: 1390-1399.
    • (1994) Hepatology , vol.19 , pp. 1390-1399
    • Roberts, E.A.1    Le Tarte, M.2    Squire, J.3    Yang, S.4
  • 9
    • 0021276357 scopus 로고
    • Effects of compactin, mevalonate and low density lipoprotein on 3-hydroxy-3-methylglutaryl-coenzyme a reductase activity and low-density-lipoprotein-receptor activity in the human hepatoma cell line HepG2
    • Cohen, L. H., M. Griffioen, L. Havekes, D. Schouten, V. van Hinsbergh, and H. J. Kempen. 1984. Effects of compactin, mevalonate and low density lipoprotein on 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity and low-density-lipoprotein-receptor activity in the human hepatoma cell line HepG2. Biochem. J. 222: 35-39.
    • (1984) Biochem. J. , vol.222 , pp. 35-39
    • Cohen, L.H.1    Griffioen, M.2    Havekes, L.3    Schouten, D.4    Van Hinsbergh, V.5    Kempen, H.J.6
  • 10
    • 0023447774 scopus 로고
    • Cellular free cholesterol in HepG2 cells is only partially available for down-regulation of low-density-lipoprotein receptor activity
    • Havekes, L. M., E. C. M. de Wit, and H. M. G. Princen. 1987. Cellular free cholesterol in HepG2 cells is only partially available for down-regulation of low-density-lipoprotein receptor activity. Biochem. J. 247: 739-746.
    • (1987) Biochem. J. , vol.247 , pp. 739-746
    • Havekes, L.M.1    De Wit, E.C.M.2    Princen, H.M.G.3
  • 11
    • 0026764203 scopus 로고
    • Complete down-regulation of low-density-lipoprotein-receptor activity in the human hepatoma cell line HepG2 by β-migrating very-low-densiry-lipoprotein and non-lipoprotein cholesterol
    • Kamps, J. A. A. M., and T. J. G. van Berkel. 1992. Complete down-regulation of low-density-lipoprotein-receptor activity in the human hepatoma cell line HepG2 by β-migrating very-low-densiry-lipoprotein and non-lipoprotein cholesterol. Eur. J. Biochem. 206: 973-978.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 973-978
    • Kamps, J.A.A.M.1    Van Berkel, T.J.G.2
  • 12
    • 0024308255 scopus 로고
    • Involvement of second messengers in regulation of the low-density lipoprotein receptor gene
    • Auwerx, J. H., A. Chait, G. Wolfbauer, and S. S. Deeb. 1989. Involvement of second messengers in regulation of the low-density lipoprotein receptor gene. Mol. Cell. Biol. 9: 2298-2302.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2298-2302
    • Auwerx, J.H.1    Chait, A.2    Wolfbauer, G.3    Deeb, S.S.4
  • 13
    • 0024511599 scopus 로고
    • Regulation of the low density lipoprotein receptor and hydroxymethylglutaryl coenzyme A reductase genes by protein kinase C and a putative negative regulatory protein
    • Auwerx, J. H., A. Chait, and S. S. Deeb. 1989. Regulation of the low density lipoprotein receptor and hydroxymethylglutaryl coenzyme A reductase genes by protein kinase C and a putative negative regulatory protein. Proc. Natl. Acad. Sci. USA. 86: 1133-1137.
    • (1989) Proc. Natl. Acad. Sci. USA. , vol.86 , pp. 1133-1137
    • Auwerx, J.H.1    Chait, A.2    Deeb, S.S.3
  • 14
    • 0027180774 scopus 로고
    • Regulation of low-density-lipoprotein receptors in the human hepatoma cell line HepG2
    • Kamps, J. A. A. M., and T. J. C. van Berkel. 1993. Regulation of low-density-lipoprotein receptors in the human hepatoma cell line HepG2. Eur. J. Biochem. 213: 989-994.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 989-994
    • Kamps, J.A.A.M.1    Van Berkel, T.J.C.2
  • 16
    • 0014013696 scopus 로고
    • A membrane-filter technique for the detection of complementary DNA
    • Denhardt, D. T. 1966. A membrane-filter technique for the detection of complementary DNA. Biochem. Biophys. Res. Commun. 23: 641-646.
    • (1966) Biochem. Biophys. Res. Commun. , vol.23 , pp. 641-646
    • Denhardt, D.T.1
  • 17
    • 0017383720 scopus 로고
    • Turnover of ribosomal RNA in cells in culture
    • Scott, J. F. 1977. Turnover of ribosomal RNA in cells in culture. Exp. Cell Res. 108: 207-219.
    • (1977) Exp. Cell Res. , vol.108 , pp. 207-219
    • Scott, J.F.1
  • 18
    • 0015503520 scopus 로고
    • Ribosomal RNA turnover in contact inhibited cells
    • Weber, M. J. 1972. Ribosomal RNA turnover in contact inhibited cells. Nature New Biol. 235: 58-61.
    • (1972) Nature New Biol. , vol.235 , pp. 58-61
    • Weber, M.J.1
  • 19
    • 0016242041 scopus 로고
    • Changes in RNA in relation to growth of the fibroblast: II. The lifetime of mRNA, rRNA, and tRNA in resting and growing cells
    • Abelson, H. T., L. F. Johnson, S. Penman, and H. Green. 1974. Changes in RNA in relation to growth of the fibroblast: II. The lifetime of mRNA, rRNA, and tRNA in resting and growing cells. Cell. 1: 161-165.
    • (1974) Cell , vol.1 , pp. 161-165
    • Abelson, H.T.1    Johnson, L.F.2    Penman, S.3    Green, H.4
  • 21
    • 0019618723 scopus 로고
    • The size and distribution of cytochrome c oxidase subunit IV mRNA between free and membrane-bound polyribosomes
    • Northemann, W., E. Schmelzer, and P. C. Heinrich. 1981. The size and distribution of cytochrome c oxidase subunit IV mRNA between free and membrane-bound polyribosomes. Eur. J. Biochem. 119: 203-208.
    • (1981) Eur. J. Biochem. , vol.119 , pp. 203-208
    • Northemann, W.1    Schmelzer, E.2    Heinrich, P.C.3
  • 22
    • 0025873671 scopus 로고
    • Interaction between mRNA, ribosomes and the cytoskeleton
    • Hesketh, J. E., and I. F. Pryme. 1991, Interaction between mRNA, ribosomes and the cytoskeleton. Biochem. J. 277: 1-10.
    • (1991) Biochem. J. , vol.277 , pp. 1-10
    • Hesketh, J.E.1    Pryme, I.F.2
  • 23
    • 15444341533 scopus 로고
    • Ph.D. thesis, Queen's University, Kingston, Ontario, Canada. 70-72
    • Cochrane, A. W. 1987. Ph.D. thesis, Queen's University, Kingston, Ontario, Canada. 70-72.
    • (1987)
    • Cochrane, A.W.1
  • 24
    • 0029009223 scopus 로고
    • Constitutive production of 92-kDa gelatinase B can be suppressed by alterations in cell shape
    • MacDougall, J. R., and R. S. Kerbel. 1995. Constitutive production of 92-kDa gelatinase B can be suppressed by alterations in cell shape. Exp. Cell Res. 218: 508-515.
    • (1995) Exp. Cell Res. , vol.218 , pp. 508-515
    • MacDougall, J.R.1    Kerbel, R.S.2
  • 25
    • 0025287304 scopus 로고
    • Actin gene expression in murine erythroleukemia cells treated with cytochalasin D
    • Sympson, C. J., and T. E. Geoghegan. 1990. Actin gene expression in murine erythroleukemia cells treated with cytochalasin D. Exp. Cell Res. 189: 28-32.
    • (1990) Exp. Cell Res. , vol.189 , pp. 28-32
    • Sympson, C.J.1    Geoghegan, T.E.2
  • 26
    • 0025243509 scopus 로고
    • Partial down-regulation of protein kinase C reverses the growth inhibitory effect of phorbol esters on HepG2 cells
    • Duronio, V., B. E. Huber, and S. Jacobs. 1990. Partial down-regulation of protein kinase C reverses the growth inhibitory effect of phorbol esters on HepG2 cells. J. Cell. Physiol. 145: 381-389.
    • (1990) J. Cell. Physiol. , vol.145 , pp. 381-389
    • Duronio, V.1    Huber, B.E.2    Jacobs, S.3
  • 27
    • 0019125093 scopus 로고
    • Phorbol esters and vasopressin stimulate DNA synthesis by a common mechanism
    • Dicker, P., and E. Rozengurt. 1980. Phorbol esters and vasopressin stimulate DNA synthesis by a common mechanism. Nature. 287: 607-612.
    • (1980) Nature , vol.287 , pp. 607-612
    • Dicker, P.1    Rozengurt, E.2
  • 28
    • 0019989535 scopus 로고
    • Binding of phorbol esters to high affinity sites on murine fibroblastic cells elicits a mitogenic response
    • Collins, M. K. L., and E. Rozengurt. 1982. Binding of phorbol esters to high affinity sites on murine fibroblastic cells elicits a mitogenic response. J. Cell. Physiol. 112: 42-50.
    • (1982) J. Cell. Physiol. , vol.112 , pp. 42-50
    • Collins, M.K.L.1    Rozengurt, E.2
  • 29
    • 0020956486 scopus 로고
    • Tumor promoter 12-O-tetradecanoylphorbol 13-acetate, like epidermal growth factor, stimulates cell proliferation and inhibits differentiation of mouse mammary epithelial cells in culture
    • Taketani, Y., and T. Oka. 1983. Tumor promoter 12-O-tetradecanoylphorbol 13-acetate, like epidermal growth factor, stimulates cell proliferation and inhibits differentiation of mouse mammary epithelial cells in culture. Proc. Natl. Acad. Sci. USA. 80: 1646-1649.
    • (1983) Proc. Natl. Acad. Sci. USA. , vol.80 , pp. 1646-1649
    • Taketani, Y.1    Oka, T.2
  • 30
    • 0018771246 scopus 로고
    • Induction of differentiation in human promyelocytic leukemia cells by tumor promoters
    • Rovera, G., T. G. O'Brien, and L. Diamond. 1977. Induction of differentiation in human promyelocytic leukemia cells by tumor promoters. Science. 240: 868-870.
    • (1977) Science , vol.240 , pp. 868-870
    • Rovera, G.1    O'Brien, T.G.2    Diamond, L.3
  • 31
    • 2642682843 scopus 로고
    • Induction of terminal differentiation in human promyelocytic leukemia cells by tumor-promoting agents
    • Huberman, E., and M. F. Callahan. 1979. Induction of terminal differentiation in human promyelocytic leukemia cells by tumor-promoting agents. Proc. Natl. Acad. Sci. USA. 76: 1293-1297.
    • (1979) Proc. Natl. Acad. Sci. USA. , vol.76 , pp. 1293-1297
    • Huberman, E.1    Callahan, M.F.2
  • 32
    • 0017657408 scopus 로고
    • Tumor promoters inhibit spontaneous and induced differentiation of murine erythrolenkemia cells in culture
    • Yamasaki, H., E. Fibach, U. Nudel, I. B. Weinstein, R. A. Rifkind, and P.A. Marks. 1977. Tumor promoters inhibit spontaneous and induced differentiation of murine erythrolenkemia cells in culture. Proc. Natl. Acad. Sci. USA. 74: 3451-3455.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3451-3455
    • Yamasaki, H.1    Fibach, E.2    Nudel, U.3    Weinstein, I.B.4    Rifkind, R.A.5    Marks, P.A.6
  • 33
    • 0017396543 scopus 로고
    • Inhibition of adipose conversion of 3T3 fibroblasts by tumour promoters
    • Diamond, L., T. G. O'Brien, and G. Rovera. 1977. Inhibition of adipose conversion of 3T3 fibroblasts by tumour promoters. Nature. 269: 247-248.
    • (1977) Nature , vol.269 , pp. 247-248
    • Diamond, L.1    O'Brien, T.G.2    Rovera, G.3
  • 34
    • 0027263506 scopus 로고
    • Metabolic requirements for phorbol ester-induced cytoskeletal changes in renal epithelium
    • Rahilly, M. A., and S. Fleming. 1993. Metabolic requirements for phorbol ester-induced cytoskeletal changes in renal epithelium. J. Pathol. 169: 439-443.
    • (1993) J. Pathol. , vol.169 , pp. 439-443
    • Rahilly, M.A.1    Fleming, S.2
  • 35
    • 0026528680 scopus 로고
    • A tumour promoter induces alterations in vinculin and actin distribution in human renal epithelium
    • Rahilly, M. A., and S. Fleming. 1992. A tumour promoter induces alterations in vinculin and actin distribution in human renal epithelium. J. Pathol. 166: 283-288.
    • (1992) J. Pathol. , vol.166 , pp. 283-288
    • Rahilly, M.A.1    Fleming, S.2
  • 36
    • 0021987524 scopus 로고
    • Altered β-actin gene expression in phorbol myristate acetate-treated chondrocytes and fibroblasts
    • Gerstenfeld, L.C., M.H. Finer, and H. Boedtker. 1985. Altered β-actin gene expression in phorbol myristate acetate-treated chondrocytes and fibroblasts. Mol. Cell. Biol. 5: 1425-1433.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1425-1433
    • Gerstenfeld, L.C.1    Finer, M.H.2    Boedtker, H.3
  • 37
    • 0021984056 scopus 로고
    • Induction of cytoskeletal vimentin and actin gene expression by a tumor-promoting phorbol ester in the human leukemic cell line K562
    • Siebert, P. D., and M. Fukuda. 1985. Induction of cytoskeletal vimentin and actin gene expression by a tumor-promoting phorbol ester in the human leukemic cell line K562. J. Biol. Chem. 260: 3868-3874.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3868-3874
    • Siebert, P.D.1    Fukuda, M.2
  • 38
    • 0028169463 scopus 로고
    • Actin mRNA localization is regulated by signal transduction mechanisms
    • Latham, V. M., E. H. Kislauskis, R. H. Singer, and A. F. Ross. 1994. β-Actin mRNA localization is regulated by signal transduction mechanisms. J. Cell Biol. 126: 1211-1219.
    • (1994) J. Cell Biol. , vol.126 , pp. 1211-1219
    • Latham, V.M.1    Kislauskis, E.H.2    Singer, R.H.3    Ross, A.F.4
  • 39
    • 0028178827 scopus 로고
    • Targeting of c-myc and β-globin coding sequences to cytoskeletal-bound polysemes by c-myc 3′ untranslated region
    • Hesketh, J. E., G. Campbell, M. Piechaczyk, and J-M. Blanchard. 1994. Targeting of c-myc and β-globin coding sequences to cytoskeletal-bound polysemes by c-myc 3′ untranslated region. Biochem. J. 298: 143-148.
    • (1994) Biochem. J. , vol.298 , pp. 143-148
    • Hesketh, J.E.1    Campbell, G.2    Piechaczyk, M.3    Blanchard, J.-M.4
  • 40
    • 0028983109 scopus 로고
    • The mRNAs for cyclin A, c-myc and ribosomal proteins L4 and S6 are associated with cytoskeletal-bound polysomes in HepG2 cells
    • Hovland, R., G. Campbell, I. Pryme, and J. Hesketh. 1995. The mRNAs for cyclin A, c-myc and ribosomal proteins L4 and S6 are associated with cytoskeletal-bound polysomes in HepG2 cells. Biochem. J. 310: 193-196.
    • (1995) Biochem. J. , vol.310 , pp. 193-196
    • Hovland, R.1    Campbell, G.2    Pryme, I.3    Hesketh, J.4
  • 41
    • 0025649192 scopus 로고
    • Differential association of membrane-bound and non-membrane-bound polysomes with the cytoskeleton
    • Zambetti, G., L. Wilming, E. G. Fey, S. Penman, J. Stein, and G. Stein. 1990. Differential association of membrane-bound and non-membrane-bound polysomes with the cytoskeleton. Exp. Cell Res. 191: 246-255.
    • (1990) Exp. Cell Res. , vol.191 , pp. 246-255
    • Zambetti, G.1    Wilming, L.2    Fey, E.G.3    Penman, S.4    Stein, J.5    Stein, G.6
  • 42
    • 0026651004 scopus 로고
    • Disorganization of microfilaments is accompanied by down-regulation of α-smooth muscle actin isoform mRNA level in cultured vascular smooth muscle cells
    • Nomura, K., H. Teraoka, H. Arita, and O. Ohara. 1992. Disorganization of microfilaments is accompanied by down-regulation of α-smooth muscle actin isoform mRNA level in cultured vascular smooth muscle cells. J. Biochem. 112: 102-106.
    • (1992) J. Biochem. , vol.112 , pp. 102-106
    • Nomura, K.1    Teraoka, H.2    Arita, H.3    Ohara, O.4
  • 43
    • 0028173553 scopus 로고
    • Cytochalasin D exerts stimulatory and inhibitory effects on insulin-induced glucokinase mRNA expression in hepatocytes
    • Beresford, G. W., and L. Agius. 1994. Cytochalasin D exerts stimulatory and inhibitory effects on insulin-induced glucokinase mRNA expression in hepatocytes. Mol. Cell. Biochem. 139: 177-184.
    • (1994) Mol. Cell. Biochem. , vol.139 , pp. 177-184
    • Beresford, G.W.1    Agius, L.2


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