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Volumn 28, Issue 1, 1998, Pages 173-178

Lack of coordinate control of ferritin and transferrin receptor expression during rat liver regeneration

Author keywords

[No Author keywords available]

Indexed keywords

CARBON TETRACHLORIDE; FERRITIN; IRON; IRON REGULATORY FACTOR; MESSENGER RNA; TRANSFERRIN RECEPTOR;

EID: 0031807868     PISSN: 02709139     EISSN: None     Source Type: Journal    
DOI: 10.1002/hep.510280123     Document Type: Article
Times cited : (26)

References (22)
  • 1
    • 0029888671 scopus 로고    scopus 로고
    • Effects of positive iron status at a cellular level
    • McCord JM. Effects of positive iron status at a cellular level. Nutr Rev 1996;54:85-88.
    • (1996) Nutr Rev , vol.54 , pp. 85-88
    • McCord, J.M.1
  • 2
    • 0025248551 scopus 로고
    • Regulation of ferritin and transferrin receptor mRNAs
    • Theil EC. Regulation of ferritin and transferrin receptor mRNAs. J Biol Chem 1990;265:4771-4774.
    • (1990) J Biol Chem , vol.265 , pp. 4771-4774
    • Theil, E.C.1
  • 3
    • 0026684574 scopus 로고
    • Iron-dependent regulation of ferritin and transferrin receptor expression by the iron-responsive element binding proteins
    • Leibold EA, Guo B. Iron-dependent regulation of ferritin and transferrin receptor expression by the iron-responsive element binding proteins. Ann Rev Nutr 1992;2:345-368.
    • (1992) Ann Rev Nutr , vol.2 , pp. 345-368
    • Leibold, E.A.1    Guo, B.2
  • 4
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klausner RD, Rouault TA, Harford JB. Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 1993;72:19-26.
    • (1993) Cell , vol.72 , pp. 19-26
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 5
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze MW, Kuhn LC. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci U S A 1996;93:8175-8182.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 6
    • 0027141376 scopus 로고
    • Aconitase, a two-faced protein: Enzyme and iron regulatory factor
    • Beinert H, Kennedy MC. Aconitase, a two-faced protein: enzyme and iron regulatory factor. FASEB J 1993;7:1442-1449.
    • (1993) FASEB J , vol.7 , pp. 1442-1449
    • Beinert, H.1    Kennedy, M.C.2
  • 7
    • 0024121621 scopus 로고
    • Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5' untranslated regions of ferritin heavy- And light-subunit mRNAs
    • Leibold EA, Munro HN. Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5' untranslated regions of ferritin heavy- and light-subunit mRNAs. Proc Natl Acad Sci U S A 1988;85:2171-2175.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 8
    • 0027717217 scopus 로고
    • Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements
    • Henderson BR, Seiser C, Kuhn LC. Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements. J Biol Chem 1993;268:27327-27334.
    • (1993) J Biol Chem , vol.268 , pp. 27327-27334
    • Henderson, B.R.1    Seiser, C.2    Kuhn, L.C.3
  • 9
    • 0028131454 scopus 로고
    • Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity
    • Guo B, Yu Y, Leibold EA. Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity. J Biol Chem 1994;269:24252-24260.
    • (1994) J Biol Chem , vol.269 , pp. 24252-24260
    • Guo, B.1    Yu, Y.2    Leibold, E.A.3
  • 11
    • 0028143071 scopus 로고
    • Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation
    • Samaniego F, Chin J, Iwai K, Rouault TA, Klausner RD. Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation. J Biol Chem 1994;269:30904-30910.
    • (1994) J Biol Chem , vol.269 , pp. 30904-30910
    • Samaniego, F.1    Chin, J.2    Iwai, K.3    Rouault, T.A.4    Klausner, R.D.5
  • 12
    • 0028929735 scopus 로고
    • Translational represser activity is equivalent and is quantitatively predicted by in vitro RNA binding for two iron-responsive element-binding proteins, IRP1 and IRP2
    • Kim HY, Klausner RD, Rouault TA. Translational represser activity is equivalent and is quantitatively predicted by in vitro RNA binding for two iron-responsive element-binding proteins, IRP1 and IRP2. J Biol Chem 1995:270:4983-4986.
    • (1995) J Biol Chem , vol.270 , pp. 4983-4986
    • Kim, H.Y.1    Klausner, R.D.2    Rouault, T.A.3
  • 14
    • 0029132168 scopus 로고
    • Differential modulation of the RNA-binding proteins IRP-1 and IRP-2 in response to iron. IRP-2 inactivation requires translation of another protein
    • Henderson BR, Kuhn LC. Differential modulation of the RNA-binding proteins IRP-1 and IRP-2 in response to iron. IRP-2 inactivation requires translation of another protein. J Biol Chem 1995;270:20509-20515.
    • (1995) J Biol Chem , vol.270 , pp. 20509-20515
    • Henderson, B.R.1    Kuhn, L.C.2
  • 15
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome
    • Guo B, Phillips JD, Yu Y, Leibold EA. Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome. J Biol Chem 1995;270:21645-21651.
    • (1995) J Biol Chem , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 16
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2
    • Iwai K, Klausner RD, Rouault TA. Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO J 1995;14:5350-5357.
    • (1995) EMBO J , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 17
    • 0028321733 scopus 로고
    • Optimal sequence and structure of iron responsive elements: Selection of RNA stem-loops with high affinity for iron regulatory factor
    • Henderson BR, Menotti E, Bonnard C, Kuhn LC. Optimal sequence and structure of iron responsive elements: selection of RNA stem-loops with high affinity for iron regulatory factor. J Biol Chem 1994;269:17481-17489.
    • (1994) J Biol Chem , vol.269 , pp. 17481-17489
    • Henderson, B.R.1    Menotti, E.2    Bonnard, C.3    Kuhn, L.C.4
  • 18
    • 0029866604 scopus 로고    scopus 로고
    • Iron regulatory proteins 1 and 2 bind distinct sets of RNA target sequences
    • Henderson BR, Menotti E, Kuhn LC. Iron regulatory proteins 1 and 2 bind distinct sets of RNA target sequences. J Biol Chem 1996:271:4900-4908.
    • (1996) J Biol Chem , vol.271 , pp. 4900-4908
    • Henderson, B.R.1    Menotti, E.2    Kuhn, L.C.3
  • 20
    • 0029128256 scopus 로고
    • Nitric-oxide-mediated activation of iron-regulatory protein controls hepatic iron metabolism during acute inflammation
    • Cairo G, Pietrangelo A. Nitric-oxide-mediated activation of iron-regulatory protein controls hepatic iron metabolism during acute inflammation. Eur J Biochem 1995;232:358-363.
    • (1995) Eur J Biochem , vol.232 , pp. 358-363
    • Cairo, G.1    Pietrangelo, A.2
  • 21
    • 0028928738 scopus 로고
    • Induction of ferritin synthesis by oxidative stress. Transcriptional and post-transcriptional regulation by expansion of the "free" iron pool
    • Cairo G, Tacchini L, Pogliaghi G, Anzon E, Tomasi A, Bernelli-Zazzera A. Induction of ferritin synthesis by oxidative stress. Transcriptional and post-transcriptional regulation by expansion of the "free" iron pool. J Biol Chem 1995;270:700-703.
    • (1995) J Biol Chem , vol.270 , pp. 700-703
    • Cairo, G.1    Tacchini, L.2    Pogliaghi, G.3    Anzon, E.4    Tomasi, A.5    Bernelli-Zazzera, A.6
  • 22
    • 0029815291 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: A protective stratagem against oxidative injury
    • Cairo G, Castrusini E, Minotti G, Bernelli-Zazzera A. Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: a protective stratagem against oxidative injury. FASEB J 1996;10: 1326-1335.
    • (1996) FASEB J , vol.10 , pp. 1326-1335
    • Cairo, G.1    Castrusini, E.2    Minotti, G.3    Bernelli-Zazzera, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.