메뉴 건너뛰기




Volumn 365, Issue 1, 2008, Pages 69-74

Modulation of immediate early gene expression by tristetraprolin in the differentiation of 3T3-L1 cells

Author keywords

3T3 L1; AU rich element; Immediate early gene; MKP 1; Tristetraprolin

Indexed keywords

CYCLOOXYGENASE 2; CYSTEINE RICH PROTEIN 61; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D; HUR PROTEIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE 1; NUCLEAR RECEPTOR NUR77; PROTEIN BTG2; PROTEIN C JUN; PROTEIN COX2; PROTEIN MKP1; PROTEIN PIP92; PROTEIN TTP; TRISTETRAPROLIN; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN;

EID: 36049006140     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.10.119     Document Type: Article
Times cited : (29)

References (42)
  • 1
    • 0029062839 scopus 로고
    • Transcriptional regulation of gene expression during adipocyte differentiation
    • MacDougald O.A., and Lane M.D. Transcriptional regulation of gene expression during adipocyte differentiation. Annu. Rev. Biochem. 64 (1995) 345-373
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 345-373
    • MacDougald, O.A.1    Lane, M.D.2
  • 4
    • 0033619778 scopus 로고    scopus 로고
    • Differential regulation of immediate early gene expression in preadipocyte cells through multiple signaling pathways
    • Inuzuka H., Nanbu-Wakao R., Masuho Y., Muramatsu M., Tojo H., and Wakao H. Differential regulation of immediate early gene expression in preadipocyte cells through multiple signaling pathways. Biochem. Biophys. Res. Commun. 265 (1999) 664-668
    • (1999) Biochem. Biophys. Res. Commun. , vol.265 , pp. 664-668
    • Inuzuka, H.1    Nanbu-Wakao, R.2    Masuho, Y.3    Muramatsu, M.4    Tojo, H.5    Wakao, H.6
  • 5
    • 0035819859 scopus 로고    scopus 로고
    • Regulation of mRNA stability in mammalian cells
    • Guhaniyogi J., and Brewer G. Regulation of mRNA stability in mammalian cells. Gene 265 (2001) 11-23
    • (2001) Gene , vol.265 , pp. 11-23
    • Guhaniyogi, J.1    Brewer, G.2
  • 6
    • 0028788194 scopus 로고
    • AU-rich elements: characterization and importance in mRNA degradation
    • Chen C.Y., and Shyu A.B. AU-rich elements: characterization and importance in mRNA degradation. Trends Biochem. Sci. 20 (1995) 465-470
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 465-470
    • Chen, C.Y.1    Shyu, A.B.2
  • 7
    • 31144448042 scopus 로고    scopus 로고
    • AU-rich elements and associated factors: are there unifying principles?
    • Barreau C., Paillard L., and Osborne H.B. AU-rich elements and associated factors: are there unifying principles?. Nucleic Acids Res. 33 (2006) 7138-7150
    • (2006) Nucleic Acids Res. , vol.33 , pp. 7138-7150
    • Barreau, C.1    Paillard, L.2    Osborne, H.B.3
  • 8
    • 0033524475 scopus 로고    scopus 로고
    • Why is Hu where? Shuttling of early-response-gene messenger RNA subsets
    • Keene J.D. Why is Hu where? Shuttling of early-response-gene messenger RNA subsets. Proc. Natl. Acad. Sci. USA 96 (1999) 5-7
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5-7
    • Keene, J.D.1
  • 9
    • 21644479921 scopus 로고    scopus 로고
    • An early event in adipogenesis, the nuclear selection of the CCAAT enhancer-binding protein β (C/EBPβ) mRNA by HuR and its translocation to the cytosol
    • Gantt K., Cherry J., Tenney R., Karschner V., and Pekala P.H. An early event in adipogenesis, the nuclear selection of the CCAAT enhancer-binding protein β (C/EBPβ) mRNA by HuR and its translocation to the cytosol. J. Biol. Chem. 280 (2005) 24768-24774
    • (2005) J. Biol. Chem. , vol.280 , pp. 24768-24774
    • Gantt, K.1    Cherry, J.2    Tenney, R.3    Karschner, V.4    Pekala, P.H.5
  • 10
    • 0034653560 scopus 로고    scopus 로고
    • Evidence that tristetraprolin is a physiological regulator of granulocyte-macrophage colony stimulating factor messenger RNA deadenylation and stability
    • Carballo E., Lai W.S., and Blackshear P.J. Evidence that tristetraprolin is a physiological regulator of granulocyte-macrophage colony stimulating factor messenger RNA deadenylation and stability. Blood 95 (2000) 1891-1899
    • (2000) Blood , vol.95 , pp. 1891-1899
    • Carballo, E.1    Lai, W.S.2    Blackshear, P.J.3
  • 12
    • 0034625369 scopus 로고    scopus 로고
    • Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to AU-rich elements and destabilization of mRNA
    • Lai W.S., Carballo E., Thorn J.M., Kennington E.A., and Blackshear P.J. Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to AU-rich elements and destabilization of mRNA. J. Biol. Chem. 275 (2000) 17827-17837
    • (2000) J. Biol. Chem. , vol.275 , pp. 17827-17837
    • Lai, W.S.1    Carballo, E.2    Thorn, J.M.3    Kennington, E.A.4    Blackshear, P.J.5
  • 13
    • 0033049125 scopus 로고    scopus 로고
    • Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA
    • Lai W.S., Carballo E., Strum J.R., Kennington E.A., Philips R.S., and Blackshear P.J. Evidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA. Mol. Cell. Biol. 19 (1999) 4311-4323
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4311-4323
    • Lai, W.S.1    Carballo, E.2    Strum, J.R.3    Kennington, E.A.4    Philips, R.S.5    Blackshear, P.J.6
  • 14
    • 0038751970 scopus 로고    scopus 로고
    • Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly (A) ribonuclease
    • Lai W.S., Kennington E.A., and Blackshear P.J. Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly (A) ribonuclease. Mol. Cell Biol. 23 (2003) 3798-3812
    • (2003) Mol. Cell Biol. , vol.23 , pp. 3798-3812
    • Lai, W.S.1    Kennington, E.A.2    Blackshear, P.J.3
  • 16
    • 0037080834 scopus 로고    scopus 로고
    • The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements
    • Mukherjee D., Gao M., O'Connor J.P., Raijmakers R., Pruijn G., Lutz C.S., and Wilusz J. The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements. EMBO J. 21 (2002) 165-174
    • (2002) EMBO J. , vol.21 , pp. 165-174
    • Mukherjee, D.1    Gao, M.2    O'Connor, J.P.3    Raijmakers, R.4    Pruijn, G.5    Lutz, C.S.6    Wilusz, J.7
  • 17
    • 13244298460 scopus 로고    scopus 로고
    • Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1
    • Lykke-Andersen J., and Wagner E. Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1. Genes Dev. 19 (2005) 351-361
    • (2005) Genes Dev. , vol.19 , pp. 351-361
    • Lykke-Andersen, J.1    Wagner, E.2
  • 19
    • 29144481702 scopus 로고    scopus 로고
    • Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping
    • Fenger-Grøn M., Fillman C., Norrild B., and Lykke-Andersen J. Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol. Cell 20 (2005) 905-915
    • (2005) Mol. Cell , vol.20 , pp. 905-915
    • Fenger-Grøn, M.1    Fillman, C.2    Norrild, B.3    Lykke-Andersen, J.4
  • 20
    • 33947301293 scopus 로고    scopus 로고
    • TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements
    • Franks T.M., and Lykke-Acdersen J. TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements. Genes Dev. 21 (2007) 719-735
    • (2007) Genes Dev. , vol.21 , pp. 719-735
    • Franks, T.M.1    Lykke-Acdersen, J.2
  • 21
    • 33846420169 scopus 로고    scopus 로고
    • Regulation of tristetraprolin during differentiation of 3T3-L1 preadipocytes
    • Lin N.-Y., Lin C.-T., Chen Y.-L., and Chang C.-J. Regulation of tristetraprolin during differentiation of 3T3-L1 preadipocytes. FEBS J. 274 (2007) 867-878
    • (2007) FEBS J. , vol.274 , pp. 867-878
    • Lin, N.-Y.1    Lin, C.-T.2    Chen, Y.-L.3    Chang, C.-J.4
  • 22
    • 2942623942 scopus 로고    scopus 로고
    • The role of mRNA turnover in the regulation of tristetraprolin expression: evidence for an extracellular signal-regulated kinase-specific, AU-rich element-dependent. Autoregulatory pathway
    • Brooks S.A., Connolly J.E., and Rigby W.F. The role of mRNA turnover in the regulation of tristetraprolin expression: evidence for an extracellular signal-regulated kinase-specific, AU-rich element-dependent. Autoregulatory pathway. J. Immun. 172 (2004) 7264-7271
    • (2004) J. Immun. , vol.172 , pp. 7264-7271
    • Brooks, S.A.1    Connolly, J.E.2    Rigby, W.F.3
  • 23
    • 3543003469 scopus 로고    scopus 로고
    • The stability of tristetraprolin mRNA is regulated by mitogen-activated protein kinase p38 by tristetraprolin itself
    • Tchen C.R., Brook M., Saklatvala J., and Clark A.R. The stability of tristetraprolin mRNA is regulated by mitogen-activated protein kinase p38 by tristetraprolin itself. J. Biol. Chem. 279 (2004) 32393-32400
    • (2004) J. Biol. Chem. , vol.279 , pp. 32393-32400
    • Tchen, C.R.1    Brook, M.2    Saklatvala, J.3    Clark, A.R.4
  • 24
    • 0037223402 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase-dependent and-independent signaling of mRNA stability of AU-rich element-containing transcripts
    • Frevel M.A., Bakheet T., Silva A.M., Hissong J.G., Khabar K.S.A., and Williams B.R.G. p38 mitogen-activated protein kinase-dependent and-independent signaling of mRNA stability of AU-rich element-containing transcripts. Mol. Cell. Biol. 23 (2003) 425-436
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 425-436
    • Frevel, M.A.1    Bakheet, T.2    Silva, A.M.3    Hissong, J.G.4    Khabar, K.S.A.5    Williams, B.R.G.6
  • 25
    • 0035823625 scopus 로고    scopus 로고
    • Distinct transcriptional profiles of adipogenesis in vivo and in vitro
    • Soukas A., Socci N.D., Saatkamp B.D., Novelli S., and Friedman J.M. Distinct transcriptional profiles of adipogenesis in vivo and in vitro. J. Biol. Chem. 276 (2001) 34167-34174
    • (2001) J. Biol. Chem. , vol.276 , pp. 34167-34174
    • Soukas, A.1    Socci, N.D.2    Saatkamp, B.D.3    Novelli, S.4    Friedman, J.M.5
  • 26
    • 24344507734 scopus 로고    scopus 로고
    • Krox20 stimulates adipogenesis via C/EBPbeta-dependent and independent mechanisms
    • Chen Z., Torrens J.I., Anand A., Spiegeiman B.M., and Friedman J.M. Krox20 stimulates adipogenesis via C/EBPbeta-dependent and independent mechanisms. Cell Metab. 1 (2005) 93-106
    • (2005) Cell Metab. , vol.1 , pp. 93-106
    • Chen, Z.1    Torrens, J.I.2    Anand, A.3    Spiegeiman, B.M.4    Friedman, J.M.5
  • 27
    • 34248670716 scopus 로고    scopus 로고
    • Orphan nuclear receptor Nur77 acclerates the initial phase of adipocyte differentiation in 3T3-L1 cells by promoting clonal expansion
    • Fumoto T., Yamaguchi T., Hirose F., and Osumi T. Orphan nuclear receptor Nur77 acclerates the initial phase of adipocyte differentiation in 3T3-L1 cells by promoting clonal expansion. J. Biochem. (Tokyo) 141 (2007) 181-192
    • (2007) J. Biochem. (Tokyo) , vol.141 , pp. 181-192
    • Fumoto, T.1    Yamaguchi, T.2    Hirose, F.3    Osumi, T.4
  • 28
    • 0035094340 scopus 로고    scopus 로고
    • The pleiotropic functions of peroxisome proliferators-activated receptor γ
    • Debril M.B., Renaud J.P., Fajas L., and Auwerx J. The pleiotropic functions of peroxisome proliferators-activated receptor γ. J. Mol. Med. 79 (2001) 30-47
    • (2001) J. Mol. Med. , vol.79 , pp. 30-47
    • Debril, M.B.1    Renaud, J.P.2    Fajas, L.3    Auwerx, J.4
  • 29
    • 0029965446 scopus 로고    scopus 로고
    • Cyr61, a product of a growth factor-inducible immediate-early gene, promotes cell proliferation, migration and adhesion
    • Kireeva M.L., Mo F.E., Yang G.P., and Lau L.F. Cyr61, a product of a growth factor-inducible immediate-early gene, promotes cell proliferation, migration and adhesion. Mol. Cell Biol. 16 (1996) 1326-1334
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1326-1334
    • Kireeva, M.L.1    Mo, F.E.2    Yang, G.P.3    Lau, L.F.4
  • 32
    • 0037853195 scopus 로고    scopus 로고
    • Tristetraprolin binds to the 3′-untranslated region of cyclooxygenase-2 mRNA. A polyadeylation variant in a cancer cell line lacks the binding site
    • Sawaoka H., Dixon D.A., Oates J.A., and Boutaud O. Tristetraprolin binds to the 3′-untranslated region of cyclooxygenase-2 mRNA. A polyadeylation variant in a cancer cell line lacks the binding site. J. Biol. Chem. 278 (2003) 13928-13935
    • (2003) J. Biol. Chem. , vol.278 , pp. 13928-13935
    • Sawaoka, H.1    Dixon, D.A.2    Oates, J.A.3    Boutaud, O.4
  • 33
    • 1242337338 scopus 로고    scopus 로고
    • Structural and functional dissection of a conserved destabilizing element of cyclo-oxygenase-2 mRNA: evidence against the involvement of AUF-1 [AU-rich element/poly(U)-binding/degradation factor-1], AUF-2, tristetraprolin, HuR (Hu antigen R) or FBP1 (far-upstream-sequence-element-binding protein 1)
    • Sully G., Dean J.L.E., Wait R., Rawlinson L., Santalucia T., Saklatvala J., and Clark A.R. Structural and functional dissection of a conserved destabilizing element of cyclo-oxygenase-2 mRNA: evidence against the involvement of AUF-1 [AU-rich element/poly(U)-binding/degradation factor-1], AUF-2, tristetraprolin, HuR (Hu antigen R) or FBP1 (far-upstream-sequence-element-binding protein 1). Biochem. J. 377 (2004) 629-639
    • (2004) Biochem. J. , vol.377 , pp. 629-639
    • Sully, G.1    Dean, J.L.E.2    Wait, R.3    Rawlinson, L.4    Santalucia, T.5    Saklatvala, J.6    Clark, A.R.7
  • 34
  • 35
    • 33646183274 scopus 로고    scopus 로고
    • Posttranscriptional mechanisms regulating the inflammatory response
    • Stoecklin G., and Anderson P. Posttranscriptional mechanisms regulating the inflammatory response. Adv. Immunol. 89 (2006) 1-37
    • (2006) Adv. Immunol. , vol.89 , pp. 1-37
    • Stoecklin, G.1    Anderson, P.2
  • 36
    • 0035168692 scopus 로고    scopus 로고
    • Transcriptional induction of MKP-1 in response to stress is associated with histone H3 phosphorylation-acetylation
    • Li J., Gorospe M., Hutter D., Barnes J., Keyse S.M., and Liu Y. Transcriptional induction of MKP-1 in response to stress is associated with histone H3 phosphorylation-acetylation. Mol. Cell. Biol. 21 (2001) 8213-8224
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8213-8224
    • Li, J.1    Gorospe, M.2    Hutter, D.3    Barnes, J.4    Keyse, S.M.5    Liu, Y.6
  • 37
    • 1642300626 scopus 로고    scopus 로고
    • Stimulated initiation of mitogen-activated protein kinase phosphatase-1 (MKP-1) gene transcription involves the synergistic action of multiple cis-acting elements in the proximal promoter
    • Ryser S., Massiha A., Piuz I., and Schlegel W. Stimulated initiation of mitogen-activated protein kinase phosphatase-1 (MKP-1) gene transcription involves the synergistic action of multiple cis-acting elements in the proximal promoter. Biochem. J. 378 (2004) 473-484
    • (2004) Biochem. J. , vol.378 , pp. 473-484
    • Ryser, S.1    Massiha, A.2    Piuz, I.3    Schlegel, W.4
  • 39
    • 33644767306 scopus 로고    scopus 로고
    • Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways
    • Brook M., Tchen C.R., Santalucia T., McIlrath J., Arthur J.S., Saklatvala J., and Clark A.R. Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways. Mol. Cell. Biol. 26 (2006) 2408-2418
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2408-2418
    • Brook, M.1    Tchen, C.R.2    Santalucia, T.3    McIlrath, J.4    Arthur, J.S.5    Saklatvala, J.6    Clark, A.R.7
  • 40
    • 33644753147 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element
    • Hitti E., Iakovleva T., Brook M., Deppenmeier S., Gruber A.D., Radzioch D., Clark A.R., Blackshear P.J., Kotlyarov A., and Gaestel M. Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element. Mol. Cell. Biol. 26 (2006) 2399-2407
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2399-2407
    • Hitti, E.1    Iakovleva, T.2    Brook, M.3    Deppenmeier, S.4    Gruber, A.D.5    Radzioch, D.6    Clark, A.R.7    Blackshear, P.J.8    Kotlyarov, A.9    Gaestel, M.10
  • 41
    • 0036884621 scopus 로고    scopus 로고
    • Restraint of proinflammatory cytokine biosynthesis by mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages
    • Chen P., Li J., Barnes J., Kokkonen G.C., Lee J.C., and Liu Y. Restraint of proinflammatory cytokine biosynthesis by mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages. J. Immun. 169 (2002) 6408-6416
    • (2002) J. Immun. , vol.169 , pp. 6408-6416
    • Chen, P.1    Li, J.2    Barnes, J.3    Kokkonen, G.C.4    Lee, J.C.5    Liu, Y.6
  • 42
    • 0036841288 scopus 로고    scopus 로고
    • Dexamethasone cause sustained expression of mitogen-activated protein kinase (MAPK) phosphatase 1 and phosphatase-mediated inhibition of MAPK p38
    • Lasa M., Abraham S.M., Boucheron C., Saklatvala J., and Clark A.R. Dexamethasone cause sustained expression of mitogen-activated protein kinase (MAPK) phosphatase 1 and phosphatase-mediated inhibition of MAPK p38. Mol. Cell. Biol. 22 (2002) 7802-7811
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7802-7811
    • Lasa, M.1    Abraham, S.M.2    Boucheron, C.3    Saklatvala, J.4    Clark, A.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.