Rapamycin destabilizes interleukin-3 mRNA in autocrine tumor cells by a mechanism requiring an intact 3' untranslated region.
Identifieur interne : 001A81 ( Main/Exploration ); précédent : 001A80; suivant : 001A82Rapamycin destabilizes interleukin-3 mRNA in autocrine tumor cells by a mechanism requiring an intact 3' untranslated region.
Auteurs : R. Banholzer [Suisse] ; A P Nair ; H H Hirsch ; X F Ming ; C. MoroniSource :
- Molecular and cellular biology [ 0270-7306 ] ; 1997.
Descripteurs français
- KwdFr :
- ARN messager (métabolisme), Amino-acid isomerases (métabolisme), Animaux (MeSH), Antibiotiques antinéoplasiques (métabolisme), Antibiotiques antinéoplasiques (pharmacologie), Cellules cancéreuses en culture (MeSH), Ciclosporine (pharmacologie), Division cellulaire (effets des médicaments et des substances chimiques), Immunosuppresseurs (pharmacologie), Interleukine-3 (génétique), Maturation post-traductionnelle des protéines (MeSH), Polyènes (métabolisme), Polyènes (pharmacologie), Protein-Serine-Threonine Kinases (antagonistes et inhibiteurs), Protéines de liaison au tacrolimus (MeSH), Protéines de liaison à l'ADN (métabolisme), Protéines de transport (métabolisme), Protéines du choc thermique (métabolisme), Ribosomal Protein S6 Kinases (MeSH), Régulation négative (effets des médicaments et des substances chimiques), Sirolimus (MeSH), Sites de fixation (MeSH), Souris (MeSH), Tacrolimus (pharmacologie).
- MESH :
- antagonistes et inhibiteurs : Protein-Serine-Threonine Kinases.
- effets des médicaments et des substances chimiques : Division cellulaire, Régulation négative.
- génétique : Interleukine-3.
- métabolisme : ARN messager, Amino-acid isomerases, Antibiotiques antinéoplasiques, Polyènes, Protéines de liaison à l'ADN, Protéines de transport, Protéines du choc thermique.
- pharmacologie : Antibiotiques antinéoplasiques, Ciclosporine, Immunosuppresseurs, Polyènes, Tacrolimus.
- Animaux, Cellules cancéreuses en culture, Maturation post-traductionnelle des protéines, Protéines de liaison au tacrolimus, Ribosomal Protein S6 Kinases, Sirolimus, Sites de fixation, Souris.
English descriptors
- KwdEn :
- Amino Acid Isomerases (metabolism), Animals (MeSH), Antibiotics, Antineoplastic (metabolism), Antibiotics, Antineoplastic (pharmacology), Binding Sites (MeSH), Carrier Proteins (metabolism), Cell Division (drug effects), Cyclosporine (pharmacology), DNA-Binding Proteins (metabolism), Down-Regulation (drug effects), Heat-Shock Proteins (metabolism), Immunosuppressive Agents (pharmacology), Interleukin-3 (genetics), Mice (MeSH), Polyenes (metabolism), Polyenes (pharmacology), Protein Processing, Post-Translational (MeSH), Protein-Serine-Threonine Kinases (antagonists & inhibitors), RNA, Messenger (metabolism), Ribosomal Protein S6 Kinases (MeSH), Sirolimus (MeSH), Tacrolimus (pharmacology), Tacrolimus Binding Proteins (MeSH), Tumor Cells, Cultured (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Protein-Serine-Threonine Kinases.
- chemical , genetics : Interleukin-3.
- chemical , metabolism : Amino Acid Isomerases, Antibiotics, Antineoplastic, Carrier Proteins, DNA-Binding Proteins, Heat-Shock Proteins, Polyenes, RNA, Messenger.
- chemical , pharmacology : Antibiotics, Antineoplastic, Cyclosporine, Immunosuppressive Agents, Polyenes, Tacrolimus.
- drug effects : Cell Division, Down-Regulation.
- Animals, Binding Sites, Mice, Protein Processing, Post-Translational, Ribosomal Protein S6 Kinases, Sirolimus, Tacrolimus Binding Proteins, Tumor Cells, Cultured.
Abstract
We analyzed the effect of rapamycin on autocrine mast cell tumor lines with abnormally stable interleukin-3 (IL-3) transcripts due to a defect in mRNA degradation. Rapamycin inhibited IL-3 mRNA expression specifically, while transcripts of IL-4 and IL-6 were not affected. As indicated by the use of the transcriptional inhibitor actinomycin D or by reporter constructs, inhibition was posttranscriptional and resulted from destabilization of the mRNA. Transcripts from transgenes lacking the AU-rich 3' untranslated region were refractory to drug-induced degradation, suggesting that these 3' sequences contain the target of the rapamycin effect. Rapamycin did not promote IL-3 mRNA degradation in cells of a tumor variant lacking expression of FKBP12, the binding protein of rapamycin. Experiments with wortmannin indicated that rapamycin does not act via p70S6 kinase. FK-506, another ligand of FKBP12 affecting the phosphatase calcineurin, did not antagonize but shared the effect of rapamycin. Our data fit a model whereby both FKBP12 and calcineurin target an unknown regulator of IL-3 mRNA turnover.
DOI: 10.1128/mcb.17.6.3254
PubMed: 9154824
PubMed Central: PMC232178
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Cyclosporine (pharmacology)</term>
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<term>RNA, Messenger (metabolism)</term>
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<term>Sirolimus (MeSH)</term>
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<term>Antibiotiques antinéoplasiques (pharmacologie)</term>
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<term>Protein-Serine-Threonine Kinases (antagonistes et inhibiteurs)</term>
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<term>Cellules cancéreuses en culture</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Protéines de liaison au tacrolimus</term>
<term>Ribosomal Protein S6 Kinases</term>
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<front><div type="abstract" xml:lang="en">We analyzed the effect of rapamycin on autocrine mast cell tumor lines with abnormally stable interleukin-3 (IL-3) transcripts due to a defect in mRNA degradation. Rapamycin inhibited IL-3 mRNA expression specifically, while transcripts of IL-4 and IL-6 were not affected. As indicated by the use of the transcriptional inhibitor actinomycin D or by reporter constructs, inhibition was posttranscriptional and resulted from destabilization of the mRNA. Transcripts from transgenes lacking the AU-rich 3' untranslated region were refractory to drug-induced degradation, suggesting that these 3' sequences contain the target of the rapamycin effect. Rapamycin did not promote IL-3 mRNA degradation in cells of a tumor variant lacking expression of FKBP12, the binding protein of rapamycin. Experiments with wortmannin indicated that rapamycin does not act via p70S6 kinase. FK-506, another ligand of FKBP12 affecting the phosphatase calcineurin, did not antagonize but shared the effect of rapamycin. Our data fit a model whereby both FKBP12 and calcineurin target an unknown regulator of IL-3 mRNA turnover.</div>
</front>
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<Abstract><AbstractText>We analyzed the effect of rapamycin on autocrine mast cell tumor lines with abnormally stable interleukin-3 (IL-3) transcripts due to a defect in mRNA degradation. Rapamycin inhibited IL-3 mRNA expression specifically, while transcripts of IL-4 and IL-6 were not affected. As indicated by the use of the transcriptional inhibitor actinomycin D or by reporter constructs, inhibition was posttranscriptional and resulted from destabilization of the mRNA. Transcripts from transgenes lacking the AU-rich 3' untranslated region were refractory to drug-induced degradation, suggesting that these 3' sequences contain the target of the rapamycin effect. Rapamycin did not promote IL-3 mRNA degradation in cells of a tumor variant lacking expression of FKBP12, the binding protein of rapamycin. Experiments with wortmannin indicated that rapamycin does not act via p70S6 kinase. FK-506, another ligand of FKBP12 affecting the phosphatase calcineurin, did not antagonize but shared the effect of rapamycin. Our data fit a model whereby both FKBP12 and calcineurin target an unknown regulator of IL-3 mRNA turnover.</AbstractText>
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<ReferenceList><Reference><Citation>Nature. 1991 Aug 29;352(6338):803-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1715516</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Biochem Sci. 1996 May;21(5):181-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8871403</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1986 Feb 20-26;319(6055):640-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3005865</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 1987 Jan 12;15(1):333-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3029676</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Immunol. 1988 Jan 1;140(1):131-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2447167</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Immunol. 1988 Jan;18(1):97-104</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2831066</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1988 Jun 3;53(5):815-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3370673</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Immunol. 1988 Dec 1;141(11):3875-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3263439</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Anal Biochem. 1988 Aug 15;173(1):93-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2461121</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1988 Dec 23;55(6):1115-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3060261</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1989 May 11;339(6220):150-2</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2524008</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1989 Mar;9(3):1183-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2498644</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1989 Dec 1;8(12):3693-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2583116</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1989 Dec;86(23):9299-302</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2512578</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Immunol. 1990 Jan 1;144(1):251-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1688572</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1990 Jan;87(2):777-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2105489</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Growth Factors. 1989;1(2):165-77</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2576219</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Immunol. 1990 Jan;20(1):163-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1968391</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1990 Dec;87(23):9231-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2123553</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1991 Aug 23;66(4):807-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1715244</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Gene. 1991 Dec 30;109(2):255-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1722474</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1992 May;11(5):1743-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1374712</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1992 Jun 25;357(6380):692-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1377361</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1992 Jun 25;357(6380):695-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1377362</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1992 Jul 2;358(6381):70-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1614535</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1992 Jun 26;69(7):1227-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1377606</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1992 Aug 7;70(3):365-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1379518</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1992 Aug 14;257(5072):973-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1380182</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Oncogene. 1992 Oct;7(10):1963-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1408138</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1993 Feb 15;268(5):3734-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8429048</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1993 May 7;73(3):585-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8387896</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Immunol. 1993;53:1-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8512033</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Exp Med. 1993 Aug 1;178(2):403-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8340751</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1993 Oct 25;268(30):22825-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8226793</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1994 May 19;369(6477):239-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8183344</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1994 May 10;91(10):4441-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8183928</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1994 Jun 30;369(6483):756-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8008069</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1994 Jul 15;78(1):35-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7518356</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Blood. 1994 Sep 1;84(5):1543-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7520778</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1994 Nov 18;269(46):28591-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7961806</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1994 Dec;14(12):7984-95</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7969138</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11477-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7972087</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1994 Dec 8;372(6506):570-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7990932</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1995 Apr;15(4):2219-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7891716</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Aug 4;270(31):18531-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7629182</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Sep 1;270(35):20629-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7657642</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Biochem Sci. 1995 Aug;20(8):303-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7667888</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Sep 8;270(36):21396-403</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7545671</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1995 Oct 5;377(6548):441-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7566123</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1995 Sep 28;377(6547):358-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7566093</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Microbiol Rev. 1995 Sep;59(3):423-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7565413</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1995 Nov 3;83(3):463-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8521476</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Biochem Sci. 1995 Nov;20(11):465-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8578590</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1996 Feb 1;15(3):658-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8599949</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Cell Biol. 1995 Dec;7(6):806-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8608011</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4076-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8633019</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1996 Aug 23;86(4):517-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8752206</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Growth Factors. 1996;13(1-2):99-110</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8804994</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Biochem. 1985 Jul 15;150(2):297-304</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3926497</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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