Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm

Peroxisome proliferator-activated receptors (PPARs) are activated by a variety of fatty acids, eicosanoids, and hypolipidemic and insulin-sensitizing drugs. Many of these compounds bind avidly to members of a family of small lipid-binding proteins, the fatty acid-binding proteins (FABPs). Fatty acid...
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Autor*in:	Torben Helledie [verfasserIn] Marianne Antonius [verfasserIn] Rikke V. Sørensen [verfasserIn] Ann V. Hertzel [verfasserIn] David A. Bernlohr [verfasserIn] Steen Kølvraa [verfasserIn] Karsten Kristiansen [verfasserIn] Susanne Mandrup [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2000

Schlagwörter:	acyl-CoA-binding protein adipocyte differentiation adipocyte lipid-binding protein/a-FABP/aP2 keratinocyte lipid-binding protein/e-FABP/MAL1 tetradecylthioacetic acid

Übergeordnetes Werk:	In: Journal of Lipid Research - Elsevier, 2021, 41(2000), 11, Seite 1740-1751
Übergeordnetes Werk:	volume:41 ; year:2000 ; number:11 ; pages:1740-1751

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/S0022-2275(20)31967-2

Katalog-ID:	DOAJ062245899

Internformat


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allfields	10.1016/S0022-2275(20)31967-2 doi (DE-627)DOAJ062245899 (DE-599)DOAJ9311808824a2433eb72858fa1407b0b4 DE-627 ger DE-627 rakwb eng QD415-436 Torben Helledie verfasserin aut Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peroxisome proliferator-activated receptors (PPARs) are activated by a variety of fatty acids, eicosanoids, and hypolipidemic and insulin-sensitizing drugs. Many of these compounds bind avidly to members of a family of small lipid-binding proteins, the fatty acid-binding proteins (FABPs). Fatty acids are activated to CoA esters, which bind with high affinity to the acyl-CoA-binding protein (ACBP). Thus, the availability of known and potential PPAR ligands may be regulated by lipid-binding proteins. In this report we show by transient transfection of CV-1 cells that coexpression of ACBP and adipocyte lipid-binding protein (ALBP) exerts a ligand- and PPAR subtype-specific attenuation of PPAR-mediated trans-activation, suggesting that lipid-binding proteins, when expressed at high levels, may function as negative regulators of PPAR activation by certain ligands. Expression of ACBP, ALBP, and keratinocyte lipid-binding protein (KLBP) is induced during adipocyte differentiation, a process during which PPARγ plays a prominent role. We present evidence that endogenous ACBP, ALBP, and KLBP not only localize to the cytoplasm but also exhibit a prominent nuclear localization in 3T3-L1 adipocytes. In addition, forced expression of ACBP, ALBP, and KLBP in CV-1 cells resulted in a substantial accumulation of all three proteins in the nucleus. These results suggest that lipid-binding proteins, contrary to the general assumption, may exert their action in the nucleus as well as in the cytoplasm.—Helledie, T., M. Antonius, R. V. Sørensen, A. V. Hertzel, D. A. Bernlohr, S. Kølvraa, K. Kristiansen, and S. Mandrup. Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm. J. Lipid Res. 2000. 41: 1740–1751. acyl-CoA-binding protein adipocyte differentiation adipocyte lipid-binding protein/a-FABP/aP2 keratinocyte lipid-binding protein/e-FABP/MAL1 tetradecylthioacetic acid Biochemistry Marianne Antonius verfasserin aut Rikke V. Sørensen verfasserin aut Ann V. Hertzel verfasserin aut David A. Bernlohr verfasserin aut Steen Kølvraa verfasserin aut Karsten Kristiansen verfasserin aut Susanne Mandrup verfasserin aut In Journal of Lipid Research Elsevier, 2021 41(2000), 11, Seite 1740-1751 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:41 year:2000 number:11 pages:1740-1751 https://doi.org/10.1016/S0022-2275(20)31967-2 kostenfrei https://doaj.org/article/9311808824a2433eb72858fa1407b0b4 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520319672 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 41 2000 11 1740-1751
spelling	10.1016/S0022-2275(20)31967-2 doi (DE-627)DOAJ062245899 (DE-599)DOAJ9311808824a2433eb72858fa1407b0b4 DE-627 ger DE-627 rakwb eng QD415-436 Torben Helledie verfasserin aut Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peroxisome proliferator-activated receptors (PPARs) are activated by a variety of fatty acids, eicosanoids, and hypolipidemic and insulin-sensitizing drugs. Many of these compounds bind avidly to members of a family of small lipid-binding proteins, the fatty acid-binding proteins (FABPs). Fatty acids are activated to CoA esters, which bind with high affinity to the acyl-CoA-binding protein (ACBP). Thus, the availability of known and potential PPAR ligands may be regulated by lipid-binding proteins. In this report we show by transient transfection of CV-1 cells that coexpression of ACBP and adipocyte lipid-binding protein (ALBP) exerts a ligand- and PPAR subtype-specific attenuation of PPAR-mediated trans-activation, suggesting that lipid-binding proteins, when expressed at high levels, may function as negative regulators of PPAR activation by certain ligands. Expression of ACBP, ALBP, and keratinocyte lipid-binding protein (KLBP) is induced during adipocyte differentiation, a process during which PPARγ plays a prominent role. We present evidence that endogenous ACBP, ALBP, and KLBP not only localize to the cytoplasm but also exhibit a prominent nuclear localization in 3T3-L1 adipocytes. In addition, forced expression of ACBP, ALBP, and KLBP in CV-1 cells resulted in a substantial accumulation of all three proteins in the nucleus. These results suggest that lipid-binding proteins, contrary to the general assumption, may exert their action in the nucleus as well as in the cytoplasm.—Helledie, T., M. Antonius, R. V. Sørensen, A. V. Hertzel, D. A. Bernlohr, S. Kølvraa, K. Kristiansen, and S. Mandrup. Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm. J. Lipid Res. 2000. 41: 1740–1751. acyl-CoA-binding protein adipocyte differentiation adipocyte lipid-binding protein/a-FABP/aP2 keratinocyte lipid-binding protein/e-FABP/MAL1 tetradecylthioacetic acid Biochemistry Marianne Antonius verfasserin aut Rikke V. Sørensen verfasserin aut Ann V. Hertzel verfasserin aut David A. Bernlohr verfasserin aut Steen Kølvraa verfasserin aut Karsten Kristiansen verfasserin aut Susanne Mandrup verfasserin aut In Journal of Lipid Research Elsevier, 2021 41(2000), 11, Seite 1740-1751 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:41 year:2000 number:11 pages:1740-1751 https://doi.org/10.1016/S0022-2275(20)31967-2 kostenfrei https://doaj.org/article/9311808824a2433eb72858fa1407b0b4 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520319672 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 41 2000 11 1740-1751
allfields_unstemmed	10.1016/S0022-2275(20)31967-2 doi (DE-627)DOAJ062245899 (DE-599)DOAJ9311808824a2433eb72858fa1407b0b4 DE-627 ger DE-627 rakwb eng QD415-436 Torben Helledie verfasserin aut Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peroxisome proliferator-activated receptors (PPARs) are activated by a variety of fatty acids, eicosanoids, and hypolipidemic and insulin-sensitizing drugs. Many of these compounds bind avidly to members of a family of small lipid-binding proteins, the fatty acid-binding proteins (FABPs). Fatty acids are activated to CoA esters, which bind with high affinity to the acyl-CoA-binding protein (ACBP). Thus, the availability of known and potential PPAR ligands may be regulated by lipid-binding proteins. In this report we show by transient transfection of CV-1 cells that coexpression of ACBP and adipocyte lipid-binding protein (ALBP) exerts a ligand- and PPAR subtype-specific attenuation of PPAR-mediated trans-activation, suggesting that lipid-binding proteins, when expressed at high levels, may function as negative regulators of PPAR activation by certain ligands. Expression of ACBP, ALBP, and keratinocyte lipid-binding protein (KLBP) is induced during adipocyte differentiation, a process during which PPARγ plays a prominent role. We present evidence that endogenous ACBP, ALBP, and KLBP not only localize to the cytoplasm but also exhibit a prominent nuclear localization in 3T3-L1 adipocytes. In addition, forced expression of ACBP, ALBP, and KLBP in CV-1 cells resulted in a substantial accumulation of all three proteins in the nucleus. These results suggest that lipid-binding proteins, contrary to the general assumption, may exert their action in the nucleus as well as in the cytoplasm.—Helledie, T., M. Antonius, R. V. Sørensen, A. V. Hertzel, D. A. Bernlohr, S. Kølvraa, K. Kristiansen, and S. Mandrup. Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm. J. Lipid Res. 2000. 41: 1740–1751. acyl-CoA-binding protein adipocyte differentiation adipocyte lipid-binding protein/a-FABP/aP2 keratinocyte lipid-binding protein/e-FABP/MAL1 tetradecylthioacetic acid Biochemistry Marianne Antonius verfasserin aut Rikke V. Sørensen verfasserin aut Ann V. Hertzel verfasserin aut David A. Bernlohr verfasserin aut Steen Kølvraa verfasserin aut Karsten Kristiansen verfasserin aut Susanne Mandrup verfasserin aut In Journal of Lipid Research Elsevier, 2021 41(2000), 11, Seite 1740-1751 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:41 year:2000 number:11 pages:1740-1751 https://doi.org/10.1016/S0022-2275(20)31967-2 kostenfrei https://doaj.org/article/9311808824a2433eb72858fa1407b0b4 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520319672 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 41 2000 11 1740-1751
allfieldsGer	10.1016/S0022-2275(20)31967-2 doi (DE-627)DOAJ062245899 (DE-599)DOAJ9311808824a2433eb72858fa1407b0b4 DE-627 ger DE-627 rakwb eng QD415-436 Torben Helledie verfasserin aut Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peroxisome proliferator-activated receptors (PPARs) are activated by a variety of fatty acids, eicosanoids, and hypolipidemic and insulin-sensitizing drugs. Many of these compounds bind avidly to members of a family of small lipid-binding proteins, the fatty acid-binding proteins (FABPs). Fatty acids are activated to CoA esters, which bind with high affinity to the acyl-CoA-binding protein (ACBP). Thus, the availability of known and potential PPAR ligands may be regulated by lipid-binding proteins. In this report we show by transient transfection of CV-1 cells that coexpression of ACBP and adipocyte lipid-binding protein (ALBP) exerts a ligand- and PPAR subtype-specific attenuation of PPAR-mediated trans-activation, suggesting that lipid-binding proteins, when expressed at high levels, may function as negative regulators of PPAR activation by certain ligands. Expression of ACBP, ALBP, and keratinocyte lipid-binding protein (KLBP) is induced during adipocyte differentiation, a process during which PPARγ plays a prominent role. We present evidence that endogenous ACBP, ALBP, and KLBP not only localize to the cytoplasm but also exhibit a prominent nuclear localization in 3T3-L1 adipocytes. In addition, forced expression of ACBP, ALBP, and KLBP in CV-1 cells resulted in a substantial accumulation of all three proteins in the nucleus. These results suggest that lipid-binding proteins, contrary to the general assumption, may exert their action in the nucleus as well as in the cytoplasm.—Helledie, T., M. Antonius, R. V. Sørensen, A. V. Hertzel, D. A. Bernlohr, S. Kølvraa, K. Kristiansen, and S. Mandrup. Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm. J. Lipid Res. 2000. 41: 1740–1751. acyl-CoA-binding protein adipocyte differentiation adipocyte lipid-binding protein/a-FABP/aP2 keratinocyte lipid-binding protein/e-FABP/MAL1 tetradecylthioacetic acid Biochemistry Marianne Antonius verfasserin aut Rikke V. Sørensen verfasserin aut Ann V. Hertzel verfasserin aut David A. Bernlohr verfasserin aut Steen Kølvraa verfasserin aut Karsten Kristiansen verfasserin aut Susanne Mandrup verfasserin aut In Journal of Lipid Research Elsevier, 2021 41(2000), 11, Seite 1740-1751 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:41 year:2000 number:11 pages:1740-1751 https://doi.org/10.1016/S0022-2275(20)31967-2 kostenfrei https://doaj.org/article/9311808824a2433eb72858fa1407b0b4 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520319672 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 41 2000 11 1740-1751
allfieldsSound	10.1016/S0022-2275(20)31967-2 doi (DE-627)DOAJ062245899 (DE-599)DOAJ9311808824a2433eb72858fa1407b0b4 DE-627 ger DE-627 rakwb eng QD415-436 Torben Helledie verfasserin aut Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peroxisome proliferator-activated receptors (PPARs) are activated by a variety of fatty acids, eicosanoids, and hypolipidemic and insulin-sensitizing drugs. Many of these compounds bind avidly to members of a family of small lipid-binding proteins, the fatty acid-binding proteins (FABPs). Fatty acids are activated to CoA esters, which bind with high affinity to the acyl-CoA-binding protein (ACBP). Thus, the availability of known and potential PPAR ligands may be regulated by lipid-binding proteins. In this report we show by transient transfection of CV-1 cells that coexpression of ACBP and adipocyte lipid-binding protein (ALBP) exerts a ligand- and PPAR subtype-specific attenuation of PPAR-mediated trans-activation, suggesting that lipid-binding proteins, when expressed at high levels, may function as negative regulators of PPAR activation by certain ligands. Expression of ACBP, ALBP, and keratinocyte lipid-binding protein (KLBP) is induced during adipocyte differentiation, a process during which PPARγ plays a prominent role. We present evidence that endogenous ACBP, ALBP, and KLBP not only localize to the cytoplasm but also exhibit a prominent nuclear localization in 3T3-L1 adipocytes. In addition, forced expression of ACBP, ALBP, and KLBP in CV-1 cells resulted in a substantial accumulation of all three proteins in the nucleus. These results suggest that lipid-binding proteins, contrary to the general assumption, may exert their action in the nucleus as well as in the cytoplasm.—Helledie, T., M. Antonius, R. V. Sørensen, A. V. Hertzel, D. A. Bernlohr, S. Kølvraa, K. Kristiansen, and S. Mandrup. Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm. J. Lipid Res. 2000. 41: 1740–1751. acyl-CoA-binding protein adipocyte differentiation adipocyte lipid-binding protein/a-FABP/aP2 keratinocyte lipid-binding protein/e-FABP/MAL1 tetradecylthioacetic acid Biochemistry Marianne Antonius verfasserin aut Rikke V. Sørensen verfasserin aut Ann V. Hertzel verfasserin aut David A. Bernlohr verfasserin aut Steen Kølvraa verfasserin aut Karsten Kristiansen verfasserin aut Susanne Mandrup verfasserin aut In Journal of Lipid Research Elsevier, 2021 41(2000), 11, Seite 1740-1751 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:41 year:2000 number:11 pages:1740-1751 https://doi.org/10.1016/S0022-2275(20)31967-2 kostenfrei https://doaj.org/article/9311808824a2433eb72858fa1407b0b4 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520319672 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 41 2000 11 1740-1751
language	English
source	In Journal of Lipid Research 41(2000), 11, Seite 1740-1751 volume:41 year:2000 number:11 pages:1740-1751
sourceStr	In Journal of Lipid Research 41(2000), 11, Seite 1740-1751 volume:41 year:2000 number:11 pages:1740-1751
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	acyl-CoA-binding protein adipocyte differentiation adipocyte lipid-binding protein/a-FABP/aP2 keratinocyte lipid-binding protein/e-FABP/MAL1 tetradecylthioacetic acid Biochemistry
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container_title	Journal of Lipid Research
authorswithroles_txt_mv	Torben Helledie @@aut@@ Marianne Antonius @@aut@@ Rikke V. Sørensen @@aut@@ Ann V. Hertzel @@aut@@ David A. Bernlohr @@aut@@ Steen Kølvraa @@aut@@ Karsten Kristiansen @@aut@@ Susanne Mandrup @@aut@@
publishDateDaySort_date	2000-01-01T00:00:00Z
hierarchy_top_id	26601593X
id	DOAJ062245899
language_de	englisch
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callnumber-first	Q - Science
author	Torben Helledie
spellingShingle	Torben Helledie misc QD415-436 misc acyl-CoA-binding protein misc adipocyte differentiation misc adipocyte lipid-binding protein/a-FABP/aP2 misc keratinocyte lipid-binding protein/e-FABP/MAL1 misc tetradecylthioacetic acid misc Biochemistry Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm
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topic_title	QD415-436 Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm acyl-CoA-binding protein adipocyte differentiation adipocyte lipid-binding protein/a-FABP/aP2 keratinocyte lipid-binding protein/e-FABP/MAL1 tetradecylthioacetic acid
topic	misc QD415-436 misc acyl-CoA-binding protein misc adipocyte differentiation misc adipocyte lipid-binding protein/a-FABP/aP2 misc keratinocyte lipid-binding protein/e-FABP/MAL1 misc tetradecylthioacetic acid misc Biochemistry
topic_unstemmed	misc QD415-436 misc acyl-CoA-binding protein misc adipocyte differentiation misc adipocyte lipid-binding protein/a-FABP/aP2 misc keratinocyte lipid-binding protein/e-FABP/MAL1 misc tetradecylthioacetic acid misc Biochemistry
topic_browse	misc QD415-436 misc acyl-CoA-binding protein misc adipocyte differentiation misc adipocyte lipid-binding protein/a-FABP/aP2 misc keratinocyte lipid-binding protein/e-FABP/MAL1 misc tetradecylthioacetic acid misc Biochemistry
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title	Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm
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title_full	Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm
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author_browse	Torben Helledie Marianne Antonius Rikke V. Sørensen Ann V. Hertzel David A. Bernlohr Steen Kølvraa Karsten Kristiansen Susanne Mandrup
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title_sort	lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm
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title_auth	Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm
abstract	Peroxisome proliferator-activated receptors (PPARs) are activated by a variety of fatty acids, eicosanoids, and hypolipidemic and insulin-sensitizing drugs. Many of these compounds bind avidly to members of a family of small lipid-binding proteins, the fatty acid-binding proteins (FABPs). Fatty acids are activated to CoA esters, which bind with high affinity to the acyl-CoA-binding protein (ACBP). Thus, the availability of known and potential PPAR ligands may be regulated by lipid-binding proteins. In this report we show by transient transfection of CV-1 cells that coexpression of ACBP and adipocyte lipid-binding protein (ALBP) exerts a ligand- and PPAR subtype-specific attenuation of PPAR-mediated trans-activation, suggesting that lipid-binding proteins, when expressed at high levels, may function as negative regulators of PPAR activation by certain ligands. Expression of ACBP, ALBP, and keratinocyte lipid-binding protein (KLBP) is induced during adipocyte differentiation, a process during which PPARγ plays a prominent role. We present evidence that endogenous ACBP, ALBP, and KLBP not only localize to the cytoplasm but also exhibit a prominent nuclear localization in 3T3-L1 adipocytes. In addition, forced expression of ACBP, ALBP, and KLBP in CV-1 cells resulted in a substantial accumulation of all three proteins in the nucleus. These results suggest that lipid-binding proteins, contrary to the general assumption, may exert their action in the nucleus as well as in the cytoplasm.—Helledie, T., M. Antonius, R. V. Sørensen, A. V. Hertzel, D. A. Bernlohr, S. Kølvraa, K. Kristiansen, and S. Mandrup. Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm. J. Lipid Res. 2000. 41: 1740–1751.
abstractGer	Peroxisome proliferator-activated receptors (PPARs) are activated by a variety of fatty acids, eicosanoids, and hypolipidemic and insulin-sensitizing drugs. Many of these compounds bind avidly to members of a family of small lipid-binding proteins, the fatty acid-binding proteins (FABPs). Fatty acids are activated to CoA esters, which bind with high affinity to the acyl-CoA-binding protein (ACBP). Thus, the availability of known and potential PPAR ligands may be regulated by lipid-binding proteins. In this report we show by transient transfection of CV-1 cells that coexpression of ACBP and adipocyte lipid-binding protein (ALBP) exerts a ligand- and PPAR subtype-specific attenuation of PPAR-mediated trans-activation, suggesting that lipid-binding proteins, when expressed at high levels, may function as negative regulators of PPAR activation by certain ligands. Expression of ACBP, ALBP, and keratinocyte lipid-binding protein (KLBP) is induced during adipocyte differentiation, a process during which PPARγ plays a prominent role. We present evidence that endogenous ACBP, ALBP, and KLBP not only localize to the cytoplasm but also exhibit a prominent nuclear localization in 3T3-L1 adipocytes. In addition, forced expression of ACBP, ALBP, and KLBP in CV-1 cells resulted in a substantial accumulation of all three proteins in the nucleus. These results suggest that lipid-binding proteins, contrary to the general assumption, may exert their action in the nucleus as well as in the cytoplasm.—Helledie, T., M. Antonius, R. V. Sørensen, A. V. Hertzel, D. A. Bernlohr, S. Kølvraa, K. Kristiansen, and S. Mandrup. Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm. J. Lipid Res. 2000. 41: 1740–1751.
abstract_unstemmed	Peroxisome proliferator-activated receptors (PPARs) are activated by a variety of fatty acids, eicosanoids, and hypolipidemic and insulin-sensitizing drugs. Many of these compounds bind avidly to members of a family of small lipid-binding proteins, the fatty acid-binding proteins (FABPs). Fatty acids are activated to CoA esters, which bind with high affinity to the acyl-CoA-binding protein (ACBP). Thus, the availability of known and potential PPAR ligands may be regulated by lipid-binding proteins. In this report we show by transient transfection of CV-1 cells that coexpression of ACBP and adipocyte lipid-binding protein (ALBP) exerts a ligand- and PPAR subtype-specific attenuation of PPAR-mediated trans-activation, suggesting that lipid-binding proteins, when expressed at high levels, may function as negative regulators of PPAR activation by certain ligands. Expression of ACBP, ALBP, and keratinocyte lipid-binding protein (KLBP) is induced during adipocyte differentiation, a process during which PPARγ plays a prominent role. We present evidence that endogenous ACBP, ALBP, and KLBP not only localize to the cytoplasm but also exhibit a prominent nuclear localization in 3T3-L1 adipocytes. In addition, forced expression of ACBP, ALBP, and KLBP in CV-1 cells resulted in a substantial accumulation of all three proteins in the nucleus. These results suggest that lipid-binding proteins, contrary to the general assumption, may exert their action in the nucleus as well as in the cytoplasm.—Helledie, T., M. Antonius, R. V. Sørensen, A. V. Hertzel, D. A. Bernlohr, S. Kølvraa, K. Kristiansen, and S. Mandrup. Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm. J. Lipid Res. 2000. 41: 1740–1751.
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title_short	Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm
url	https://doi.org/10.1016/S0022-2275(20)31967-2 https://doaj.org/article/9311808824a2433eb72858fa1407b0b4 http://www.sciencedirect.com/science/article/pii/S0022227520319672 https://doaj.org/toc/0022-2275
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Lipid-binding proteins modulate ligand-dependent trans-activation by peroxisome proliferator-activated receptors and localize to the nucleus as well as the cytoplasm

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