FABP7 Regulates Acetyl-CoA Metabolism Through the Interaction with ACLY in the Nucleus of Astrocytes
Fatty acid binding protein 7 (FABP7) is an intracellular fatty acid chaperon that is highly expressed in astrocytes, oligodendrocyte-precursor cells, and malignant glioma. Previously, we reported that FABP7 regulates the response to extracellular stimuli by controlling the expression of caveolin-1,...
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| Veröffentlicht in: | Molecular neurobiology 2020-12, Vol.57 (12), p.4891-4910 |
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| creator | Kagawa, Yoshiteru Umaru, Banlanjo Abdulaziz Shima, Hiroki Ito, Ryo Zama, Ryo Islam, Ariful Kanno, Shin-ichiro Yasui, Akira Sato, Shun Jozaki, Kosuke Shil, Subrata Kumar Miyazaki, Hirofumi Kobayashi, Shuhei Yamamoto, Yui Kogo, Hiroshi Shimamoto-Mitsuyama, Chie Sugawara, Akira Sugino, Norihiro Kanamori, Masayuki Tominaga, Teiji Yoshikawa, Takeo Fukunaga, Kohji Igarashi, Kazuhiko Owada, Yuji |
| description | Fatty acid binding protein 7 (FABP7) is an intracellular fatty acid chaperon that is highly expressed in astrocytes, oligodendrocyte-precursor cells, and malignant glioma. Previously, we reported that FABP7 regulates the response to extracellular stimuli by controlling the expression of caveolin-1, an important component of lipid raft. Here, we explored the detailed mechanisms underlying FABP7 regulation of caveolin-1 expression using primary cultured FABP7-KO astrocytes as a model of loss of function and NIH-3T3 cells as a model of gain of function. We discovered that FABP7 interacts with ATP-citrate lyase (ACLY) and is important for acetyl-CoA metabolism in the nucleus. This interaction leads to epigenetic regulation of several genes, including caveolin-1. Our novel findings suggest that FABP7-ACLY modulation of nuclear acetyl-CoA has more influence on histone acetylation than cytoplasmic acetyl-CoA. The changes to histone structure may modify caveolae-related cell activity in astrocytes and tumors, including malignant glioma. |
| doi_str_mv | 10.1007/s12035-020-02057-3 |
| format | Article |
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Previously, we reported that FABP7 regulates the response to extracellular stimuli by controlling the expression of caveolin-1, an important component of lipid raft. Here, we explored the detailed mechanisms underlying FABP7 regulation of caveolin-1 expression using primary cultured FABP7-KO astrocytes as a model of loss of function and NIH-3T3 cells as a model of gain of function. We discovered that FABP7 interacts with ATP-citrate lyase (ACLY) and is important for acetyl-CoA metabolism in the nucleus. This interaction leads to epigenetic regulation of several genes, including caveolin-1. Our novel findings suggest that FABP7-ACLY modulation of nuclear acetyl-CoA has more influence on histone acetylation than cytoplasmic acetyl-CoA. The changes to histone structure may modify caveolae-related cell activity in astrocytes and tumors, including malignant glioma.</description><identifier>ISSN: 0893-7648</identifier><identifier>EISSN: 1559-1182</identifier><identifier>DOI: 10.1007/s12035-020-02057-3</identifier><identifier>PMID: 32812201</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Acetylation ; Astrocytes ; ATP citrate lyase ; Biomedical and Life Sciences ; Biomedicine ; Biosynthesis ; Brain tumors ; Cancer ; Caveolae ; Caveolin ; Caveolin-1 ; Cell Biology ; Cytoplasm ; Dehydrogenases ; DNA methylation ; Enzymes ; Epigenetics ; Fatty acid-binding protein ; Fatty acids ; Gene regulation ; Genes ; Glioma ; Glioma cells ; Histones ; Laboratories ; Lipids ; Medicine ; Metabolism ; Metabolites ; Neurobiology ; Neurology ; Neurosciences ; Oxidation ; Proteins ; Transcription factors ; University graduates</subject><ispartof>Molecular neurobiology, 2020-12, Vol.57 (12), p.4891-4910</ispartof><rights>The Author(s) 2020</rights><rights>The Author(s) 2020. 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Previously, we reported that FABP7 regulates the response to extracellular stimuli by controlling the expression of caveolin-1, an important component of lipid raft. Here, we explored the detailed mechanisms underlying FABP7 regulation of caveolin-1 expression using primary cultured FABP7-KO astrocytes as a model of loss of function and NIH-3T3 cells as a model of gain of function. We discovered that FABP7 interacts with ATP-citrate lyase (ACLY) and is important for acetyl-CoA metabolism in the nucleus. This interaction leads to epigenetic regulation of several genes, including caveolin-1. Our novel findings suggest that FABP7-ACLY modulation of nuclear acetyl-CoA has more influence on histone acetylation than cytoplasmic acetyl-CoA. The changes to histone structure may modify caveolae-related cell activity in astrocytes and tumors, including malignant glioma.</description><subject>Acetylation</subject><subject>Astrocytes</subject><subject>ATP citrate lyase</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Biosynthesis</subject><subject>Brain tumors</subject><subject>Cancer</subject><subject>Caveolae</subject><subject>Caveolin</subject><subject>Caveolin-1</subject><subject>Cell Biology</subject><subject>Cytoplasm</subject><subject>Dehydrogenases</subject><subject>DNA methylation</subject><subject>Enzymes</subject><subject>Epigenetics</subject><subject>Fatty acid-binding protein</subject><subject>Fatty acids</subject><subject>Gene regulation</subject><subject>Genes</subject><subject>Glioma</subject><subject>Glioma 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astrocytes, oligodendrocyte-precursor cells, and malignant glioma. Previously, we reported that FABP7 regulates the response to extracellular stimuli by controlling the expression of caveolin-1, an important component of lipid raft. Here, we explored the detailed mechanisms underlying FABP7 regulation of caveolin-1 expression using primary cultured FABP7-KO astrocytes as a model of loss of function and NIH-3T3 cells as a model of gain of function. We discovered that FABP7 interacts with ATP-citrate lyase (ACLY) and is important for acetyl-CoA metabolism in the nucleus. This interaction leads to epigenetic regulation of several genes, including caveolin-1. Our novel findings suggest that FABP7-ACLY modulation of nuclear acetyl-CoA has more influence on histone acetylation than cytoplasmic acetyl-CoA. 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| subjects | Acetylation Astrocytes ATP citrate lyase Biomedical and Life Sciences Biomedicine Biosynthesis Brain tumors Cancer Caveolae Caveolin Caveolin-1 Cell Biology Cytoplasm Dehydrogenases DNA methylation Enzymes Epigenetics Fatty acid-binding protein Fatty acids Gene regulation Genes Glioma Glioma cells Histones Laboratories Lipids Medicine Metabolism Metabolites Neurobiology Neurology Neurosciences Oxidation Proteins Transcription factors University graduates |
| title | FABP7 Regulates Acetyl-CoA Metabolism Through the Interaction with ACLY in the Nucleus of Astrocytes |
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