Cargando…

TDP-43 regulates cholesterol biosynthesis by inhibiting sterol regulatory element-binding protein 2

Dyslipidemia is considered an essential component of the pathological process of amyotrophic lateral sclerosis (ALS), a fatal motor neuron disease. Although TAR DNA Binding Protein 43 kDa (TDP-43) links both familial and sporadic forms of ALS and cytoplasmic aggregates are a hallmark of most cases o...

Descripción completa

Detalles Bibliográficos
Autores principales: Egawa, Naohiro, Izumi, Yuishin, Suzuki, Hidefumi, Tsuge, Itaru, Fujita, Koji, Shimano, Hitoshi, Izumikawa, Keiichi, Takahashi, Nobuhiro, Tsukita, Kayoko, Enami, Takako, Nakamura, Masahiro, Watanabe, Akira, Naitoh, Motoko, Suzuki, Shigehiko, Seki, Tsuneyoshi, Kobayashi, Kazuhiro, Toda, Tatsushi, Kaji, Ryuji, Takahashi, Ryosuke, Inoue, Haruhisa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9107471/
https://www.ncbi.nlm.nih.gov/pubmed/35568729
http://dx.doi.org/10.1038/s41598-022-12133-4
_version_ 1784708499130810368
author Egawa, Naohiro
Izumi, Yuishin
Suzuki, Hidefumi
Tsuge, Itaru
Fujita, Koji
Shimano, Hitoshi
Izumikawa, Keiichi
Takahashi, Nobuhiro
Tsukita, Kayoko
Enami, Takako
Nakamura, Masahiro
Watanabe, Akira
Naitoh, Motoko
Suzuki, Shigehiko
Seki, Tsuneyoshi
Kobayashi, Kazuhiro
Toda, Tatsushi
Kaji, Ryuji
Takahashi, Ryosuke
Inoue, Haruhisa
author_facet Egawa, Naohiro
Izumi, Yuishin
Suzuki, Hidefumi
Tsuge, Itaru
Fujita, Koji
Shimano, Hitoshi
Izumikawa, Keiichi
Takahashi, Nobuhiro
Tsukita, Kayoko
Enami, Takako
Nakamura, Masahiro
Watanabe, Akira
Naitoh, Motoko
Suzuki, Shigehiko
Seki, Tsuneyoshi
Kobayashi, Kazuhiro
Toda, Tatsushi
Kaji, Ryuji
Takahashi, Ryosuke
Inoue, Haruhisa
author_sort Egawa, Naohiro
collection PubMed
description Dyslipidemia is considered an essential component of the pathological process of amyotrophic lateral sclerosis (ALS), a fatal motor neuron disease. Although TAR DNA Binding Protein 43 kDa (TDP-43) links both familial and sporadic forms of ALS and cytoplasmic aggregates are a hallmark of most cases of ALS, the molecular mechanism and the in vivo relation of ALS dyslipidemia with TDP-43 have been unclear. To analyze the dyslipidemia-related gene expression by TDP-43, we performed expression microarray and RNA deep sequencing (RNA-Seq) using cell lines expressing high levels of TDP-43 and identified 434 significantly altered genes including sterol regulatory element-binding protein 2 (SREBP2), a master regulator of cholesterol homeostasis and its downstream genes. Elevated TDP-43 impaired SREBP2 transcriptional activity, leading to inhibition of cholesterol biosynthesis. The amount of cholesterol was significantly decreased in the spinal cords of TDP-43-overexpressed ALS model mice and in the cerebrospinal fluids of ALS patients. These results suggested that TDP-43 could play an essential role in cholesterol biosynthesis in relation to ALS dyslipidemia.
format Online
Article
Text
id pubmed-9107471
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-91074712022-05-16 TDP-43 regulates cholesterol biosynthesis by inhibiting sterol regulatory element-binding protein 2 Egawa, Naohiro Izumi, Yuishin Suzuki, Hidefumi Tsuge, Itaru Fujita, Koji Shimano, Hitoshi Izumikawa, Keiichi Takahashi, Nobuhiro Tsukita, Kayoko Enami, Takako Nakamura, Masahiro Watanabe, Akira Naitoh, Motoko Suzuki, Shigehiko Seki, Tsuneyoshi Kobayashi, Kazuhiro Toda, Tatsushi Kaji, Ryuji Takahashi, Ryosuke Inoue, Haruhisa Sci Rep Article Dyslipidemia is considered an essential component of the pathological process of amyotrophic lateral sclerosis (ALS), a fatal motor neuron disease. Although TAR DNA Binding Protein 43 kDa (TDP-43) links both familial and sporadic forms of ALS and cytoplasmic aggregates are a hallmark of most cases of ALS, the molecular mechanism and the in vivo relation of ALS dyslipidemia with TDP-43 have been unclear. To analyze the dyslipidemia-related gene expression by TDP-43, we performed expression microarray and RNA deep sequencing (RNA-Seq) using cell lines expressing high levels of TDP-43 and identified 434 significantly altered genes including sterol regulatory element-binding protein 2 (SREBP2), a master regulator of cholesterol homeostasis and its downstream genes. Elevated TDP-43 impaired SREBP2 transcriptional activity, leading to inhibition of cholesterol biosynthesis. The amount of cholesterol was significantly decreased in the spinal cords of TDP-43-overexpressed ALS model mice and in the cerebrospinal fluids of ALS patients. These results suggested that TDP-43 could play an essential role in cholesterol biosynthesis in relation to ALS dyslipidemia. Nature Publishing Group UK 2022-05-14 /pmc/articles/PMC9107471/ /pubmed/35568729 http://dx.doi.org/10.1038/s41598-022-12133-4 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Egawa, Naohiro
Izumi, Yuishin
Suzuki, Hidefumi
Tsuge, Itaru
Fujita, Koji
Shimano, Hitoshi
Izumikawa, Keiichi
Takahashi, Nobuhiro
Tsukita, Kayoko
Enami, Takako
Nakamura, Masahiro
Watanabe, Akira
Naitoh, Motoko
Suzuki, Shigehiko
Seki, Tsuneyoshi
Kobayashi, Kazuhiro
Toda, Tatsushi
Kaji, Ryuji
Takahashi, Ryosuke
Inoue, Haruhisa
TDP-43 regulates cholesterol biosynthesis by inhibiting sterol regulatory element-binding protein 2
title TDP-43 regulates cholesterol biosynthesis by inhibiting sterol regulatory element-binding protein 2
title_full TDP-43 regulates cholesterol biosynthesis by inhibiting sterol regulatory element-binding protein 2
title_fullStr TDP-43 regulates cholesterol biosynthesis by inhibiting sterol regulatory element-binding protein 2
title_full_unstemmed TDP-43 regulates cholesterol biosynthesis by inhibiting sterol regulatory element-binding protein 2
title_short TDP-43 regulates cholesterol biosynthesis by inhibiting sterol regulatory element-binding protein 2
title_sort tdp-43 regulates cholesterol biosynthesis by inhibiting sterol regulatory element-binding protein 2
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9107471/
https://www.ncbi.nlm.nih.gov/pubmed/35568729
http://dx.doi.org/10.1038/s41598-022-12133-4
work_keys_str_mv AT egawanaohiro tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT izumiyuishin tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT suzukihidefumi tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT tsugeitaru tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT fujitakoji tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT shimanohitoshi tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT izumikawakeiichi tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT takahashinobuhiro tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT tsukitakayoko tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT enamitakako tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT nakamuramasahiro tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT watanabeakira tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT naitohmotoko tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT suzukishigehiko tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT sekitsuneyoshi tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT kobayashikazuhiro tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT todatatsushi tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT kajiryuji tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT takahashiryosuke tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2
AT inoueharuhisa tdp43regulatescholesterolbiosynthesisbyinhibitingsterolregulatoryelementbindingprotein2