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Transcriptome analysis revealed that PME-1 suppresses inflammatory signaling, activates PI3K/Akt signaling, and promotes epithelial-mesenchymal transition.
Ikeda, Shunta; Sato, Koichi; Ohama, Takashi.
Affiliation
  • Ikeda S; Laboratory of Veterinary Pharmacology, Joint Faculty of Veterinary Medicine, Yamaguchi University, 1677-1 Yoshida, Yamaguchi 753-8515, Japan.
  • Sato K; Laboratory of Veterinary Pharmacology, Joint Faculty of Veterinary Medicine, Yamaguchi University, 1677-1 Yoshida, Yamaguchi 753-8515, Japan.
  • Ohama T; Laboratory of Veterinary Pharmacology, Joint Faculty of Veterinary Medicine, Yamaguchi University, 1677-1 Yoshida, Yamaguchi 753-8515, Japan. Electronic address: t.ohama@yamaguchi-u.ac.jp.
Biochem Biophys Res Commun ; 692: 149148, 2024 Jan 15.
Article in En | MEDLINE | ID: mdl-38043157
ABSTRACT
Protein phosphatase 2A (PP2A) is an essential serine/threonine protein phosphatase that belongs to the type2A protein phosphatase family with PP4 and PP6. PP2A functions as a trimeric holoenzyme, and the composition of the trimer is regulated by the methyl-esterification (methylation) of PP2A. Demethylation of PP2A is catalyzed by protein phosphatase methyl-esterase-1 (PME-1). Despite the physiological and pathophysiological importance of PME-1, the impact of changes in PME-1 expression on the transcriptome has not been reported. This study provides transcriptome data to gain a comprehensive understanding of the effects of PME-1 knockout on intracellular signaling of mouse embryonic fibroblasts. Our data showed that PME-1 suppresses inflammatory signaling, activates PI3K/Akt signaling, and promotes epithelial-mesenchymal transition.
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Full text: 1 Database: MEDLINE Main subject: Phosphatidylinositol 3-Kinases / Proto-Oncogene Proteins c-akt Limits: Animals Language: En Journal: Biochem Biophys Res Commun Year: 2024 Type: Article Affiliation country: Japan

Full text: 1 Database: MEDLINE Main subject: Phosphatidylinositol 3-Kinases / Proto-Oncogene Proteins c-akt Limits: Animals Language: En Journal: Biochem Biophys Res Commun Year: 2024 Type: Article Affiliation country: Japan