Protein Arginine Methyltransferase 1 Interacts With PGC1α and Modulates Thermogenic Fat Activation.

作者: Xiaona Qiao , Dong-il Kim , Heejin Jun , Yingxu Ma , Alexander J Knights

DOI: 10.1210/EN.2019-00504

关键词:

摘要: Protein arginine methyltransferases (PRMTs) are enzymes that regulate the evolutionarily conserved process of methylation. It has been reported PRMTs involved in many metabolic regulatory pathways. However, until now, their roles adipocyte function, especially browning and thermogenesis, have not evaluated. Even though Prmt1 adipocyte-specific-deleted mice (Prmt1fl/flAQcre) appeared normal at basal level, following cold exposure or β-adrenergic stimulation, impaired induction thermogenic program was observed both interscapular brown adipose tissue inguinal white Prmt1fl/flAQcre compared with littermate controls. Different splicing variants reported. Among them, PRMT1 variant 1 2 (PRMT1V2) well between humans mice. Both contribute to activation fat, PRMT1V2 playing a more dominant role. Mechanistic studies using cultured murine human adipocytes revealed mediates fat through PGC1α, transcriptional coactivator shown play key role mitochondrial biogenesis. To our knowledge, data first demonstrate plays function. These findings suggest modulating activity may represent new avenues mediate energy homeostasis. This function is primary adipocytes, suggesting further investigation this pathway ultimately lead therapeutic strategies against obesity associated disorders.

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