PRMT1 mediates RANKL-induced osteoclastogenesis and contributes to bone loss in ovariectomized mice.

Experimental & Molecular Medicine
Joo-Hee ChoiJong-Hwan Park

Abstract

Protein arginine methylation is a novel form of posttranslational modification mediated by protein arginine methyltransferase (PRMTs). PRMT1, a major isoform of the PRMT family, is responsible for various biological functions, including cellular differentiation. Although the important function that PRMT1 plays in various tissues is being increasingly recognized, its role in receptor activation of NF-κB ligand (RANKL)-induced osteoclastogenesis or osteoporosis has not yet been described. Here, we show that PRMT1 is essential for RANKL-induced osteoclastogenesis in vitro and for bone loss in vivo. RANKL treatment increased the expression of PRMT1 and its nuclear localization in bone marrow-derived macrophages (BMDMs) in a c-Jun N-terminal kinase (JNK)-dependent manner. Silencing PRMT1 attenuated RANKL-induced osteoclastogenesis by decreasing tartrate-resistant acid phosphatase (TRAP)-positive cells and inhibiting F-actin ring formation and bone resorption, which was confirmed in a separate experiment using haploinsufficient cells from PRMT1+/- mice. Our results also revealed that PRMT1 regulates the transcription activity of NF-κB by directly interacting with it in RANKL-treated BMDMs. An in vivo study showed that the haploinsuff...Continue Reading

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Citations

Jun 30, 2019·International Journal of Molecular Sciences·Sun-Ju YiKyunghwan Kim
Nov 22, 2019·BMC Complementary and Alternative Medicine·Rui Hong GuoYoung Ran Kim
Oct 1, 2020·International Journal of Molecular Sciences·Kristina AstlefordKim C Mansky

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Methods Mentioned

BETA
genotyping
electrophoresis
transfection
PCR
Enzyme-linked immunosorbent assay
ELISA
Assay
Fluorescence
immunoprecipitation

Software Mentioned

Leica Application Suite Advanced Fluorescence ( LAS AF )
image J
GraphPad Prism
CTAn
Image Reconstruction

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