A5064998487- Cancer-related gene regulation
- Epigenetics and DNA Methylation
- Tryptophan and brain disorders
- Neuroinflammation and Neurodegeneration Mechanisms
- RNA modifications and cancer
- Plant Molecular Biology Research
- Adipokines, Inflammation, and Metabolic Diseases
- Plant tissue culture and regeneration
- Biological Stains and Phytochemicals
- Diet, Metabolism, and Disease
- Signaling Pathways in Disease
- Regulation of Appetite and Obesity
- Stress Responses and Cortisol
The Ohio State University
2019-2023
Institute for Behavioral Medicine
2019-2023
The Ohio State University Wexner Medical Center
2019-2020
Protein arginine methyltransferase 5 (PRMT5) catalyzes symmetric dimethylation (SDM) of arginine, a posttranslational modification involved in oncogenesis and embryonic development. However, the role mechanisms by which PRMT5 modulates Th cell polarization autoimmune disease have not yet been elucidated. Here, we found that promoted SREBP1 SDM induction cholesterol biosynthetic pathway enzymes produce retinoid-related orphan receptor (ROR) agonists activate RORγt. Specific loss CD4+...
Multiple sclerosis is an autoimmune disease of the central nervous system (CNS) mediated by CD4+ T cells and modeled via experimental encephalomyelitis (EAE). Inhibition PRMT5, major Type II arginine methyltransferase, suppresses pathogenic cell responses EAE. PRMT5 transiently induced in proliferating memory inflammatory Th1 during However, mechanisms driving protein induction repression as expand return to resting currently unknown. Here, we used naive mouse human Th1/Th2 models identify...
Protein arginine methyltransferase (PRMT) 5 is the type 2 catalyzing symmetric dimethylation of arginine. PRMT5 inhibition or deletion in CD4 Th cells reduces TCR engagement-induced IL-2 production and cell expansion confers protection against experimental autoimmune encephalomyelitis, animal model multiple sclerosis. However, mechanisms by which modulates proliferation are still not completely understood, neither methylation targets T cells. In this manuscript, we uncover role on...
Abstract Protein Arginine Methyltransferase (PRMT) 5 catalyzes symmetric dimethylation of arginine, a post-translational modification involved in cancer and embryonic development. However, the role PRMT5 T helper (Th) cell polarization Th cell-mediated disease has not yet been elucidated. Here we report that is necessary for Th17 differentiation EAE, via enhancement cholesterol biosynthesis activation ROR-γt. additionally controls thymic peripheral homeostasis CD4 life cycle, as well iNK CD8...
Abstract Severe asthma affects 2.4 million Americans and 23.8 people worldwide accounts for the majority of total hospital costs. Most severe is mediated by Th17/neutrophilic responses, alone or combined with Th2 and/or Th1 responses. In contrast, Treg responses are deficient. Protein Arginine Methyl Transferase (PRMT) 5 catalyzes symmetric dimethylation (SDM) arginine on histones other proteins, thereby regulating gene expression. PRMT5 promotes murine Th1/Th17 in central nervous system...
Abstract PRMT5 catalyzes symmetric dimethylation (SDM) on arginine residues. methylates histone H3 and H4 producing remodeling of chromatin regulation gene transcription. is induced after T cell activation. Furthermore, both inhibitors knockdown impair proliferation However, the role in differentiation has not been analyzed. cells undergo metabolic reprograming during activation which critical for polarization. Differentiating increase bioenergetics anabolic pathways enhancing glycolysis,...
Abstract Protein Arginine Methyltransferase (PRMT) 5 is the major type 2 methyltransferase catalyzing symmetric dimethylation (SDM) of arginine. PRMT5 inhibition or deletion in CD4 Th cells reduces TcR engagement-induced IL-2 production and cell expansion confers protection against experimental autoimmune encephalomyelitis (EAE), animal model Multiple Sclerosis. However, mechanisms by which modulates T helper (Th) proliferation are still not completely understood neither methylation targets...