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Protein Arginine Methyltransferases in Cardiovascular and Neuronal Function.
Couto E Silva, Alexandre; Wu, Celeste Yin-Chieh; Citadin, Cristiane T; Clemons, Garrett A; Possoit, HarLee E; Grames, Mychal S; Lien, Chih-Feng; Minagar, Alireza; Lee, Reggie Hui-Chao; Frankel, Adam; Lin, Hung Wen.
Affiliation
  • Couto E Silva A; Department of Cellular Biology & Anatomy, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
  • Wu CY; Department of Neurology, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
  • Citadin CT; Department of Cellular Biology & Anatomy, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
  • Clemons GA; Department of Cellular Biology & Anatomy, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
  • Possoit HE; Department of Neurology, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
  • Grames MS; Department of Pharmacology, Toxicology, and Neuroscience, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
  • Lien CF; Department of Neurology, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
  • Minagar A; Department of Neurology, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
  • Lee RH; Department of Neurology, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
  • Frankel A; Faculty of Pharmaceutical Sciences, The University of British Columbia, Vancouver, British Columbia, Canada.
  • Lin HW; Department of Cellular Biology & Anatomy, Louisiana State University Health Sciences Center, Shreveport, LA, USA. hlin2@lsuhsc.edu.
Mol Neurobiol ; 57(3): 1716-1732, 2020 Mar.
Article de En | MEDLINE | ID: mdl-31823198
ABSTRACT
The methylation of arginine residues by protein arginine methyltransferases (PRMTs) is a type of post-translational modification which is important for numerous cellular processes, including mRNA splicing, DNA repair, signal transduction, protein interaction, and transport. PRMTs have been extensively associated with various pathologies, including cancer, inflammation, and immunity response. However, the role of PRMTs has not been well described in vascular and neurological function. Aberrant expression of PRMTs can alter its metabolic products, asymmetric dimethylarginine (ADMA), and symmetric dimethylarginine (SDMA). Increased ADMA levels are recognized as an independent risk factor for cardiovascular disease and mortality. Recent studies have provided considerable advances in the development of small-molecule inhibitors of PRMTs to study their function under normal and pathological states. In this review, we aim to elucidate the particular roles of PRMTs in vascular and neuronal function as a potential target for cardiovascular and neurological diseases.
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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Arginine / Protein-arginine N-methyltransferases / Maladies cardiovasculaires / Système cardiovasculaire Type d'étude: Risk_factors_studies Limites: Animals / Humans Langue: En Journal: Mol Neurobiol Sujet du journal: BIOLOGIA MOLECULAR / NEUROLOGIA Année: 2020 Type de document: Article Pays d'affiliation: États-Unis d'Amérique

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Arginine / Protein-arginine N-methyltransferases / Maladies cardiovasculaires / Système cardiovasculaire Type d'étude: Risk_factors_studies Limites: Animals / Humans Langue: En Journal: Mol Neurobiol Sujet du journal: BIOLOGIA MOLECULAR / NEUROLOGIA Année: 2020 Type de document: Article Pays d'affiliation: États-Unis d'Amérique