Open AccessOgfod1 deletion increases cardiac beta-alanine levels and protects mice against ischaemia– reperfusion injury
Author(s) -
Michael Harris,
Junhui Sun,
Karen J. Keeran,
Angel Aponte,
Komudi Singh,
Danielle Springer,
Marjan Guček,
Mehdi Pirooznia,
Matthew E. Cockman,
Elizabeth Murphy,
Leslie Kennedy
Publication year - 2021
Publication title -
cardiovascular research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.774
H-Index - 219
eISSN - 1755-3245
pISSN - 0008-6363
DOI - 10.1093/cvr/cvab323
Subject(s) - inosine , biochemistry , purine , hydroxylation , inosine monophosphate , catabolism , chemistry , pyrimidine metabolism , biology , nucleotide , adenosine , metabolism , enzyme , gene
Prolyl hydroxylation is a post-translational modification that regulates protein stability, turnover, and activity. The proteins that catalyze prolyl hydroxylation belong to the 2-oxoglutarate- and iron-dependent oxygenase family of proteins. 2-oxoglutarate- and iron-dependent oxygenase domain-containing protein 1 (Ogfod1), which hydroxylates a proline in ribosomal protein s23 is a newly described member of this family. The aims of this study were to investigate roles for Ogfod1 in the heart, and in the heart's response to stress.