L-arginine dependence of breast cancer - molecular subtypes matter.

ABSTRACT: L-arginine limits proliferation in highly proliferative tissues. It is a substrate for nitric oxide synthases, arginases; its methylation by protein-L-arginine methyltransferases (PRMTs) leads to asymmetric (ADMA) and symmetric dimethylarginine (SDMA). We measured L-arginine and its metabolites L-ornithine, L-citrulline, ADMA, and SDMA in a prospective cohort of 243 women with primary breast cancer (BC) and their associations with mortality and disease recurrence during 88 (IQR, 82-93) months of follow-up. We quantified these metabolites and expression of genes involved in L-arginine metabolic pathways in MCF-7, BT-474, SK-BR-3, MDA-MB-231, and MDA-MB-468 cells representing ER-positive, HER2-positive, and triple-negative BC compared to MCF-12 A cells. Plasma L-arginine and ADMA concentrati

SUBMITTER: Hannemann J 

PROVIDER: S-EPMC11948839 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature