INOS is not responsible for RyR1 S-nitrosylation in mdx mice with truncated dystrophin.

ABSTRACT:

Background

Previous research indicated that nitric oxide synthase (NOS) is the key molecule for S-nitrosylation of ryanodine receptor 1 (RyR1) in DMD model mice (mdx mice) and that both neuronal NOS (nNOS) and inducible NOS (iNOS) might contribute to the reaction because nNOS is mislocalized in the cytoplasm and iNOS expression is higher in mdx mice. We investigated the effect of iNOS on RyR1 S-nitrosylation in mdx mice and whether transgenic expression of truncated dystrophin reduced iNOS expression in mdx mice or not.

Methods

Three- to 4-month-old C57BL/6 J, mdx, and transgenic mdx mice expressing exon 45-55-deleted human dystrophin (Tg/mdx mice) were used. We also generated two double mutant mice, mdx iNOS KO and Tg/mdx iNOS KO to reveal the iNOS contribution to RyR1 S-ni

SUBMITTER: Nogami K 

PROVIDER: S-EPMC7374827 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature