4.0 Article

Anserine is expressed in human cardiac and skeletal muscles

Journal

PHYSIOLOGICAL REPORTS
Volume 11, Issue 19, Pages -

Publisher

WILEY
DOI: 10.14814/phy2.15833

Keywords

anserine; carnosine-N-methyltransferase; heart; human; muscle

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This study demonstrates the presence of anserine in the human heart ventricle and confirms its low expression in human skeletal muscle.
We evaluated whether anserine, a methylated analog of the dipeptide carnosine, is present in the cardiac and skeletal muscles of humans and whether the CARNMT1 gene, which encodes the anserine synthesizing enzyme carnosine-N-methyltransferase, is expressed in human skeletal muscle. We found that anserine is present at low concentrations (low micromolar range) in both cardiac and skeletal muscles, and that anserine content in skeletal muscle is similar to 15 times higher than in cardiac muscle (cardiac muscle: 10.1 +/- 13.4 mu mol.kg(-1) of dry muscle, n = 12; skeletal muscle: 158.1 +/- 68.5 mu mol.kg(-1) of dry muscle, n = 11, p < 0.0001). Anserine content in the heart was highly variable between individuals, ranging from 1.4 to 45.4 mu mol.kg(-1) of dry muscle, but anserine content was not associated with sex, age, or body mass. We also showed that CARNMT1 gene is poorly expressed in skeletal muscle (n = 10). This is the first study to demonstrate that anserine is present in the ventricle of the human heart. The presence of anserine in human heart and the confirmation of its expression in human skeletal muscle open new avenues of investigation on the specific and differential physiological functions of histidine dipeptides in striated muscles.

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