Anserine is expressed in human cardiac and skeletal muscles

Author:

de Souza Gonçalves Lívia12,Pereira Wagner Ribeiro1ORCID,da Silva Rafael Pires1,Yamaguchi Guilherme Carvalho1,Carvalho Victor Henrique3,Vargas Bianca Scigliano3,Jensen Leonardo4,de Medeiros Marisa Helena Gennari3,Roschel Hamilton1,Artioli Guilherme Giannini5ORCID

Affiliation:

1. Applied Physiology & Nutrition Research Group—Center of Lifestyle, Faculdade de Medicina Universidade de São Paulo São Paulo Brazil

2. Division of Pediatrics Department of Pediatrics University of California San Francisco California USA

3. Departamento de Bioquímica, Instituto de Química Universidade de São Paulo São Paulo Brasil

4. Laboratorio de Hipertensao do Instituto do Coraçao do Hospital das Clínicas da Faculdade de Medicina da Universidade São Paulo São Paulo Brazil

5. Department of Life Sciences Manchester Metropolitan University Manchester UK

Abstract

AbstractWe 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 ~15 times higher than in cardiac muscle (cardiac muscle: 10.1 ± 13.4 μmol·kg−1 of dry muscle, n = 12; skeletal muscle: 158.1 ± 68.5 μmol·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 μmol·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.

Funder

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior

Fundação de Amparo à Pesquisa do Estado de São Paulo

Publisher

Wiley

Subject

Physiology (medical),Physiology

Reference37 articles.

1. Role of histidine‐related compounds as intracellular proton buffering constituents in vertebrate muscle;Abe H.;Biochemistry (Mosc),2000

2. Role of histidine‐related compounds to intracellular buffering in fish skeletal muscle;Abe H.;The American Journal of Physiology,1985

3. Histidine-containing dipeptides as endogenous regulators of the activity of sarcoplasmic reticulum Ca-release channels

4. Biosynthesis of carnosine and related peptides by skeletal muscle cells in primary culture

5. Structural Elucidation of a Carnosine-Acrolein Adduct and its Quantification in Human Urine Samples

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