Abstract Title:

Carnosine protects cardiac myocytes against lipid peroxidation products.

Abstract Source:

Amino Acids. 2019 Jan ;51(1):123-138. Epub 2018 Nov 17. PMID: 30449006

Abstract Author(s):

Jingjing Zhao, Dheeraj Kumar Posa, Vijay Kumar, David Hoetker, Amit Kumar, Smirthy Ganesan, Daniel W Riggs, Aruni Bhatnagar, Michael F Wempe, Shahid P Baba

Article Affiliation:

Jingjing Zhao


Endogenous histidyl dipeptides such as carnosine (β-alanine-L-histidine) form conjugates with lipid peroxidation products such as 4-hydroxy-trans-2-nonenal (HNE and acrolein), chelate metals, and protect against myocardial ischemic injury. Nevertheless, it is unclear whether these peptides protect against cardiac injury by directly reacting with lipid peroxidation products. Hence, to examine whether changes in the structure of carnosine could affect its aldehyde reactivity and metal chelating ability, we synthesized methylated analogs of carnosine, balenine (β-alanine-N-methylhistidine) and dimethyl balenine (DMB), and measured their aldehyde reactivity and metal chelating properties. We found that methylation of Nresidue of imidazole ring (balenine) or trimethylation of carnosine backbone at Nresidue of imidazole ring and terminal amine group dimethyl balenine (DMB) abolishes the ability of these peptides to react with HNE. Incubation of balenine with acrolein resulted in the formation of single product (m/z 297), whereas DMB did not react with acrolein. In comparison with carnosine, balenine exhibited moderate acrolein quenching capacity. The Fechelating ability of balenine was higher than that of carnosine, whereas DMB lacked chelating capacity. Pretreatment of cardiac myocytes with carnosine increased the mean lifetime of myocytes superfused with HNE or acrolein compared with balenine or DMB. Collectively, these results suggest that carnosine protects cardiac myocytes against HNE and acrolein toxicity by directly reacting with these aldehydes. This reaction involves both the amino group ofβ-alanyl residue and the imidazole residue of L-histidine. Methylation of these sites prevents or abolishes the aldehyde reactivity of carnosine, alters its metal-chelating property, and diminishes its ability to prevent electrophilic injury.

Study Type : In Vitro Study
Additional Links
Pharmacological Actions : Antioxidants : CK(21528) : AC(8856)

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