Skip to main content
Log in

Natural histidine-containing dipeptide Carnosine as a potent hydrophilic antioxidant with membrane stabilizing function

A biomedical aspect

  • Published:
Molecular and Chemical Neuropathology

Abstract

A review on the distribution and biological effects of carnosine and a hypothesis for its biological mechanisms of action are presented. Carnosine and its structural and functional relative, anserine, were found in skeletal muscles at the beginning of the century. Their effects on muscle-working capacity, on the stability of membrane-bound enzymes, as well as their potent immunomodulating property, could not be explained by their pH-buffering capacity or formation of the secondary metabolites histidine and β-alanine alone. This article suggests that the basis for the biological activities of carnosine and relative compounds is their potent antioxidant and membrane-protecting activity. The plausible chemical mechanism of this activity is discussed, and data regarding the usage of carnosine as a drug for treatment of immunodeficiency are summarized.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Ackerman D., Timpe O., and Poller K. (1929) Uber das Anserin, einen-neuen Bestandteil der Vogelmuskulatur.Hoppe-Seyler’s Z. Physiol. Chem. 183, 1–10.

    Google Scholar 

  • Boldyrev A. A. (1990) Retrospectives and perspectives on the biological activity of histidine-containing dipeptides.Int. J. Biochem. 22, 129–132.

    Article  PubMed  CAS  Google Scholar 

  • Boldyrev A. A. and Severin S. E. (1990) The histidine-containing dipeptides, carnosine and anserine: distribution, properties and biological significance.Adv. Enzyme Regulation,30, 175–194.

    Article  CAS  Google Scholar 

  • Dahl T. A., Midden W. R., and Hartman Ph.E. (1988) Some prevalent biomolecules as defenses against singlet oxygen damage.Photochem. Photobiol. 47, 357–361.

    Article  PubMed  CAS  Google Scholar 

  • Dupin A. M., Boldyrev A. A., Archipenko Yu. V., and Kagan V. E. (1984) Carnosine affords protection of Ca2+ transport in lipid peroxydation induced damage.Bull. Exp. Biol. Med. (USSR) 97, 186–188.

    Google Scholar 

  • Egorov S. Yu., Kurella E. G., Boldyrev A. A., and Krasnovsky A. A., Jr. (1992) The quenching of singlet molecular oxygen by carnosine and anserine in aqueous solution.Bioorganic Chem. (USSR) 18, 169–172.

    Google Scholar 

  • Giralt E., Ludeviv M.-D., and Pedroso E. (1986) The relevance of imidazole tautomerism for the hormonal activity of histidine-containing peptides.Bioorganic Chem. 14, 405–416.

    Article  CAS  Google Scholar 

  • Gulevitsch W. S. (1911) Zur Kentniss der Extraktivstoffe der Muskeln. Uber die Konstitution des Carnosin.Hoppe-Seyler’s Z. Physiol. Chem. 73, 434–440.

    Google Scholar 

  • Gulevitsch W. S. and Amiradgibi S. (1990) Uber das Carnosin, eine neue organische Base des Fleischextraktes.Ber. Deutsch. Chem. Ges. 33, 1902, 1903.

    Article  Google Scholar 

  • Harding J. and Margolis F. L. (1976) Denervation in primary olfactory pathway of mice. III. Effect of enzymes of carnosine metabolism.Brain Res. 110, 351–360.

    Article  PubMed  CAS  Google Scholar 

  • Hartman Ph.E., Hartman Z., and Ault K. T. (1990) Scavenging of singlet molecular oxygen by imidazole compounds: high and sustained activities of carboxy terminal histidine dipeptides and exceptional activity of imidazole-4-acetic acid.Photochem. Photobiol. 51, 59–66.

    Article  PubMed  CAS  Google Scholar 

  • Kohen R., Yamamoto Y., Cundy K. C., and Ames B. N. (1988) Antioxidant activity of carnosine, homocarnosine and anserine present in muscle and brain.Proc. Natl. Acad. Sci. USA 85, 3175–3179.

    Article  PubMed  CAS  Google Scholar 

  • Kurella E. G., Maltseva V. V., Seslavina L. S., and Stvolinsky S. L. (1991) Stimulating effect of carnosine on haemopoietic stem cells.Bull. Exp. Biol. Med. (USSR) 112, 52, 53.

    CAS  Google Scholar 

  • Lenney J. F., George R. P., Weiss A. M., Kucera C. M., Chan P. W. H., and Rhizler G. S. (1982) Human serum carnosinase: characterization, distinction from cellular carnosinase and activation by cadmium.Clin. Chim. Acta. 123, 21–31.

    Article  Google Scholar 

  • Maltseva V. V., Sergienko V. I., and Stvolinsky S. L. (1992) Effect of carnosine on the activity of haemopoietic stem cells in irradiated animals.Biochemistry (Russia) 57, 1378–1382.

    CAS  Google Scholar 

  • Nagai K. and Suda T. (1988) Realization of spontaneous healing function by carnosine.Meth. Finds. Exp. Clin. Pharmacol. 10, 497–507.

    CAS  Google Scholar 

  • Pavlov A. R., Revina A. A., Dupin A. M., Boldyrev A. A., and Yaropolov A. I. (1990) Interaction of carnosine with superoxide radicals in aqueous solutions.Bull. Exp. Biol. Med. (USSR) 108, 391–393.

    Google Scholar 

  • Severin S. E. and Boldyrev A. A. (1991) Effects of carnosine, a specific component of striated muscle, on muscle and other tissues.Biomedical Sci. 2, 91–93.

    CAS  Google Scholar 

  • Tolkatschevskaya N. (1929) Zur Kentniss der Extraktivstoffe dur Muskeln. Uber die Extraktivstoffe des Huhnerfleisches.Hoppe-Seyler’s Z. Physiol. Chem. 185, 28–32.

    Google Scholar 

  • Wood M. R. G. and Johnson P. (1981) Purification of carnosine synthetase from avian muscle by affinity chromatography and determination of its subunit structure.Biochim. Biophys. Acta 662, 138–144.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Boldyrev, A.A., Koldobski, A., Kurella, E. et al. Natural histidine-containing dipeptide Carnosine as a potent hydrophilic antioxidant with membrane stabilizing function. Molecular and Chemical Neuropathology 19, 185–192 (1993). https://doi.org/10.1007/BF03160178

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF03160178

Index Entries

Navigation