Bioactive properties of carnosine
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Katedra i Zakład Biochemii i Biotechnologii Uniwersytet Medyczny w Lublinie
Ewa Syta   

Katedra i Zakład Biochemii i Biotechnologii\nUniwersytet Medyczny w Lublinie, ul. Kameralna5/60, 20-864 lublin, Polska
Med Og Nauk Zdr. 2018;24(2):96–100
Carnosine (β-alanyl-L-histidine) is a dipeptide that occurs endogenously in the body, the level of which decreases with age. It is a natural neuroprotective substance and its presence in the body prevents the processes of senescence – the aging of cells. In addition, it has antioxidant and chelating properties in relation to heavy metal ions. Carnosine maintains an acidalkaline balance – it buffers excitable tissues and also neutralizes lactic acid produced as a result of anaerobic glycolysis. It supports myocardial contractility by regulating the activity of calcium channels in cardiomyocytes and skeletal muscles. It limits the toxicity of free oxygen radicals and aldehydes – removing toxic products resulting from free radical reactions. As an anti-glycoprotein, it protects the cellular proteins against reactive oxygen species. It is bacteriostatic in relation to Helicobacter pylori. Carnosine is recognized as a potential therapeutic agent for many diseases correlated with the aging process. This substance is a potential therapeutic agent in the case of Parkinson’s and Alzheimer’s disease, as well as ischemic stroke. It reduces the level of pro-inflammatory cytokins and also has a potential anti-tumour effect. In addition, it counteracts the development of cataracts. This work is a review of the bioactive properties of carnosine and presents current cases of use of this substance in the manufacture of pharmaceuticals. This substance is becoming more and more popular as a component of dietary supplements.
Bakardijev A, Bauer K. Biosynthesis, release and uptake of carnosine in primary cultures. Biochemistry 2000; 65: 779–782.
Kang JH, Kim KS. Enhanced oligomerization of the alpha-synuclein mutant by the Cu, Zn-superoxide dismutase and hydrogen peroxide system. Mol Cells 2003; 15: 87–93.
Tanida M, Niijima A, Fukuda Y, Sawai H, Tsuruoka N, Shen J, Yamada S, Kiso Y, Nagai K. Dose-dependent effects of L-carnosine on the renal sympathetic nerve and blood pressure in urethane-anesthetized rats. Am J Physiol Regul Integr Comp Physiol 2005; 288: 447–455.
McGinnis WR. Oxidative stress in autism. Altern Ther Health Med 2004; 10: 22–36.
Teufel M, Saudek V, Ledig JP, Bernhardt A, Boularand S, Carreau A, Cairns NJ, Carter C, Cowley DJ, Duverger D, Ganzhorn AJ, Guenet C, Heintzelmann B, Laucher V, Sauvage C, Smirnova T. Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. J Biol Chem. 2003; 278: 6521–6531.
McDonough CW, Hicks PJ, Lu L, Langefeld CD, Freedman BJ, Bowden DW. The influence of carnosinase gene polymorphisms on diabetic nephropathy risk in African Americans. Hum Genet. 2009; 126(2): 265–275.
Gardner ML, Illingworth KM, Kelleher J, Wood D. Intestinal absorption of the intact peptide carnosine in man, and comparison with intestinal permeability to lactulose. J Physiol. 1991; 439: 411–422.
Chan WK, Decker EA, Chow CK, Boissonneault GA. Effect of dietary carnosine on plasma and tissue antioxidant concentrations and on lipid oxidation in rat skeletal muscle. Lipids, 1994; 29: 461–466.
Roberts PR, Zaloga GP. Cardiovascular effects of carnosine. Biochemistry 2000; 65: 856–861.
Zaloga GP, Roberts PR, Black KW, Lin M, Zapata-Sudo G, Sudo RT, Nelson TE. Carnosine is a novel peptide modulator of intracellular calcium and contractility in cardiac cells. Am J Phys 1997; 272: 462–468.
Sharma V, Bell RM, Yellon DM. Targeting reperfusion injury in acute myocardial infarction: a review of reperfusion injury pharmacotherapy. Expert Opin Pharmacother. 2012; 13(8): 1153–75.
Baye E, Ukropcova B, Ukropec J, Hipkiss A, Aldini G, de Courten B. Physiological and therapeutic effects of carnosine on cardiometabolic risk and disease. Amino Acids 2016; 48: 1131–49.
Boldyrev A, Abe H, Stvolinsky S, Tyulina O. Effects of carnosine and related compounds on generation of free oxygen species: a comparative study. Comp Biochem Physiol B Biochem Mol Biol 1995; 112: 481–485.
Fontana M, Pinnen F, Lucente G, Pecci L. Prevention of peroxynitrite¬-dependent damage by carnosine and related sulphonamido pseudodipeptides. Cell Mol Life Sci 2002; 59: 546–551.
Nagasawa T, Yonekura T, Nishizawa N, Kitts DD. In vitro and in vivo inhibition of muscle lipid and protein oxidation by carnosine. Mol Cell Biochem 2001; 225: 29–34.
Hu X, Tao C, Gan Q, Zheng J, Li H, You C. Oxidative stress in intra¬cerebral hemorrhage: sources, mechanisms, and therapeutic targets. Oxid Med Cell Longev 2016:3215391.
Boldyrev AA. Problems and perspectives in studying the biological role of carnosine. Biochemistry 2000; 65: 751–756.
Decker EA, Livisay SA, Zhou S. A re-evaluation of the antioxidant activity of purified carnosine. Biochemistry 2000; 65: 766–770.
Hipkiss AR. Carnosine and protein carbonyl groups: a possible rela¬tionship. Biochemistry 2000; 65: 771–778.
Price DL, Rhett PM, Thorpe SR, Baynes JW. Chelating activity of advanced glycation end-product inhibitors. J Biol Chem 2001; 276: 48967–48972.
Trombley PQ, Horning MS, Blakemore LJ. Interactions between car¬nosine and zinc and copper: implications for neuromodulation and neuroprotection. Biochemistry 2000; 65: 807–816.
Abdelkader H, Longman M, Alany G, Pierscionek B. On the anticata¬ractogenic effects of L-carnosine: Is it best described as an antioxidant, metal-chelating agent or glycation inhibitor? Oxid Med Cell Longev. 2016; 3: 1–11.
Maichuk IuF, Formaziuk VE, Sergienko VI. Development of carnosine eyedrops and assessing their efficacy in corneal diseases. Vestn Oftalmol 1997; 113: 27–31.
Gallant S, Kukley M, Stvolinsky S, Bulygina E, Boldyrev A. Effect of carnosine on rats under experimental brain ischemia. Tohoku J Exp Med 2000; 191: 85–99.
Ok-Nam B, Kelsey S, Seung-Hoon B, Ki Yong L, Anne D, Wilson R, Scott D. Fitzgerald, Muhammad U Farooq, Bharath N, Archit B, Arshad M. Safety and efficacy evaluation of carnosine, an endogenous neuropro¬tective agent for ischemic stroke. 2013; 44 (1): 205–212.
Khaspekov LG, Klyushnik TP, Dupin AM, Lyzhin AA, Bezrukov MV. Protective effect of Biolan during ischemic damages to cultured cerebellar granular cells. Bull Exp Biol Med 2002; 133: 136–138.
Paslawski W, Lorenzen N, Otzen DE. Formation and characterization of α-synuclein oligomers. Methods Mol Biol. 2016; 1345: 133–150.
Matsukura T, Tanaka H. Applicability of zinc complex of L-carnosine for medical use. Biochemistry 2000; 65: 817–823.
Pandurangan M, Mistry B, Enkhataivan G, Kim DH. Efficacy of carnosine on activation of caspase-3 and human renal carcinoma cell inhibition. Int J Biol Macromol. 2016; 92: 377–382.
Tehrani MHH, Bamoniri A, Gholibeikian M. The toxicity study of synthesized inverse carnosine peptide analogues on HepG2 and HT-29 cells. Iran J Basic Med Sci. 2018; 21(1): 39–46.
Ding M, Jiao G, Shi H, Chen Y. Investigations on in vitro anti-carci¬nogenic potential of L-carnosine in liver cancer cells. Cytotechnology. 2018; 70(1): 163–167.
Banerjee S, Sinha K, Chowdhury S, Sil PC. Unfolding the mechanism of cisplatin induced pathophysiology in spleen and its amelioration by carnosine. Chem Biol Interact. 2018; 279: 159–170.
Wallace DC. A mitochondrial paradigm for degenerative diseases and ageing. Novartis Found Symp. 2001; 235: 247–263.
Agathocleous M, Love NK, Randlett O, Harris JJ, Liu J, Murray AJ, Harris WA. Metabolic differentiation in the embryonic retina. Nat Cell Biol. 2012; 14: 859–864.
De Marchis S, Modena C, Peretto P, Migheli A, Margolis FL, Fasolo A. Carnosine-related dipeptides in neurons and glia. Biochemistry (Mosc) 2000; 65: 824–833.
Pognetto MS, Panzanelli P, Fasolo A, Cantino D. Expression of carnosine-like immunoreactivity during retinal development in the clawed frog (Xenopus laevis). Brain Res Dev Brain Res. 1992; 70: 134–138.
Baguet A, Everaert I, Achten E, Thomis M, Derave W. The influence of sex, age and heritability on human skeletal muscle carnosine content. Amino Acids. 2012; 43: 13–20.
Gaunitz F, Hipkiss AR. Carnosine and cancer: a perspective. Amino Acids 2012, 43: 135–142.
Derave W, Everaert I, Beeckman S, Baguet A. Muscle carnosine me¬tabolism and beta-alanine supplementation in relation to exercise and training. Sports Med. 2010; 40: 247–263.
Hipkiss AR, Chana H. Carnosine protects proteins against methy¬lglyoxal-mediated modifications. Biochem Biophys Res Commun. 1998; 248: 28–32.
Abe H. Role of histidine-related compounds as intracellular proton buffering constituents in vertebrate muscle. Biochemistry 2000; 65: 757–765.
Rubtsov AM. Molecular mechanisms of regulation of the activity of sar¬coplasmic reticulum Ca-release channels (ryanodine receptors), muscle fatigue, and Severin’s phenomenon. Biochemistry 2001; 66: 1132–1143.
Ikeda D, Wada S, Yoneda C, Abe H, Watabe S. Carnosine stimulates vimentin expression in cultured rat fibroblasts. Cell Struct Funct. 1999; 24: 79–87. doi: 10.1247/csf.24.79.
Nekrasova OE, Mendez MG, Chernoivanenko IS, Tyurin-Kuzmin PA, Kuczmarski ER, Gelfand VI, Goldman RD, Minin AA. Vimentin intermediate filaments modulate the motility of mitochondria. Mol Biol Cell. 2011; 22: 2282–2289.
Zakharchenko MV, Temnov AV, Kondrashova MN. Effect of carnosine on self-organization of mitochondrial assemblies in rat liver homoge¬nate. Biochemistry (Mosc) 2003; 68: 1002–1005.
Maher PA, Schubert DR. Metabolic links between diabetes and Alzheimer’s disease. Expert Rev Neurother. 2009; 9: 617–630.
Mai A. Revelations into resveratrol’s mechanism. Nat Med. 2012; 18: 500–501.
Stvolinsky SL, Fedorova TN, Devyatov AA, Medvedev OS, Belousova MA, Ryzhkov IN, Tutelyan VA. A neuroprotective action of carnosine in conditions of experimental focal cerebral ischemia-reperfusion. Zhurnal Nevrologii Psikhiatr Imeni S S Korsakova. 2017; 117: 60–64.
Baran EJ. Metal complexes of carnosine. Biochemistry 2000; 65: 789–797.