- Carnosine is generally very low and increases proportionally after meat intake.
- Urine levels peak after ~5 hours and are completely excreted within 20–25 hours.
- Urine carnosine increased with albuminuria in patients with diabetes.
- Patients with eGFR < 30 ml/mi had higher urine-carnosine excretion rates compared to eGFR (> 90 ml).
- Psoriasis patients had elevated asparagine, carnosine, and phosphoserine. They were all positively associated with psoriasis.
Carnosine (beta-alanyl-L-histidine) is a urinary biomarker which comes from the consumption of beef, pork, and to a lesser extent, poultry.
It is a dipeptide consisting of the amino acids histidine and beta-alanine and is concentrated in skeletal and heart muscle, brain, and kidneys. Carnosine has antioxidant properties, antiglycation effects, enhanced calcium sensitivity, and pH buffering activity during highintensity exercise.
It also has neuroprotective properties and may play an important role in Alzheimer’s disease and other neurodegenerative diseases.
Carnosine is also protective against secondary diabetic renal complications.
Plasma levels are non-detectable in fasting individuals; after beef consumption, postprandial plasma carnosine levels tend to rise then decrease to non-detectable levels within hours of consumption. In urine, levels reach a peak after 5 hours, but carnosine is completely excreted within 20-25 hours following the meal.
Carnosine has an affinity to chelate zinc, copper, cobalt, nickel and cadmium. The combination of zinc chelated with L-carnosine has been used therapeutically in the treatment of gastric ulcers. Carnosine is measured in FMV urine only.
- Cuparencu C, Pratico G, Hemeryck LY, et al. Biomarkers of meat and seafood intake: an extensive literature review. Genes Nutr. 2019;14:35.
- Cheung W, Keski-Rahkonen P, Assi N, et al. A metabolomic study of biomarkers of meat and fish intake. Am J Clin Nutr. 2017;105(3):600-608.
- Sadikali F, Darwish R, Watson WC. Carnosinase activity of human gastrointestinal mucosa. Gut. 1975;16(8):585-589.
- Derave W, De Courten B, Baba SP. An update on carnosine and anserine research. Amino Acids. 2019;51(1):1-4.
- Bellia F, Vecchio G, Rizzarelli E. Carnosinases, their substrates and diseases. Molecules. 2014;19(2):2299-2329.
- Boldyrev AA, Aldini G, Derave W. Physiology and pathophysiology of carnosine. Physiol Rev. 2013;93(4):1803- 1845.
- Peters V, Klessens CQ, Baelde HJ, et al. Intrinsic carnosine metabolism in the human kidney. Amino Acids. 2015;47(12):2541-2550.
- Perim P, Marticorena FM, Ribeiro F, et al. Can the Skeletal Muscle Carnosine Response to Beta-Alanine Supplementation Be Optimized? Front Nutr. 2019;6:135.
- Hipkiss AR. Would carnosine or a carnivorous diet help suppress aging and associated pathologies? Ann NY Acad Sci. 2006;1067:369-374.
- Hipkiss AR. Carnosine and its possible roles in nutrition and health. Adv Food Nutr Res. 2009;57:87-154.
- Kawahara M, Tanaka KI, Kato-Negishi M. Zinc, Carnosine, and Neurodegenerative Diseases. Nutrients. 2018;10(2).
- Bellia F, Calabrese V, Guarino F, et al. Carnosinase levels in aging brain: redox state induction and cellular stress response. Antiox Redox Signaling. 2009;11(11):2759-2775.
- Everaert I, Taes Y, De Heer E, et al. Low plasma carnosinase activity promotes carnosinemia after carnosine ingestion in humans. Am J Physiol Renal Physiol. 2012;302(12):F1537- 1544.
- Park YJ, Volpe SL, Decker EA. Quantitation of carnosine in humans plasma after dietary consumption of beef. J Agricult Food Chem. 2005;53(12):4736-4739.
- Perim P, Marticorena FM, Ribeiro F, et al. Can the Skeletal Muscle Carnosine Response to Beta-Alanine Supplementation Be Optimized? Front Nutr. 2019;6:135. Accessed 2019
- Everaert I, Taes Y, De Heer E, et al. Low plasma carnosinase activity promotes carnosinemia after carnosine ingestion in humans. Am J Physiol Renal Physiol. 2012;302(12):F1537-F1544.
Carnosine can be decreased with low animal protein intake, as seen in vegetarian or vegan diets.
Elevations are likely due to high consumption of meat or betaalanine supplementation. Since it is a dipeptide, elevations might also signify incomplete protein digestion. Zinc and manganese are important cofactors for the enzyme carnosinase that splits carnosine into the amino acids histidine and beta-alanine. Functional need for these nutrients can contribute to elevations of carnosine. Lastly, carnosinemia/carnosinuria is a rare inborn error of metabolism caused by a deficiency of the enzyme carnosinase.
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