Journal articles: 'Carnosinase'

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Everaert, Inge, Youri Taes, Emile De Heer, Hans Baelde, Ana Zutinic, Benito Yard, Sibylle Sauerhöfer, et al. "Low plasma carnosinase activity promotes carnosinemia after carnosine ingestion in humans." American Journal of Physiology-Renal Physiology 302, no. 12 (June 15, 2012): F1537—F1544. http://dx.doi.org/10.1152/ajprenal.00084.2012.

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A polymorphism in the carnosine dipeptidase-1 gene ( CNDP1), resulting in decreased plasma carnosinase activity, is associated with a reduced risk for diabetic nephropathy. Because carnosine, a natural scavenger/suppressor of ROS, advanced glycation end products, and reactive aldehydes, is readily degraded in blood by the highly active carnosinase enzyme, it has been postulated that low serum carnosinase activity might be advantageous to reduce diabetic complications. The aim of this study was to examine whether low carnosinase activity promotes circulating carnosine levels after carnosine supplementation in humans. Blood and urine were sampled in 25 healthy subjects after acute supplementation with 60 mg/kg body wt carnosine. Precooled EDTA-containing tubes were used for blood withdrawal, and plasma samples were immediately deproteinized and analyzed for carnosine and β-alanine by HPLC. CNDP1 genotype, baseline plasma carnosinase activity, and protein content were assessed. Upon carnosine ingestion, 8 of the 25 subjects (responders) displayed a measurable increase in plasma carnosine up to 1 h after supplementation. Subjects with no measurable increment in plasma carnosine (nonresponders) had ∼2-fold higher plasma carnosinase protein content and ∼1.5-fold higher activity compared with responders. Urinary carnosine recovery was 2.6-fold higher in responders versus nonresponders and was negatively dependent on both the activity and protein content of the plasma carnosinase enzyme. In conclusion, low plasma carnosinase activity promotes the presence of circulating carnosine upon an oral challenge. These data may further clarify the link among CNDP1 genotype, carnosinase, and diabetic nephropathy.

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Rodriguez-Niño, Angelica, Diego O. Pastene, Adrian Post, M. Yusof Said, Antonio W. Gomes-Neto, Lyanne M. Kieneker, M. Rebecca Heiner-Fokkema, et al. "Urinary Carnosinase-1 Excretion is Associated with Urinary Carnosine Depletion and Risk of Graft Failure in Kidney Transplant Recipients: Results of the TransplantLines Cohort Study." Antioxidants 10, no. 7 (July 9, 2021): 1102. http://dx.doi.org/10.3390/antiox10071102.

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Carnosine affords protection against oxidative and carbonyl stress, yet high concentrations of the carnosinase-1 enzyme may limit this. We recently reported that high urinary carnosinase-1 is associated with kidney function decline and albuminuria in patients with chronic kidney disease. We prospectively investigated whether urinary carnosinase-1 is associated with a high risk for development of late graft failure in kidney transplant recipients (KTRs). Carnosine and carnosinase-1 were measured in 24 h urine in a longitudinal cohort of 703 stable KTRs and 257 healthy controls. Cox regression was used to analyze the prospective data. Urinary carnosine excretions were significantly decreased in KTRs (26.5 [IQR 21.4–33.3] µmol/24 h versus 34.8 [IQR 25.6–46.8] µmol/24 h; p < 0.001). In KTRs, high urinary carnosinase-1 concentrations were associated with increased risk of undetectable urinary carnosine (OR 1.24, 95%CI [1.06–1.45]; p = 0.007). During median follow-up for 5.3 [4.5–6.0] years, 84 (12%) KTRs developed graft failure. In Cox regression analyses, high urinary carnosinase-1 excretions were associated with increased risk of graft failure (HR 1.73, 95%CI [1.44–2.08]; p < 0.001) independent of potential confounders. Since urinary carnosine is depleted and urinary carnosinase-1 imparts a higher risk for graft failure in KTRs, future studies determining the potential of carnosine supplementation in these patients are warranted.

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Bando, Keiichi, Kiyoshi Ichihara, Tsunesuke Shimotsuji, Hiroyuki Toyoshima, Kazuma Koda, Chozo Hayashi, and Kiyoshi Miyai. "Reduced Serum Carnosinase Activity in Hypothyroidism." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 23, no. 2 (March 1986): 190–94. http://dx.doi.org/10.1177/000456328602300208.

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Carnosinase hydrolyses carnosine in muscle, and its deficiency is associated with extensive neuromuscular abnormalities. We measured serum carnosinase activity in patients with thyroid dysfunction which often involves neuromuscular systems. In hyperthyroidism, the carnosinase activity was not significantly different from that in normal subjects. In hypothyroidism, however, it was significantly lower than that in normal subjects. The activity examined in five patients with hypothyroidism returned to normal after replacement therapy. In hypothyroidism, the carnosinase activity showed significant correlation with concentration of serum thyroxine and negative correlation with serum creatine kinase activity. This finding may be of practical importance in the differential diagnosis of disorders causing carnosinase deficiency.

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Lenney, J. F., S. C. Peppers, C. M. Kucera-Orallo, and R. P. George. "Characterization of human tissue carnosinase." Biochemical Journal 228, no. 3 (June 15, 1985): 653–60. http://dx.doi.org/10.1042/bj2280653.

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Human tissue carnosinase (EC 3.4.13.3) had optimum activity at pH9.5 and was a cysteine peptidase, being activated by dithiothreitol and inhibited by p-hydroxymercuribenzoate. By optimizing assay conditions, the activity per g of tissue was increased 10-fold compared with values in the literature. The enzyme was present in every human tissue assayed and was entirely different from serum carnosinase. Highly purified tissue carnosinase had a broader specificity than hog kidney carnosinase. Although tissue carnosinase was very strongly inhibited by bestatin, it did not hydrolyse tripeptides, and thus appears to be a dipeptidase rather than an aminopeptidase. It had a relative molecular mass of 90 000, an isoelectric point of 5.6, and a Km value of 10 mM-carnosine. Two forms of kidney and brain carnosinase were separated by high-resolution anion-exchange chromatography, although only one form was detected by various electrophoretic methods. Homocarnosinase and Mn2+-independent carnosinase were not detected in human tissues, although these enzymes are present in rat and hog kidney.

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Oppermann, Henry, Stefanie Elsel, Claudia Birkemeyer, Jürgen Meixensberger, and Frank Gaunitz. "Erythrocytes Prevent Degradation of Carnosine by Human Serum Carnosinase." International Journal of Molecular Sciences 22, no. 23 (November 26, 2021): 12802. http://dx.doi.org/10.3390/ijms222312802.

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The naturally occurring dipeptide carnosine (β-alanyl-l-histidine) has beneficial effects in different diseases. It is also frequently used as a food supplement to improve exercise performance and because of its anti-aging effects. Nevertheless, after oral ingestion, the dipeptide is not detectable in human serum because of rapid degradation by serum carnosinase. At the same time, intact carnosine is excreted in urine up to five hours after intake. Therefore, an unknown compartment protecting the dipeptide from degradation has long been hypothesized. Considering that erythrocytes may constitute this compartment, we investigated the uptake and intracellular amounts of carnosine in human erythrocytes cultivated in the presence of the dipeptide and human serum using liquid chromatography–mass spectrometry. In addition, we studied carnosine’s effect on ATP production in red blood cells and on their response to oxidative stress. Our experiments revealed uptake of carnosine into erythrocytes and protection from carnosinase degradation. In addition, no negative effect on ATP production or defense against oxidative stress was observed. In conclusion, our results for the first time demonstrate that erythrocytes can take up carnosine, and, most importantly, thereby prevent its degradation by human serum carnosinase.

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Menini, Stefano, Carla Iacobini, Claudia Blasetti Fantauzzi, and Giuseppe Pugliese. "L-carnosine and its Derivatives as New Therapeutic Agents for the Prevention and Treatment of Vascular Complications of Diabetes." Current Medicinal Chemistry 27, no. 11 (April 23, 2020): 1744–63. http://dx.doi.org/10.2174/0929867326666190711102718.

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Vascular complications are among the most serious manifestations of diabetes. Atherosclerosis is the main cause of reduced life quality and expectancy in diabetics, whereas diabetic nephropathy and retinopathy are the most common causes of end-stage renal disease and blindness. An effective therapeutic approach to prevent vascular complications should counteract the mechanisms of injury. Among them, the toxic effects of Advanced Glycation (AGEs) and Lipoxidation (ALEs) end-products are well-recognized contributors to these sequelae. L-carnosine (β-alanyl-Lhistidine) acts as a quencher of the AGE/ALE precursors Reactive Carbonyl Species (RCS), which are highly reactive aldehydes derived from oxidative and non-oxidative modifications of sugars and lipids. Consistently, L-carnosine was found to be effective in several disease models in which glyco/lipoxidation plays a central pathogenic role. Unfortunately, in humans, L-carnosine is rapidly inactivated by serum carnosinase. Therefore, the search for carnosinase-resistant derivatives of Lcarnosine represents a suitable strategy against carbonyl stress-dependent disorders, particularly diabetic vascular complications. In this review, we present and discuss available data on the efficacy of L-carnosine and its derivatives in preventing vascular complications in rodent models of diabetes and metabolic syndrome. We also discuss genetic findings providing evidence for the involvement of the carnosinase/L-carnosine system in the risk of developing diabetic nephropathy and for preferring the use of carnosinase-resistant compounds in human disease. The availability of therapeutic strategies capable to prevent both long-term glucose toxicity, resulting from insufficient glucoselowering therapy, and lipotoxicity may help reduce the clinical and economic burden of vascular complications of diabetes and related metabolic disorders.

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Kiliś-Pstrusińska, Katarzyna. "Carnosine, carnosinase and kidney diseases." Postępy Higieny i Medycyny Doświadczalnej 66 (April 20, 2012): 215–23. http://dx.doi.org/10.5604/17322693.991600.

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Macarini, José Roberto, Soliany Grassi Maravai, José Henrique Cararo, Nádia Webber Dimer, Cinara Ludvig Gonçalves, Luiza Wilges Kist, Mauricio Reis Bogo, Patrícia Fernanda Schuck, Emilio Luiz Streck, and Gustavo Costa Ferreira. "Impairment of Electron Transfer Chain Induced by Acute Carnosine Administration in Skeletal Muscle of Young Rats." BioMed Research International 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/632986.

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Serum carnosinase deficiency is an inherited disorder that leads to an accumulation of carnosine in the brain tissue, cerebrospinal fluid, skeletal muscle, and other tissues of affected patients. Considering that high levels of carnosine are associated with neurological dysfunction and that the pathophysiological mechanisms involved in serum carnosinase deficiency remain poorly understood, we investigated thein vivoeffects of carnosine on bioenergetics parameters, namely, respiratory chain complexes (I–III, II, and II-III), malate dehydrogenase, succinate dehydrogenase, and creatine kinase activities and the expression of mitochondrial-specific transcription factors (NRF-1, PGC-1α, andTFAM) in skeletal muscle of young Wistar rats. We observed a significant decrease of complexes I–III and II activities in animals receiving carnosine acutely, as compared to control group. However, no significant alterations in respiratory chain complexes, citric acid cycle enzymes, and creatine kinase activities were found between rats receiving carnosine chronically and control group animals. As compared to control group, mRNA levels ofNRF-1, PGC-1α, andTFAMwere unchanged. The present findings indicate that electron transfer through the respiratory chain is impaired in skeletal muscle of rats receiving carnosine acutely. In case these findings are confirmed by further studies and ATP depletion is also observed, impairment of bioenergetics could be considered a putative mechanism responsible for the muscle damage observed in serum carnosinase-deficient patients.

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Kilis-Pstrusinska, Katarzyna. "Carnosine and Kidney Diseases: What We Currently Know?" Current Medicinal Chemistry 27, no. 11 (April 23, 2020): 1764–81. http://dx.doi.org/10.2174/0929867326666190730130024.

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: Carnosine (beta-alanyl-L-histidine) is an endogenously synthesised dipeptide which is present in different human tissues e.g. in the kidney. Carnosine is degraded by enzyme serum carnosinase, encoding by CNDP1 gene. Carnosine is engaged in different metabolic pathways in the kidney. It reduces the level of proinflammatory and profibrotic cytokines, inhibits advanced glycation end products’ formation, moreover, it also decreases the mesangial cell proliferation. Carnosine may also serve as a scavenger of peroxyl and hydroxyl radicals and a natural angiotensin-converting enzyme inhibitor. : This review summarizes the results of experimental and human studies concerning the role of carnosine in kidney diseases, particularly in chronic kidney disease, ischemia/reperfusion-induced acute renal failure, diabetic nephropathy and also drug-induced nephrotoxicity. The interplay between serum carnosine concentration and serum carnosinase activity and polymorphism in the CNDP1 gene is discussed. : Carnosine has renoprotective properties. It has a promising potential for the treatment and prevention of different kidney diseases, particularly chronic kidney disease which is a global public health issue. Further studies of the role of carnosine in the kidney may offer innovative and effective strategies for the management of kidney diseases.

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Blancquaert, L., I. Everaert, A. Baguet, T. Bex, S. Barbaresi, S. de Jager, E. Lievens, et al. "Acute preexercise supplementation of combined carnosine and anserine enhances initial maximal power of Wingate tests in humans." Journal of Applied Physiology 130, no. 6 (June 1, 2021): 1868–78. http://dx.doi.org/10.1152/japplphysiol.00602.2020.

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Current results reveal that carnosine and anserine competitively bind to the highly active carnosinase enzyme in human plasma. Acute combined carnosine and anserine supplementation is therefore described as novel strategy to raise plasma anserine and carnosine. We report that indices of maximal exercise/muscle power during the initial stage of a Wingate test were significantly improved by preexercise 20–25mg/kg body wt anserine and carnosine supplementation, pointing toward a novel acute nutritional strategy to improve high-intensity exercise performance.

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Wetzel, Charlotte, Tilman Pfeffer, Ruben Bulkescher, Johanna Zemva, Sergio Modafferi, Alessandra Polimeni, Angela Trovato Salinaro, Vittorio Calabrese, Claus Peter Schmitt, and Verena Peters. "Anserine and Carnosine Induce HSP70-Dependent H2S Formation in Endothelial Cells and Murine Kidney." Antioxidants 12, no. 1 (December 28, 2022): 66. http://dx.doi.org/10.3390/antiox12010066.

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Anserine and carnosine have nephroprotective actions; hydrogen sulfide (H2S) protects from ischemic tissue damage, and the underlying mechanisms are debated. In view of their common interaction with HSP70, we studied possible interactions of both dipeptides with H2S. H2S formation was measured in human proximal tubular epithelial cells (HK-2); three endothelial cell lines (HUVEC, HUAEC, MCEC); and in renal murine tissue of wild-type (WT), carnosinase-1 knockout (Cndp1-KO) and Hsp70-KO mice. Diabetes was induced by streptozocin. Incubation with carnosine increased H2S synthesis capacity in tubular cells, as well as with anserine in all three endothelial cell lines. H2S dose-dependently reduced anserine/carnosine degradation rate by serum and recombinant carnosinase-1 (CN1). Endothelial Hsp70-KO reduced H2S formation and abolished the stimulation by anserine and could be restored by Hsp70 transfection. In female Hsp70-KO mice, kidney H2S formation was halved. In Cndp1-KO mice, kidney anserine concentrations were several-fold and sex-specifically increased. Kidney H2S formation capacity was increased 2–3-fold in female mice and correlated with anserine and carnosine concentrations. In diabetic Cndp1-KO mice, renal anserine and carnosine concentrations as well as H2S formation capacity were markedly reduced compared to non-diabetic Cndp1-KO littermates. Anserine and carnosine induce H2S formation in a cell-type and Hsp70-specific manner within a positive feedback loop with CN1.

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Antonova, N. A., G. M. Sorokoumova, T. N. Fedorova, S. L. Stvolynsky, D. A. Abaimov, V. I. Popenko, and V. I. Shvets. "CARNOSINE-CONTAINING LIPOSOMES: PREPARATION AND PROPERTIES." Fine Chemical Technologies 11, no. 6 (December 28, 2016): 55–62. http://dx.doi.org/10.32362/2410-6593-2018-13-2-55-62.

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Carnosine is a natural dipeptide antioxidant. It is proved that it protects human’s cells from oxidative stress. However, it has a short lifetime in a human organism due to the carnosinase activity. In order to solve this problem we used carnosine encapsulated in liposomes. Thus, the aim of this study was the creation of a new liposomal carnosine drug form. We used two encapsulation methods that show different carnosine behavior: a passive and an active one. We took into account that conditions of obtaining liposomes such as lipid composition, pH and temperature are important. In this study the lipid composition providing the maximum encapsulation efficiency was determined. Dipalmitoylphosphotidylcholine (DPPC) and its mixture with cholesterol (Chol) wereused as composition lipids. It was shown that the active encapsulation method using the creation of ammonium sulphate pH gradient provided the best results: 41.7% encapsulation efficiency (according to NMR spectroscopy) when using DPPC:Chol (7:3) mixture as lipids. Moreover, the properties of the liposomes were studied. Using the dynamic light scattering and electron microscopy methods carnosine liposomes (DPPC:Chol) were shown to be spherical nanoparticles with an average size of 133 nm. Carnosine release kinetics studied with the use of a France’s cell showed that carnosine was released in 24 hours (liposomal composition DPPC:Chol was 7:3). A study of carnosinase action on liposomal carnosine showed that the maximum amount of carnosine remained unchanged in DPPC:Chol liposomes (7:3). The results of the study make it possible to conclude that liposomal carnosine has a better activity in the human organism.

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Bhatt, Achal, Renee Green, Roswell Coles, Michael Condon, and Nancy D. Connell. "A Mutant of Mycobacterium smegmatisDefective in Dipeptide Transport." Journal of Bacteriology 180, no. 24 (December 15, 1998): 6773–75. http://dx.doi.org/10.1128/jb.180.24.6773-6775.1998.

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ABSTRACT A mutant of Mycobacterium smegmatis unable to use the dipeptide carnosine (β-alanyl-l-histidine) as a sole carbon or nitrogen source was isolated. Carnosinase activity and the ability to grow on β-Ala and/or l-His were similar in the mutant and the wild type. However, the mutant showed significant impairment in the uptake of carnosine. This study is the first description of a peptide utilization mutant of a mycobacterium.

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Stegen, Sanne, Ronald J. Sigal, Glen P. Kenny, Farah Khandwala, Benito Yard, Emile De Heer, Hans Baelde, Wim Peersman, and Wim Derave. "Aerobic and resistance training do not influence plasma carnosinase content or activity in type 2 diabetes." American Journal of Physiology-Endocrinology and Metabolism 309, no. 7 (October 1, 2015): E663—E669. http://dx.doi.org/10.1152/ajpendo.00142.2015.

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A particular allele of the carnosinase gene (CNDP1) is associated with reduced plasma carnosinase activity and reduced risk for nephropathy in diabetic patients. On the one hand, animal and human data suggest that hyperglycemia increases plasma carnosinase activity. On the other hand, we recently reported lower carnosinase activity levels in elite athletes involved in high-intensity exercise compared with untrained controls. Therefore, this study investigates whether exercise training and the consequent reduction in hyperglycemia can suppress carnosinase activity and content in adults with type 2 diabetes. Plasma samples were taken from 243 males and females with type 2 diabetes (mean age = 54.3 yr, SD = 7.1) without major microvascular complications before and after a 6-mo exercise training program [4 groups: sedentary control ( n = 61), aerobic exercise ( n = 59), resistance exercise ( n = 63), and combined exercise training ( n = 60)]. Plasma carnosinase content and activity, hemoglobin (Hb) A1c, lipid profile, and blood pressure were measured. A 6-mo exercise training intervention, irrespective of training modality, did not decrease plasma carnosinase content or activity in type 2 diabetic patients. Plasma carnosinase content and activity showed a high interindividual but very low intraindividual variability over the 6-mo period. Age and sex, but not Hb A1c, were significantly related to the activity or content of this enzyme. It can be concluded that the beneficial effects of exercise training on the incidence of diabetic complications are probably not related to a lowering effect on plasma carnosinase content or activity.

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Baguet, Audrey, Inge Everaert, Benito Yard, Verena Peters, Johannes Zschocke, Ana Zutinic, Emile De Heer, Tomasz Podgórski, Katarzyna Domaszewska, and Wim Derave. "Does low serum carnosinase activity favor high-intensity exercise capacity?" Journal of Applied Physiology 116, no. 5 (March 1, 2014): 553–59. http://dx.doi.org/10.1152/japplphysiol.01218.2013.

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Given the ergogenic properties of β-alanyl-L-histidine (carnosine) in skeletal muscle, it can be hypothesized that elevated levels of circulating carnosine could equally be advantageous for high-intensity exercises. Serum carnosinase (CN1), the enzyme hydrolyzing the dipeptide, is highly active in the human circulation. Consequently, dietary intake of carnosine usually results in rapid degradation upon absorption, yet this is less pronounced in subjects with low CN1 activity. Therefore, acute carnosine supplementation before high-intensity exercise could be ergogenic in these subjects. In a cross-sectional study, we determined plasma CN1 activity and content in 235 subjects, including 154 untrained controls and 45 explosive and 36 middle- to long-distance elite athletes. In a subsequent double-blind, placebo-controlled, crossover study, 12 men performed a cycling capacity test at 110% maximal power output (CCT 110%) following acute carnosine (20 mg/kg body wt) or placebo supplementation. Blood samples were collected to measure CN1 content, carnosine, and acid-base balance. Both male and female explosive athletes had significantly lower CN1 activity (14% and 21% lower, respectively) and content (30% and 33% lower, respectively) than controls. Acute carnosine supplementation resulted only in three subjects in carnosinemia. The CCT 110% performance was not improved after carnosine supplementation, even when accounting for low/high CN1 content. No differences were found in acid-base balance, except for elevated resting bicarbonate following carnosine supplementation and in low CN1 subjects. In conclusion, explosive athletes have lower serum CN1 activity and content compared with untrained controls, possibly resulting from genetic selection. Acute carnosine supplementation does not improve high-intensity performance.

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Duane, P., and T. J. Peters. "Serum carnosinase activities in patients with alcoholic chronic skeletal muscle myopathy." Clinical Science 75, no. 2 (August 1, 1988): 185–90. http://dx.doi.org/10.1042/cs0750185.

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1. Serum carnosinase activity was assayed in a group of alcoholic patients with and without histologically proven atrophy of type II skeletal muscle fibres, and in control subjects. No significant activity was detected in muscle biopsy samples or washed erythrocytes. 2. Serum carnosinase activity was significantly lower in chronic alcoholic patients compared with a group of age-matched controls. Alcoholics with abnormal muscle biopsies had significantly lower enzyme activities than either those patients with normal muscle biopsies or the controls. Serum enzyme activities in patients with normal muscle biopsies were not significantly different from controls. 3. Serum carnosinase activity was inversely correlated with the degree of muscle atrophy as measured by the type II fibre atrophy factor. There was a positive correlation between the enzyme activity and skeletal muscle mass as reflected by the creatinine-height index. Furthermore, the enzyme activity significantly increased, with resolution or improvement in the myopathy, in patients who abstained from alcohol. 4. Kinetic studies showed that the reduced carnosinase activity was due mainly to a decrease in the apparent Vmax. The apparent Km was significantly higher in the myopathic compared with non-myopathic alcoholics. Mixing serum from controls and patients with myopathy gave the expected values, indicating the absence of a serum enzyme inhibitory factor. Acute alcohol loading had no effect on the serum carnosinase activity. 5. The decrease in serum carnosinase activity in alcoholics was not related to the severity of their liver disease. Assays of serum carnosinase in chronic alcoholics can thus be used as a marker of their associated myopathy.

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Makk-Merczel, Kinga, and András Szarka. "A karbonilstressz szerepe a diabetes szövődményeinek kialakulásában." Orvosi Hetilap 160, no. 40 (October 2019): 1567–73. http://dx.doi.org/10.1556/650.2019.31519.

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Abstract: The relationship between the potentially developing complications of the 451 million people affected by diabetes and hyperglycaemia can be based on the enhanced generation of advanced glycation endproducts and the more intensive oxidative and carbonyl stress. Advanced glycation endproducts generated partly due to carbonyl stress play an important role in the pathogenesis of diabetic complications such as elevated arterial thickness, vascular permeability, enhanced angiogenesis or the more rigid vessels induced nephropathy, neuropathy, retinopathy. Furthermore, the elevated thrombocyte aggregation, the reduced fibrinolysis induced elevated coagulation, and the atherosclerosis or the mitochondrial dysfunction are important as well. The most potent target of both the non-oxidative and oxidative generation of advanced glycation endproducts can be the scavenging of α,β-unsaturated aldehydes. Although, aminoguanidine, the prototype of scavenger molecules, showed protection in different animal models, it failed in the human clinical studies. Finally, the clinical studies were terminated almost 20 years ago. The endogen dipeptide L-carnosine was also expected to mitigate the complications due to carbonyl stress. However, its clinical significance was limited by the serum carnosinases and by the consequent low serum stability and bioavailability. The carnosinase resistance of the molecule can be achieved by the change of the carboxyl group of the molecule to hydroxyl group. At the same time, the biosafety and the carbonyl stress scavenging activity of the molecule could be preserved. Although clinical studies could not be performed in the last six months, on the basis of the in vitro and in vivo results, carnosinole seems to be a promising compound to mitigate and prevent the diabetic complications. Thus it is worth to the attention of the clinicians. Orv Hetil. 2019; 160(40): 1567–1573.

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Peters, Verena, Benito Yard, and Claus Peter Schmitt. "Carnosine and Diabetic Nephropathy." Current Medicinal Chemistry 27, no. 11 (April 23, 2020): 1801–12. http://dx.doi.org/10.2174/0929867326666190326111851.

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Diabetic Nephropathy (DN) is a major complication in patients with type 1 or type 2 diabetes and represents the leading cause of end-stage renal disease. Novel therapeutic approaches are warranted. In view of a polymorphism in the carnosinase 1 gene CNDP1, resulting in reduced carnosine degradation activity and a significant DN risk reduction, carnosine (β-alanyl-L-histidine) has gained attention as a potential therapeutic target. Carnosine has anti-inflammatory, antioxidant, anti-glycation and reactive carbonyl quenching properties. In diabetic rodents, carnosine supplementation consistently improved renal histology and function and in most studies, also glucose metabolism. Even though plasma half-life of carnosine in humans is short, first intervention studies in (pre-) diabetic patients yielded promising results. The precise molecular mechanisms of carnosine mediated protective action, however, are still incompletely understood. This review highlights the recent knowledge on the role of the carnosine metabolism in DN.

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Arnould, J. M. "Mise en évidence in vitro de la biosynthèse d'histamine à partir de carnosine par le rein de souris gravide." Canadian Journal of Physiology and Pharmacology 65, no. 1 (January 1, 1987): 70–74. http://dx.doi.org/10.1139/y87-013.

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Kidneys of pregnant mice synthesize histamine when incubated in the presence of carnosine, manganese, and pyridoxal phosphate. Intensity of biosynthesis increases linearly with the amount of enzyme and the incubation time. The reaction can only be catalysed by two enzymes that are located in kidneys and act in succession: carnosinase, which hydrolyzes carnosine into its two moieties, and histidine decarboxylase, which transforms histidine, a product of carnosine degradation, into histamine. The biosynthesis of histamine from carnosine seems to increase with the progress of pregnancy. In nonpregnant mice, kidneys do not effect this biosynthesis. The above results directly demonstrate that carnosine may be used for histamine synthesis when the activity of histidine decarboxylase is high, as in pregnant mouse kidney. Vertebrate carnosine, its role still enigmatic, might thus be mainly a potential histidine reservoir that would be mobilized any time there is a significant requirement for histidine, such as for histamine biosynthesis.

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Peters, Verena, Johannes Zschocke, and Claus P. Schmitt. "Carnosinase, diabetes mellitus and the potential relevance of carnosinase deficiency." Journal of Inherited Metabolic Disease 41, no. 1 (October 13, 2017): 39–47. http://dx.doi.org/10.1007/s10545-017-0099-2.

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Sauerhofer, S., G. Yuan, G. S. Braun, M. Deinzer, M. Neumaier, N. Gretz, J. Floege, W. Kriz, F. van der Woude, and M. J. Moeller. "L-Carnosine, a Substrate of Carnosinase-1, Influences Glucose Metabolism." Diabetes 56, no. 10 (June 29, 2007): 2425–32. http://dx.doi.org/10.2337/db07-0177.

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Bando, K., K. Ichihara, H. Toyoshima, T. Shimotuji, K. Koda, C. Hayashi, and K. Miyai. "Decreased activity of carnosinase in serum of patients with chronic liver disorders." Clinical Chemistry 32, no. 8 (August 1, 1986): 1563–65. http://dx.doi.org/10.1093/clinchem/32.8.1563.

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Abstract We measured the activity of carnosinase, a prominent hepatic peptidase, in sera from 69 patients with liver disorders. Mean values (and SDs) for those with liver cirrhosis (17 cases) and hepatoma (seven cases) were 0.51 (0.28) and 0.68 (0.21) mumol/mL per hour, respectively--clearly less than for normal adults: 4.19 (0.95) mumol/mL per hour. Samples from 17 cases of chronic hepatitis also showed moderately decreased activity, 1.41 (0.97) mumol/mL per hour. In contrast, 14 cases of acute hepatitis generally showed values falling within the normal limits: 3.41 (1.97) mumol/mL per hour. Our results for carnosinase correlated with those for cholinesterase (r = 0.70) and with the concentration of albumin in serum (r = 0.59), but not with the activity of either creatine kinase, aspartate aminotransferase, or alanine aminotransferase in serum. Carnosinase values differed more among groups of disorders than did the values for cholinesterase or albumin. Measurement of serum carnosinase activity may be of clinical value in assessing the severity of chronic liver-cell damage, but not in differentiating liver disease from nutritional, muscle, or endocrine disorders.

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Kalra, Jawahar, Cynthia Balion, K. Lorne Massey, and Victor A. Laxdal. "Regulation of carnosine metabolism: The subcellular localization of carnosinase in liver." Clinical Biochemistry 21, no. 5 (October 1988): 315–18. http://dx.doi.org/10.1016/s0009-9120(88)80088-2.

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Toviwek, Borvornwat, Skorn Koonawootrittriron, Thanathip Suwanasopee, and Prapasiri Pongprayoon. "Molecular insights into the binding of carnosine and anserine to human serum carnosinase 1 (CN1)." PeerJ Physical Chemistry 4 (October 20, 2022): e25. http://dx.doi.org/10.7717/peerj-pchem.25.

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Carnosine (CAR) and anserine (ANS) are histidine-containing dipeptides that show the therapeutic properties and protective abilities against diabetes and cognitive deficit. Both dipeptides are rich in meat products and have been used as a supplement. However, in humans, both compounds have a short half-life due to the rapid degradation by dizinc carnosinase 1 (CN1) which is a hurdle for its therapeutic application. To date, a comparative study of carnosine- and anserine-CN1 complexes is limited. Thus, in this work, molecular dynamics (MD) simulations were performed to explore the binding of carnosine and anserine to CN1. CN1 comprises 2 chains (Chains A and B). Both monomers are found to work independently and alternatingly. The displacement of Zn2+ pair is found to disrupt the substrate binding. CN1 employs residues from the neighbour chain (H235, T335, and T337) to form the active site. This highlights the importance of a dimer for enzymatic activity. Anserine is more resistant to CN 1 than carnosine because of its bulky and dehydrated imidazole moiety. Although both dipeptides can direct the peptide oxygen to the active Zn2+ which can facilitate the catalytic reaction, the bulky methylated imidazole on anserine promotes various poses that can retard the hydrolytic activity in contrast to carnosine. Anserine is likely to be the temporary competitive inhibitor by retarding the carnosine catabolism.

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Stvolinsky, S. L., N. A. Antonova, O. I. Kulikova, A. V. Lopachev, D. A. Abaimov, I. Al-Baidani, O. M. Lopacheva, T. N. Fedorova, A. P. Kaplun, and G. M. Sorokoumova. "Lipoilcarnosine: synthesis, study of physico-chemical and antioxidant properties, biological activity." Biomeditsinskaya Khimiya 64, no. 3 (2018): 268–75. http://dx.doi.org/10.18097/pbmc20186403268.

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Synthesis of lipoilcarnosine (LipC) – a conjugated molecule based on two natural antioxidants, carnosine and a-lipoic acid, is described. Its physico-chemical, antioxidant properties and biological activity are characterized. According to reversed-phase HPLC with a UV detector, purity of the final product was 89.3%. The individuality of the obtained sodium salt of LipC was confirmed by tandem HPLC-mass spectrometry. High resistance of LipC to hydrolysis with serum carnosinase was demonstrated. The antioxidant activity of LipC measured by reaction with the formation of thiobarbituric acid reacting substances and kinetic parameters of iron-induced chemiluminescence was higher than that of carnosine and lipoic acid. LipC did not affect viability of SH-SY5Y human neuroblastoma culture cells, differentiated towards the dopaminergic type, at concentrations not exceeding 5 mM. At the concentration range of 0.1-0.25 mM LipC protected neuronal cells against 1-methyl-4-phenylpyridinium (MPP + )-induced toxicity.

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Naletova, Irina, Valentina Greco, Sebastiano Sciuto, Francesco Attanasio, and Enrico Rizzarelli. "Ionophore Ability of Carnosine and Its Trehalose Conjugate Assists Copper Signal in Triggering Brain-Derived Neurotrophic Factor and Vascular Endothelial Growth Factor Activation In Vitro." International Journal of Molecular Sciences 22, no. 24 (December 16, 2021): 13504. http://dx.doi.org/10.3390/ijms222413504.

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l-carnosine (β-alanyl-l-histidine) (Car hereafter) is a natural dipeptide widely distributed in mammalian tissues and reaching high concentrations (0.7–2.0 mM) in the brain. The molecular features of the dipeptide underlie the antioxidant, anti-aggregating and metal chelating ability showed in a large number of physiological effects, while the biological mechanisms involved in the protective role found against several diseases cannot be explained on the basis of the above-mentioned properties alone, requiring further research efforts. It has been reported that l-carnosine increases the secretion and expression of various neurotrophic factors and affects copper homeostasis in nervous cells inducing Cu cellular uptake in keeping with the key metal-sensing system. Having in mind this l-carnosine ability, here we report the copper-binding and ionophore ability of l-carnosine to activate tyrosine kinase cascade pathways in PC12 cells and stimulate the expression of BDNF. Furthermore, the study was extended to verify the ability of the dipeptide to favor copper signaling inducing the expression of VEGF. Being aware that the potential protective action of l-carnosine is drastically hampered by its hydrolysis, we also report on the behavior of a conjugate of l-carnosine with trehalose that blocks the carnosinase degradative activity. Overall, our findings describe a copper tuning effect on the ability of l-carnosine and, particularly its conjugate, to activate tyrosine kinase cascade pathways.

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Toviwek, Borvornwat, Thanathip Suwanasopee, Skorn Koonawootrittriron, and Prapasiri Pongprayoon. "A computational insight into how human serum carnosinase 1 recognises carnosine and anserine." Biophysical Journal 121, no. 3 (February 2022): 50a—51a. http://dx.doi.org/10.1016/j.bpj.2021.11.2452.

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Guilherme, João Paulo Limongi França, and Antonio Herbert Lancha. "Single Nucleotide Polymorphisms in Carnosinase Genes (CNDP1 and CNDP2) are Associated With Power Athletic Status." International Journal of Sport Nutrition and Exercise Metabolism 27, no. 6 (December 2017): 533–42. http://dx.doi.org/10.1123/ijsnem.2017-0098.

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Carnosine (β-alanyl-L-histidine), abundantly found in skeletal muscle, plays an important role during exercise, especially for high-intensity contractions. Variability in muscle carnosine content between individuals exists and may also be explained by different genetic bases, although no study has addressed the association of polymorphisms in genes related to carnosine metabolism in athletes. This study aimed to investigate the frequency of single nucleotide polymorphisms (SNPs) in the carnosinase genes (CNDP1 and CNDP2) in a large Brazilian cohort of athletes and nonathletes. Eight SNPs were compared between a representative cohort of elite athletes from Brazil (n = 908) and a paired group of nonathletes (n = 967). The athletes were stratified into three groups: endurance (n = 328), power (n = 415), and combat (n = 165). The CNDP2 rs6566810 (A/A genotype) is overrepresented in endurance athletes, but only in international-level endurance athletes. Three SNPs (CNDP2 rs3764509, CNDP2-CNDP1 rs2346061, and CNDP1 rs2887) were overrepresented in power athletes compared with nonathletes. Carriers of the minor allele had an increased odds ratio of being a power athlete. For the rs2346061, no significant difference was observed in genotype frequencies between power and combat sports athletes, but for rs2887 the power and combat groups showed an inverse genotype distribution. In conclusion, we found that minor alleles carriers for CNDP2 rs3764509 (G-allele), CNDP2-CNDP1 rs2346061 (C-allele), and CNDP1 rs2887 (A-allele) are more likely to be a power athlete. These polymorphisms may be novel genetic markers for power athletes. Furthermore, these results are suggestive of a distinct CNDP genotype for sporting development.

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Wassif, W. S., R. A. Sherwood, N. Leigh, and T. J. Peters. "Serum Carnosinase Activities in Neurological Disorders." Clinical Science 86, s30 (February 1, 1994): 25P. http://dx.doi.org/10.1042/cs086025p.

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Inaba, Chiaki, Shinsuke Higuchi, Hironobu Morisaka, Kouichi Kuroda, and Mitsuyoshi Ueda. "Synthesis of functional dipeptide carnosine from nonprotected amino acids using carnosinase-displaying yeast cells." Applied Microbiology and Biotechnology 86, no. 6 (January 15, 2010): 1895–902. http://dx.doi.org/10.1007/s00253-009-2396-7.

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Boldyrev, Alexander A., Giancarlo Aldini, and Wim Derave. "Physiology and Pathophysiology of Carnosine." Physiological Reviews 93, no. 4 (October 2013): 1803–45. http://dx.doi.org/10.1152/physrev.00039.2012.

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Carnosine (β-alanyl-l-histidine) was discovered in 1900 as an abundant non-protein nitrogen-containing compound of meat. The dipeptide is not only found in skeletal muscle, but also in other excitable tissues. Most animals, except humans, also possess a methylated variant of carnosine, either anserine or ophidine/balenine, collectively called the histidine-containing dipeptides. This review aims to decipher the physiological roles of carnosine, based on its biochemical properties. The latter include pH-buffering, metal-ion chelation, and antioxidant capacity as well as the capacity to protect against formation of advanced glycation and lipoxidation end-products. For these reasons, the therapeutic potential of carnosine supplementation has been tested in numerous diseases in which ischemic or oxidative stress are involved. For several pathologies, such as diabetes and its complications, ocular disease, aging, and neurological disorders, promising preclinical and clinical results have been obtained. Also the pathophysiological relevance of serum carnosinase, the enzyme actively degrading carnosine into l-histidine and β-alanine, is discussed. The carnosine system has evolved as a pluripotent solution to a number of homeostatic challenges. l-Histidine, and more specifically its imidazole moiety, appears to be the prime bioactive component, whereas β-alanine is mainly regulating the synthesis of the dipeptide. This paper summarizes a century of scientific exploration on the (patho)physiological role of carnosine and related compounds. However, far more experiments in the fields of physiology and related disciplines (biology, pharmacology, genetics, molecular biology, etc.) are required to gain a full understanding of the function and applications of this intriguing molecule.

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Baguet, Audrey, Harmen Reyngoudt, Andries Pottier, Inge Everaert, Stefanie Callens, Eric Achten, and Wim Derave. "Carnosine loading and washout in human skeletal muscles." Journal of Applied Physiology 106, no. 3 (March 2009): 837–42. http://dx.doi.org/10.1152/japplphysiol.91357.2008.

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Carnosine (β-alanyl-l-histidine) is present in high concentrations in human skeletal muscles. The oral ingestion of β-alanine, the rate-limiting precursor in carnosine synthesis, has been shown to elevate the muscle carnosine content both in trained and untrained humans. Little human data exist about the dynamics of the muscle carnosine content, its metabolic regulation, and its dependence on muscle fiber type. The present study aimed to investigate in three skeletal muscle types the supplementation-induced amplitude of carnosine synthesis and its subsequent elimination on cessation of supplementation (washout). Fifteen untrained males participated in a placebo-controlled double-blind study. They were supplemented for 5–6 wk with either 4.8 g/day β-alanine or placebo. Muscle carnosine was quantified in soleus, tibialis anterior, and medial head of the gastrocnemius by proton magnetic resonance spectroscopy (MRS), before and after supplementation and 3 and 9 wk into washout. The β-alanine supplementation significantly increased the carnosine content in soleus by 39%, in tibialis by 27%, and in gastrocnemius by 23% and declined postsupplementation at a rate of 2–4%/wk. Average muscle carnosine remained increased compared with baseline at 3 wk of washout (only one-third of the supplementation-induced increase had disappeared) and returned to baseline values within 9 wk at group level. Following subdivision into high responders (+55%) and low responders (+15%), washout period was 15 and 6 wk, respectively. In the placebo group, carnosine remained relatively constant with variation coefficients of 9–15% over a 3-mo period. It can be concluded that carnosine is a stable compound in human skeletal muscle, confirming the absence of carnosinase in myocytes. The present study shows that washout periods for crossover designs in supplementation studies for muscle metabolites may sometimes require months rather than weeks.

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Pavlin, Matic, Giulia Rossetti, Marco De Vivo, and Paolo Carloni. "Carnosine and Homocarnosine Degradation Mechanisms by the Human Carnosinase Enzyme CN1: Insights from Multiscale Simulations." Biochemistry 55, no. 19 (May 4, 2016): 2772–84. http://dx.doi.org/10.1021/acs.biochem.5b01263.

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Dieter, B. P., C. J. Macias, T. J. Sharpe, B. Roberts, M. Wille, A. Young, C. Reisenauer, B. Cantrell, and W. M. Bayly. "Transdermal delivery of carnosine into equine skeletal muscle." Comparative Exercise Physiology 17, no. 5 (September 14, 2021): 429–34. http://dx.doi.org/10.3920/cep200077.

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The dipeptide carnosine consists of β-alanine and L-histidine. It plays a major role in skeletal muscle metabolism, especially as an intracellular buffer and antioxidant. Increasing intramuscular carnosine has been shown to improve recovery from exercise and increase anaerobic threshold and time-to-exhaustion. Dietary supplementation with carnosine does not effectively increase intramuscular carnosine due to the presence of carnosinase in the blood. However, an effective transdermal delivery process could expediently increase intramuscular concentrations of carnosine. This study’s objective was to examine the efficacy of a transdermal system for delivering carnosine into the skeletal muscle of horses, using a randomised, placebo controlled, crossover study. Carnosine plus a proprietary transdermal delivery agent or the agent alone (placebo) were applied to the middle gluteal muscles of 10 Thoroughbred racehorses, and muscle biopsies were taken before and 30, 60, and 120 min after application. Muscle carnosine concentration was measured using an enzyme-linked immunosorbent assay. A two-way repeated measures analysis of variance was used to test for the main effects of time and treatment (placebo or carnosine) as well as an interaction between time and treatment. Independent F-tests examined the change in intramuscular carnosine levels from baseline to each time point (30, 60, and 120 min). There was a significant main effect of treatment (P=0.004), no significant main effect for time (P=0.18), and a non-significant interaction of treatment with time (P=0.08). Mean intramuscular carnosine concentrations increased from baseline to 120 min. Compared to concentrations following placebo application, carnosine was greater by ~35% at 30 min (P=0.002) and ~46% after 60 min (P=0.044), but not at 120 min (P=0.20). The results indicated that intramuscular carnosine can be increased using a transdermal delivery system within 60 min of application which could have important implications for the health of horses, and their capacity to perform and recover from physical activity.

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Cohen, M., P. L. Hartlage, N. Krawiecki, R. A. Roesel, A. L. Carter, and F. A. Homines. "SERUM CARNOSINASE DEFICIENCY: A NON-DISABLING PHENOTYPE?" Journal of Intellectual Disability Research 29, no. 4 (June 28, 2008): 383–89. http://dx.doi.org/10.1111/j.1365-2788.1985.tb00364.x.

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36

Wołos, A., Z. Luberda, A. Ciereszko, and R. Babiński. "Some biochemical properties of swine uterus carnosinase." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 80, no. 1 (January 1985): 135–38. http://dx.doi.org/10.1016/0305-0491(85)90434-1.

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Jackson, Mel C., Christine M. Kucera, and James F. Lenney. "Purification and properties of human serum carnosinase." Clinica Chimica Acta 196, no. 2-3 (February 1991): 193–205. http://dx.doi.org/10.1016/0009-8981(91)90073-l.

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Arai, Yukio, and Norio Sakuragawa. "Purification and characterization of human placental carnosinase." Pediatric Neurology 11, no. 2 (September 1994): 175. http://dx.doi.org/10.1016/0887-8994(94)90490-1.

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Weigand, Tim, Florian Colbatzky, Tilman Pfeffer, Sven F. Garbade, Kristina Klingbeil, Florian Colbatzky, Michael Becker, et al. "A Global Cndp1-Knock-Out Selectively Increases Renal Carnosine and Anserine Concentrations in an Age- and Gender-Specific Manner in Mice." International Journal of Molecular Sciences 21, no. 14 (July 10, 2020): 4887. http://dx.doi.org/10.3390/ijms21144887.

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Carnosinase 1 (CN1) is encoded by the Cndp1 gene and degrades carnosine and anserine, two natural histidine-containing dipeptides. In vitro and in vivo studies suggest carnosine- and anserine-mediated protection against long-term sequelae of reactive metabolites accumulating, e.g., in diabetes mellitus. We have characterized the metabolic impact of CN1 in 11- and 55-week-old Cndp1-knockout (Cndp1-KO) mice and litter-matched wildtypes (WT). In Cndp1-KO mice, renal carnosine and anserine concentrations were gender-specifically increased 2- to 9-fold, respectively in the kidney and both most abundant in the renal cortex, but remained unchanged in all other organs and in serum. Renal oxidized/reduced glutathione concentrations, renal morphology and function were unaltered. In Cndp1-KO mice at week 11, renal asparagine, serine and glutamine levels and at week 55, renal arginine concentration were reduced. Renal heat-shock-protein 70 (Hspa1a/b) mRNA declined with age in WT but not in Cndp1-KO mice, transcription factor heat-shock-factor 1 was higher in 55-week-old KO mice. Fasting blood glucose concentrations decreased with age in WT mice, but were unchanged in Cndp1-KO mice. Blood glucose response to intraperitoneal insulin was gender- but not genotype-dependent, the response to intraperitoneal glucose injection was similar in all groups. A global Cndp1-KO selectively, age- and gender-specifically, increases renal carnosine and anserine concentrations, alters renal amino acid- and HSP70 profile and modifies systemic glucose homeostasis. Increase of the natural occurring carnosine and anserine levels in the kidney by modulation of CN1 represents a promising therapeutic approach to mitigate or prevent chronic kidney diseases such as diabetic nephropathy.

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Adelmann, Katja, Dirk Frey, Eva Riedl, Hannes Koeppel, Frederick Pfister, Verena Peters, Claus P. Schmitt, et al. "Different conformational forms of serum carnosinase detected by a newly developed sandwich ELISA for the measurements of carnosinase concentrations." Amino Acids 43, no. 1 (February 17, 2012): 143–51. http://dx.doi.org/10.1007/s00726-012-1244-8.

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Wassif, W. S., R. A. Sherwood, A. Amir, B. Idowu, B. Summers, N. Leigh, and T. J. Peters. "Serum carnosinase activities in central nervous system disorders." Clinica Chimica Acta 225, no. 1 (February 1994): 57–64. http://dx.doi.org/10.1016/0009-8981(94)90027-2.

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LENNEY, James F. "Separation and Characterization of Two Carnosine-Splitting Cytosolic Dipeptidases from Hog Kidney (Carnosinase and Non-Specific Dipeptidase)." Biological Chemistry Hoppe-Seyler 371, no. 1 (January 1990): 433–40. http://dx.doi.org/10.1515/bchm3.1990.371.1.433.

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Peters, Verena, Erwin E. W. Jansen, Cornelis Jakobs, Eva Riedl, Bart Janssen, Benito A. Yard, Johannes Wedel, et al. "Anserine inhibits carnosine degradation but in human serum carnosinase (CN1) is not correlated with histidine dipeptide concentration." Clinica Chimica Acta 412, no. 3-4 (January 2011): 263–67. http://dx.doi.org/10.1016/j.cca.2010.10.016.

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Zhou, Zhou, Xue-qi Liu, Shi-qi Zhang, Xiang-ming Qi, Qiu Zhang, Benito Yard, and Yong-gui Wu. "Correlation between serum carnosinase concentration and renal damage in diabetic nephropathy patients." Amino Acids 53, no. 5 (April 3, 2021): 687–700. http://dx.doi.org/10.1007/s00726-021-02975-z.

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AbstractDiabetic nephropathy (DN) is one of the major complications of diabetes and contributes significantly towards end-stage renal disease. Previous studies have identified the gene encoding carnosinase (CN-1) as a predisposing factor for DN. Despite this fact, the relationship of the level of serum CN-1 and the progression of DN remains uninvestigated. Thus, the proposed study focused on clarifying the relationship among serum CN-1, indicators of renal function and tissue injury, and the progression of DN. A total of 14 patients with minimal changes disease (MCD) and 37 patients with DN were enrolled in the study. Additionally, 20 healthy volunteers were recruited as control. Further, DN patients were classified according to urinary albumin excretion rate into two groups: DN with microalbuminuria (n = 11) and DN with macroalbuminuria (n = 26). Clinical indicators including urinary protein components, serum carnosine concentration, serum CN-1 concentration and activity, and renal biopsy tissue injury indexes were included for analyzation. The serum CN-1 concentration and activity were observed to be the highest, but the serum carnosine concentration was the lowest in DN macroalbuminuria group. Moreover, within DN group, the concentration of serum CN-1 was positively correlated with uric acid (UA, r = 0.376, p = 0.026) and serum creatinine (SCr, r = 0.399, p = 0.018) and negatively correlated with serum albumin (Alb, r = − 0.348, p = 0.041) and estimated glomerular filtration rate (eGRF, r = − 0.432, p = 0.010). Furthermore, the concentration of serum CN-1 was discovered to be positively correlated with indicators including 24-h urinary protein–creatinine ratio (24 h-U-PRO/CRE, r = 0.528, p = 0.001), urinary albumin-to-creatinine ratio (Alb/CRE, r = 0.671, p = 0.000), urinary transferrin (TRF, r = 0.658, p = 0.000), retinol-binding protein (RBP, r = 0.523, p = 0.001), N-acetyl-glycosaminidase (NAG, r = 0.381, p = 0.024), immunoglobulin G (IgG, r = 0.522, p = 0.001), cystatin C (Cys-C, r = 0.539, p = 0.001), beta-2-microglobulin (β2-MG, r = 0.437, p = 0.009), and alpha-1-macroglobulin (α1-MG, r = 0.480, p = 0.004). Besides, in DN with macroalbuminuria group, serum CN-1 also showed a positive correlation with indicators of fibrosis, oxidative stress, and renal tubular injury. Taken together, our data suggested that the level of CN-1 was increased as clinical DN progressed. Thus, the level of serum CN-1 might be an important character during the occurrence and progression of DN. Our study will contribute significantly to future studies focused on dissecting the underlying mechanism of DN.

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Jain, Saurabh, Eun-Sun Kim, Donghyun Kim, David Burrows, Milena De Felice, Minyeong Kim, Seung-Hoon Baek, et al. "Comparative Cerebroprotective Potential of d- and l-Carnosine Following Ischemic Stroke in Mice." International Journal of Molecular Sciences 21, no. 9 (April 26, 2020): 3053. http://dx.doi.org/10.3390/ijms21093053.

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l-carnosine is an attractive therapeutic agent for acute ischemic stroke based on its robust preclinical cerebroprotective properties and wide therapeutic time window. However, large doses are needed for efficacy because carnosine is rapidly degraded in serum by carnosinases. The need for large doses could be particularly problematic when translating to human studies, as humans have much higher levels of serum carnosinases. We hypothesized that d-carnosine, which is not a substrate for carnosinases, may have a better pharmacological profile and may be more efficacious at lower doses than l-carnosine. To test our hypothesis, we explored the comparative pharmacokinetics and neuroprotective properties of d- and L-carnosine in acute ischaemic stroke in mice. We initially investigated the pharmacokinetics of d- and L-carnosine in serum and brain after intravenous (IV) injection in mice. We then investigated the comparative efficacy of d- and l-carnosine in a mouse model of transient focal cerebral ischemia followed by in vitro testing against excitotoxicity and free radical generation using primary neuronal cultures. The pharmacokinetics of d- and l-carnosine were similar in serum and brain after IV injection in mice. Both d- and l-carnosine exhibited similar efficacy against mouse focal cerebral ischemia. In vitro studies in neurons showed protection against excitotoxicity and the accumulation of free radicals. d- and l-carnosine exhibit similar pharmacokinetics and have similar efficacy against experimental stroke in mice. Since humans have far higher levels of carnosinases, d-carnosine may have more favorable pharmacokinetics in future human studies.

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Regazzoni, Luca, Laura Fumagalli, Angelica Artasensi, Silvia Gervasoni, Ettore Gilardoni, Angelica Mazzolari, Giancarlo Aldini, and Giulio Vistoli. "Cyclo(His-Pro) Exerts Protective Carbonyl Quenching Effects through Its Open Histidine Containing Dipeptides." Nutrients 14, no. 9 (April 23, 2022): 1775. http://dx.doi.org/10.3390/nu14091775.

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Cyclo(His-Pro) (CHP) is a cyclic dipeptide which is endowed with favorable pharmacokinetic properties combined with a variety of biological activities. CHP is found in a number of protein-rich foods and dietary supplements. While being stable at physiological pH, CHP can open yielding two symmetric dipeptides (His-Pro, Pro-His), the formation of which might be particularly relevant from dietary CHP due to the gastric acidic environment. The antioxidant and protective CHP properties were repeatedly reported although the non-enzymatic mechanisms were scantly investigated. The CHP detoxifying activity towards α,β unsaturated carbonyls was never investigated in detail, although its open dipeptides might be effective as already observed for histidine containing dipeptides. Hence, this study investigated the scavenging properties of TRH, CHP and its open derivatives towards 4-hydroxy-2-nonenal. The obtained results revealed that Pro-His possesses a marked activity and is more reactive than l-carnosine. As investigated by DFT calculations, the enhanced reactivity can be ascribed to the greater electrophilicity of the involved iminium intermediate. These findings emphasize that the primary amine (as seen in l-carnosine) can be replaced by secondary amines with beneficial effects on the quenching mechanisms. Serum stability of the tested peptides was also evaluated, showing that Pro-His is characterized by a greater stability than l-carnosine. Docking simulations suggested that its hydrolysis can be catalyzed by serum carnosinase. Altogether, the reported results evidence that the antioxidant CHP properties can be also due to the detoxifying activity of its open dipeptides, which might be thus responsible for the beneficial effects induced by CHP containing food.

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Chen, Ying, Thomas V. Getchell, D. Larry Sparks, and Marilyn L. Getchell. "Cellular Localization of Carnosinase in the Human Nasal Mucosa." Acta Oto-Laryngologica 114, no. 2 (January 1994): 193–98. http://dx.doi.org/10.3109/00016489409126041.

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Janssen, B., D. Hohenadel, P. Brinkkoetter, V. Peters, N. Rind, C. Fischer, I. Rychlik, et al. "Carnosine as a Protective Factor in Diabetic Nephropathy: Association With a Leucine Repeat of the Carnosinase Gene CNDP1." Diabetes 54, no. 8 (July 25, 2005): 2320–27. http://dx.doi.org/10.2337/diabetes.54.8.2320.

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Lanza, Valeria, Francesco Bellia, Roberta D'Agata, Giuseppe Grasso, Enrico Rizzarelli, and Graziella Vecchio. "New glycoside derivatives of carnosine and analogs resistant to carnosinase hydrolysis: Synthesis and characterization of their copper(II) complexes." Journal of Inorganic Biochemistry 105, no. 2 (February 2011): 181–88. http://dx.doi.org/10.1016/j.jinorgbio.2010.10.014.

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Riedl, Eva, Hannes Koeppel, Frederick Pfister, Verena Peters, Sibylle Sauerhoefer, Paula Sternik, Paul Brinkkoetter, et al. "N-Glycosylation of Carnosinase Influences Protein Secretion and Enzyme Activity." Diabetes 59, no. 8 (May 11, 2010): 1984–90. http://dx.doi.org/10.2337/db09-0868.

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Journal articles on the topic 'Carnosinase'

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