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1
Ferreira Matos, Victor Araújo, Nailton José Brandão De Albuquerque Filho, Victor Hugo de Oliveira Segundo, et al. "Aspectos atuais sobre beta alanina, carnosina e exercício físico." Revista Brasileira de Fisiologia do Exerc&iacute cio 15, no. 1 (2022): 56–60. http://dx.doi.org/10.33233/rbfe.v15i1.37.
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A carnosina é um dipeptídeo encontrado em concentrações elevadas no músculo esquelético humano, sintetizado a partir dos aminoácidos Beta alanina e histidina, tendo a beta alanina como precursor. Recentemente, foi demonstrado que níveis elevados de carnosina podem ser benéficos ao desempenho desportivo, através do tamponamento dos íons de hidrogênio, por minimizar a redução do pH intramuscular durante o exercício. Fatores como idade, sexo, tipo de fibra muscular e alimentação também são considerados variáveis determinantes nas concentrações desse composto. Logo, o objetivo desta revisão narrativa foi analisar os principais estudos que relataram sobre os fatores determinantes da concentração de carnosina intramuscular e os potenciais efeitos na performance esportiva através da suplementação de beta alanina. A presente revisão detectou que a suplementação de beta alanina pode ser considerada um recurso eficiente para o aumento no estoque dos níveis de carnosina em diversas populações como indivíduos fisicamente ativos, atletas e idosos, de ambos os sexos, além de melhorar o rendimento em modalidades esportivas e exercícios nas quais predominem alta intensidade.Palavras-chave: β-alanina, carnosina muscular, fadiga muscular, tamponamento intramuscular.
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Shaheed, Haneen Subhee, and Shatha Hussein Ali. "Association of Carnosinase-1 Gene Polymorphism with Serum Carnosine and Carnosinease-1 Isoform Levels in Type 2 Diabetics with Cardiovascular Diseases in Iraq." Al-Rafidain Journal of Medical Sciences ( ISSN 2789-3219 ) 4 (June 25, 2023): 109–17. http://dx.doi.org/10.54133/ajms.v4i.121.
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Background: Genetic variations in the carnosinase-1 gene, which may also be associated with cardiovascular issues and result in a higher serum carnosinease-1 level, may affect the levels of carnosine and carnosine synthase in diabetes patients. Objective: To examine the impact of the Carnosineas-1 gene polymorphism SNP (rs 2887) on blood levels of carnosine and carnosine synthase-1 and their relationship to CVD in diabetes. Method: The serum concentrations of carnosine and carnosineas-1 were determined using ELISA-specific kits. The carnosineas-1 gene (CN1) was subjected to the high-resolution melt technique (HRM) with the purpose of identifying gene polymorphisms. Results: Carnosinase-1 levels were considerably raised in the T2DM with CVD group, but serum carnosine levels were significantly higher in both groups. SNPs had little impact on serum carnosine levels, whereas polymorphisms had a big impact on carnosinase-1 levels. Conclusion: By raising serum levels of carnosenease-1, which in turn increases carnosine breakdown, the SNP (rs2887) of the carnosinase-1 gene contributes indirectly to the development of CVD in T2DM.
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França, Elias, Fábio Santos Lira, Marcio Flávio Ruaro, et al. "The antioxidant effect of beta-alanine or carnosine supplementation on exercise- induced oxidative stress: a systematic review and meta-analysis." Revista Intertox de Toxicologia, Risco Ambiental e Sociedade 12, no. 3 (2019): 21. http://dx.doi.org/10.22280/revintervol12ed3.452.
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O objetivo deste estudo foi realizar uma revisão sistemática e meta-análise dos artigos que abordaram o efeito da suplementação de BA ou carnosina sobre o estresse oxidativo (TE) induzido pelo exercício físico (EF). Antes de maio de 2018, pesquisamos em todo PubMed, CAPES Periodic e SPORTDiscus modelo humano de revisão por pares, estudos randomizados de controle com suplementação crônica de BA ou carnosina em SO induzida por PE. Um total de 128 citações foram encontradas. Apenas quatro artigos preencheram critérios para inclusão. Todos os quatro estudos utilizaram jovens saudáveis, sedentários, recreativos ou atléticos. Após uma suplementação crônica com BA ou carnosina, os estudos avaliaram a SG induzida por PE imediatamente e várias horas após o exercício (0,5 a 48 h). Em resposta ao SO induzido por PE, quando comparado ao placebo, a suplementação com BA / carnosina aumentou a capacidade antioxidante total [TAC; Tamanho do Efeito (ES) = 0,35, Intervalo de Confiança 95% (CI) 0,06 a 0,65, p = 0,02] e concentrações de glutationa (GSH; ES = 0,75, IC 95% 0,32 a 1,19, p = 0,0007) enquanto diminuiu os marcadores OS diretos ( ES = -1,19, IC 95% -1,48 a -0,80, p
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Santos, Eduardo Figueirêdo dos, Luana Bernardes de Oliveira, and Maína Ribeiro Pereira-Castro. "Avaliação da suplementação de beta-alanina no desempenho esportivo." Research, Society and Development 12, no. 6 (2023): e20712642214. http://dx.doi.org/10.33448/rsd-v12i6.42214.
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A suplementação de beta-alanina tem sido amplamente utilizada como um suplemento alimentar para melhorar o desempenho físico. Seus efeitos positivos estão associados ao aumento da carnosina muscular, que proporciona maior resistência e redução da fadiga durante os treinos em diferentes modalidades esportivas. Posto isso, este artigo tem como objetivo apresentar uma revisão bibliográfica narrativa que explora os benefícios da suplementação de beta-alanina no desempenho esportivo e sua influência na composição corporal. A revisão também enfoca o papel da beta-alanina na formação da carnosina, um composto dipeptídeo presente naturalmente no corpo humano. Os resultados destacam que a beta-alanina apresenta benefícios no desempenho físico, com apenas um efeito colateral facilmente evitado, contribuindo para a melhoria da resistência e redução da fadiga muscular durante os treinos de resistência. Os estudos investigados demonstram que a suplementação de beta-alanina contribui para o melhor desenvolvimento do exercício, elevando os níveis de carnosina e minimizando a sensação de fadiga, resultando em aprimoramento do rendimento físico.
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Souza, dos Santos Thiago, Barbosa dos Santos Nicolly Marinho, and Santos Fernanda Gabriella Dos. "EFEITOS DA SUPLEMENTAÇÃO DE BETA-ALANINA EM ADULTOS PRATICANTES DE ENDURANCE." Congresso Nacional de Projeto, Pesquisa e Extensão do Instituto Thetona 01 (April 13, 2024): 12. https://doi.org/10.5281/zenodo.10969245.
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Nas últimas décadas, com o avanço tecnológico, novos suplementos nutricionais têm surgido e tomado espaço no âmbito esportivo como ferramenta para garantir o corpo desejado e atingir uma melhor performance. Nesse contexto, a beta-alanina é introduzida ao mercado nacional. Este aminoácido é um intermediário na síntese de carnosina, um dipepitídeo presente principalmente no músculo esquelético que desempenha função de diminuir a acidez muscular retardando a fadiga durante a prática de exercício físico. A beta-alanina tem apresentado garantia de efetividade nas pesquisas científicas e por isso, faz-se necessário um maior aprofundamento sobre o tema. O objetivo geral do presente estudo foi avaliar os efeitos da suplementação de beta-alanina em adultos praticantes de Endurance. Quanto aos procedimentos metodológicos, a revisão bibliográfica foi desenvolvida a partir de estudos exploratórios sobre a suplementação nutricional de beta-alanina. Foram realizadas buscas através do banco de dado PUBMED, por meio de artigos científicos publicados entre 2010 e 2023, nos idiomas português e inglês. A suplementação de beta-alanina aumenta os níveis de carnosina intramuscular, o que resulta em uma diminuição da fadiga muscular e consequentemente, um melhor desempenho em exercícios de alta intensidade, possibilitando um maior rendimento no treino. Dessa forma, o estudo permite observar como a suplementação age no metabolismo de adultos praticantes de Endurance assim como, os seus efeitos adversos e as principais características fisiológicas e funcionais.
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Everaert, Inge, Youri Taes, Emile De Heer, et al. "Low plasma carnosinase activity promotes carnosinemia after carnosine ingestion in humans." American Journal of Physiology-Renal Physiology 302, no. 12 (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, 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 (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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Kiyomi Vechiato Kawai et al., Giulia. "Efeito da carnosina na criopreservação de sêmen de garanhões com baixa congelabilidade." Revista Acadêmica: Ciência Animal 15 (July 21, 2017): 141. http://dx.doi.org/10.7213/academica.15.s01.2017.70.
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Artasensi, Angelica, Sarah Mazzotta, Ines Sanz, et al. "Exploring Secondary Amine Carnosine Derivatives: Design, Synthesis, and Properties." Molecules 29, no. 21 (2024): 5083. http://dx.doi.org/10.3390/molecules29215083.
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Carnosine is a naturally occurring dipeptide that has been advocated by some authors as an interesting scaffold for the development of potential therapeutic agents in view of the positive outcomes of its supplementation in animal models of human diseases. Its mode of action seems to depend on the quenching of toxic electrophiles, such as 4–hydroxynonenal (HNE). However, carnosine’s bioavailability in humans is lower than that in other mammals. The main reason for such an unfavorable pharmacokinetic profile is the activity of the enzyme human serum carnosinase (E.C. 3.4.13.20), which rapidly hydrolyzes carnosine upon absorption. Therefore, some studies have focused on the design of carnosinase-resistant derivatives that retain binding activity toward toxic electrophiles. Nevertheless, the structural modification of the N-terminus amino group of carnosine has rarely been considered, possibly because of its key role in the electrophile scavenging mechanism. This was proven, since some carnosine N-terminus modification generated inactive compounds, despite some derivatives retaining oral bioavailability and gaining resistance to carnosinase hydrolysis. Herein, we therefore report a study aimed at exploring whether the amino group of carnosine can be conveniently modified to develop carnosinase-resistant derivatives retaining the dipeptide activity toward toxic electrophiles.
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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 (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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Macarini, José Roberto, Soliany Grassi Maravai, José Henrique Cararo, et al. "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 (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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Rezende de Carvalho, Julio Cesar, Renan Rodrigues Calil, José Augusto Moraes Jacob, Bruno César Do Nascimento Souza, Rycharles Rudson Medeiros de Melo, and Carlos Alberto Rangearo Peres. "EFEITOS DA BETA-ALANINA DURANTE A PRÁTICA DE EXERCÍCIOS FÍSICOS – REVISÃO DA LITERATURA." Revista de Patologia do Tocantins 10, no. 2 (2023): 98–103. http://dx.doi.org/10.20873/10.20873/uft.2446-6492.2023v10n2p98.
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Introdução – A beta-alanina é um aminoácido com papel fundamental no metabolismo muscular. Ela é encontrada naturalmente no organismo humano, mas também pode ser consumida através de suplementação. Metodologia – Esse estudo de revisão da literatura foi desenvolvido por busca de artigos indexados, estudos longitudinais, transversais e ensaios clínicos, no qual foram encontrados 80 artigos no período de 2004 a 2022. Resultados – Foram encontrados um total de 80 artigos sendo 30 da base de dados PubMed MEDLINE, 20 SciELO, 18 CDSR e 12 BVS sendo que um total de 6 estudos foram selecionados para a revisão sistemática. Conclusão – Suplementação de beta-alanina pode ser uma estratégia eficaz para melhorar o desempenho atlético. Ela aumenta os níveis de carnosina nos músculos, retardando a fadiga muscular, reduzindo o acúmulo de ácido lático e protegendo as células musculares contra danos oxidativos.
 Palavras-chave: BETA ALANINA.CARNOSINA.EXERCÍCIOS.
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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 (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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Blancquaert, L., I. Everaert, A. Baguet, 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 (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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Antonova, N. A., G. M. Sorokoumova, T. N. Fedorova, et al. "CARNOSINE-CONTAINING LIPOSOMES: PREPARATION AND PROPERTIES." Fine Chemical Technologies 11, no. 6 (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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Wetzel, Charlotte, Tilman Pfeffer, Ruben Bulkescher, et al. "Anserine and Carnosine Induce HSP70-Dependent H2S Formation in Endothelial Cells and Murine Kidney." Antioxidants 12, no. 1 (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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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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Peters, Verena, Benito Yard, and Claus Peter Schmitt. "Carnosine and Diabetic Nephropathy." Current Medicinal Chemistry 27, no. 11 (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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Bando, Keiichi, Kiyoshi Ichihara, Tsunesuke Shimotsuji, et al. "Reduced Serum Carnosinase Activity in Hypothyroidism." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 23, no. 2 (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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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 (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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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 (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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SCHÖN, M., I. JUST, P. KRUMPOLEC, et al. "Supplementation-Induced Change in Muscle Carnosine is Paralleled by Changes in Muscle Metabolism, Protein Glycation and Reactive Carbonyl Species Sequestering." Physiological Research 72, no. 1 (2023): 87–97. http://dx.doi.org/10.33549/physiolres.934911.
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Carnosine is a performance-enhancing food supplement with a potential to modulate muscle energy metabolism and toxic metabolites disposal. In this study we explored interrelations between carnosine supplementation (2 g/day, 12 weeks) induced effects on carnosine muscle loading and parallel changes in (i) muscle energy metabolism, (ii) serum albumin glycation and (iii) reactive carbonyl species sequestering in twelve (M/F=10/2) sedentary, overweight-to-obese (BMI: 30.0±2.7 kg/m2) adults (40.1±6.2 years). Muscle carnosine concentration (Proton Magnetic Resonance Spectroscopy; 1H-MRS), dynamics of muscle energy metabolism (Phosphorus Magnetic Resonance Spectroscopy; 31P-MRS), body composition (Magnetic Resonance Imaging; MRI), resting energy expenditure (indirect calorimetry), glucose tolerance (oGTT), habitual physical activity (accelerometers), serum carnosine and carnosinase-1 content/activity (ELISA), albumin glycation, urinary carnosine and carnosine-propanal concentration (mass spectrometry) were measured. Supplementation-induced increase in muscle carnosine was paralleled by improved dynamics of muscle post-exercise phosphocreatine recovery, decreased serum albumin glycation and enhanced urinary carnosine-propanal excretion (all p<0.05). Magnitude of supplementation-induced muscle carnosine accumulation was higher in individuals with lower baseline muscle carnosine, who had lower BMI, higher physical activity level, lower resting intramuscular pH, but similar muscle mass and dietary protein preference. Level of supplementation-induced increase in muscle carnosine correlated with reduction of protein glycation, increase in reactive carbonyl species sequestering, and acceleration of muscle post-exercise phosphocreatine recovery.
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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 (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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Baguet, Audrey, Inge Everaert, Benito Yard, et al. "Does low serum carnosinase activity favor high-intensity exercise capacity?" Journal of Applied Physiology 116, no. 5 (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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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 (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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Lopes Filho, Jurimar Cidade. "Revisão abrangente sobre os principais suplementos ergogenicos utilizados." Brazilian Journal of Health Review 7, no. 1 (2024): 6514–24. http://dx.doi.org/10.34119/bjhrv7n1-525.
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Objetivo: Este artigo visa oferecer uma revisão abrangente e baseada em evidências sobre o uso de suplementos ergogênicos - creatina, beta-alanina, cafeína, BCAAs e whey protein - na melhoria da performance atlética, destacando a necessidade de acompanhamento profissional e a segurança em seu uso. Métodos: A revisão foi realizada através da análise de literatura científica, incluindo estudos clínicos, revisões sistemáticas e meta-análises, focando na eficácia, mecanismos de ação, segurança e recomendações de uso dos suplementos mencionados. Resultados: Creatina: Mostrou aumento significativo nos estoques de fosfocreatina muscular, melhorando a performance em exercícios de alta intensidade. Beta-Alanina: Demonstrou capacidade de aumentar os níveis de carnosina muscular, beneficiando exercícios de média duração. Cafeína: Revelou melhorias na alerta, concentração e performance em uma variedade de atividades esportivas. BCAAs: Foram eficazes na redução da fadiga durante exercícios prolongados e na promoção da recuperação muscular. Whey Protein: Destacou-se na promoção da síntese proteica muscular e recuperação pós-exercício. Conclusão: Os suplementos ergogênicos podem ser ferramentas eficazes para melhorar a performance atlética e a recuperação. No entanto, seu uso deve ser sempre personalizado, baseado em uma avaliação profissional abrangente, e diferenciado do uso de esteroides anabolizantes. A educação contínua e a desmistificação desses suplementos são fundamentais para o seu uso responsável e seguro.
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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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Dieter, B. P., C. J. Macias, T. J. Sharpe, et al. "Transdermal delivery of carnosine into equine skeletal muscle." Comparative Exercise Physiology 17, no. 5 (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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Baguet, Audrey, Harmen Reyngoudt, Andries Pottier, et al. "Carnosine loading and washout in human skeletal muscles." Journal of Applied Physiology 106, no. 3 (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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Boldyrev, Alexander A., Giancarlo Aldini, and Wim Derave. "Physiology and Pathophysiology of Carnosine." Physiological Reviews 93, no. 4 (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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de Giacomi, Chiara, and Luca Regazzoni. "A Green and Cost-Effective Chromatographic Method for the Measurement of the Activity of Human Serum Carnosinase." Separations 10, no. 8 (2023): 460. http://dx.doi.org/10.3390/separations10080460.
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Carnosinase (i.e., CN1; E.C. 3.4.13.20) is an enzyme found in the sera of higher primates. CN1 preferentially catalyzes the hydrolysis of natural, orally adsorbed histidine dipeptides like carnosine (i.e., β-alanyl-L-histidine). This is the reason why carnosine has a limited use as a human food supplement or pharmacological agent, despite the promising results obtained in experiments on animal models of human diseases. Herein, an assay is reported for the measurement of serum CN1 activity. The method is intended for the screening of CN1 inhibitors able to enhance carnosine bioavailability in humans. The method was developed to monitor serum hydrolytic activity via the quantitation of one of the products of carnosine hydrolysis (i.e., histidine). Separation was achieved without using organic solvents by means of ion chromatography (IC), whereas detection was provided by UV spectroscopy. The assay herein reported is a green and cost-effective alternative to a recently published method based on hydrophilic interaction liquid chromatography (HILIC) and mass spectrometry (MS). The results show that such a method produces reliable measurements of serum hydrolytic activity and can be used for the screening of CN1 inhibitors.
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Stvolinsky, S. L., N. A. Antonova, O. I. Kulikova, et al. "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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Weigand, Tim, Florian Colbatzky, Tilman Pfeffer, 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 (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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Pfeffer, Tilman, Charlotte Wetzel, Philip Kirschner, et al. "Carnosinase-1 Knock-Out Reduces Kidney Fibrosis in Type-1 Diabetic Mice on High Fat Diet." Antioxidants 12, no. 6 (2023): 1270. http://dx.doi.org/10.3390/antiox12061270.
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Carnosine and anserine supplementation markedLy reduce diabetic nephropathy in rodents. The mode of nephroprotective action of both dipeptides in diabetes, via local protection or improved systemic glucose homeostasis, is uncertain. Global carnosinase-1 knockout mice (Cndp1-KO) and wild-type littermates (WT) on a normal diet (ND) and high fat diet (HFD) (n = 10/group), with streptozocin (STZ)-induced type-1 diabetes (n = 21–23/group), were studied for 32 weeks. Independent of diet, Cndp1-KO mice had 2- to 10-fold higher kidney anserine and carnosine concentrations than WT mice, but otherwise a similar kidney metabolome; heart, liver, muscle and serum anserine and carnosine concentrations were not different. Diabetic Cndp1-KO mice did not differ from diabetic WT mice in energy intake, body weight gain, blood glucose, HbA1c, insulin and glucose tolerance with both diets, whereas the diabetes-related increase in kidney advanced glycation end-product and 4-hydroxynonenal concentrations was prevented in the KO mice. Tubular protein accumulation was lower in diabetic ND and HFD Cndp1-KO mice, interstitial inflammation and fibrosis were lower in diabetic HFD Cndp1-KO mice compared to diabetic WT mice. Fatalities occurred later in diabetic ND Cndp1-KO mice versus WT littermates. Independent of systemic glucose homeostasis, increased kidney anserine and carnosine concentrations reduce local glycation and oxidative stress in type-1 diabetic mice, and mitigate interstitial nephropathy in type-1 diabetic mice on HFD.
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Liang, I.-Chau, Ettore Gilardoni, Islam A. Berdaweel, Knute D. Carter, and Ethan J. Anderson. "Low Plasma Carnosinase-1 Activity in Patients with Left Ventricular Systolic Dysfunction: Implications for Carnosine Therapy in Heart Failure." International Journal of Molecular Sciences 26, no. 6 (2025): 2608. https://doi.org/10.3390/ijms26062608.
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Therapeutic efficacy of histidyl dipeptides such as carnosine is hampered by circulating carnosinase-1 (CN1), which catalyzes carnosine’s hydrolysis and degradation. Prior reports suggest that oral carnosine may improve cardiometabolic parameters in patients with heart failure (HF), but whether CN1 activity is affected by HF is unknown. Here, we measured CN1 content and carnosine degradation rate (CDR) in preoperative plasma samples from a cohort of patients (n = 138) undergoing elective cardiac surgery to determine whether plasma CN1 and/or CDR varied with left ventricular (LV) systolic dysfunction. CN1 content was normally distributed in the cohort, but plasma CDR displayed a quasi-bimodal distribution into high- (>2 nmol/(h*μL)) and low-activity (≤2 nmol/(h*μL)) clusters. Multivariable analysis confirmed female sex, diabetes and LV systolic dysfunction was associated with the low-activity CDR cluster. Although CN1 content did not differ, logistic regression analysis revealed that CDR and CN1-specific activity (CDR/CN1 content) was significantly lower in patients with both moderate (ejection fraction, EF ≥ 35 to <50%) and severe LV systolic dysfunction (EF < 35%) compared with patients in the normal range (EF ≥ 50%). These findings suggest that plasma CN1 activity is regulated by factors independent of expression, and that a decline in LV systolic function is associated with low CN1 activity. Further studies are needed to delineate specific mechanisms controlling CN1 expression and activity, which will facilitate the development of carnosine and other histidyl dipeptide therapies for cardiometabolic disorders such as HF.
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Sauerhofer, S., G. Yuan, G. S. Braun, et al. "L-Carnosine, a Substrate of Carnosinase-1, Influences Glucose Metabolism." Diabetes 56, no. 10 (2007): 2425–32. http://dx.doi.org/10.2337/db07-0177.
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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 (1988): 315–18. http://dx.doi.org/10.1016/s0009-9120(88)80088-2.
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Priscylla Fernandes Vasconcelos Lino, Larruama, Mahalla Hanne dos Santos Vieira, Laura Izabele Xavier Guedes Martins, et al. "RELEVÂNCIA DE ESTRATÉGIAS NUTRICIONAIS E INTERVENÇÕES DE EDUCAÇÃO ALIMENTAR E NUTRICIONAL NO DESENVOLVIMENTO DE CRIANÇAS COM TRANSTORNO DO ESPECTRO AUTISTA (TEA)." Brazilian Journal of Implantology and Health Sciences 6, no. 6 (2024): 1797–811. http://dx.doi.org/10.36557/2674-8169.2024v6n6p1797-1811.
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O transtorno do espectro autista (TEA) é caracterizado por uma desorganização neural influenciado por múltiplos fatores genéticos, ambientais e imunológicos que desempenham um papel na sua patogênese, de modo a apresentar comprometimento no comportamento como deficiências na interação social, na linguagem, na comunicação e no jogo imaginativo, envolve um grupo de manifestações, como anormalidades metabólicas, inflamação intestinal, desequilíbrio imunológico, sintomas relacionados com o sistema gastrintestinal e problemas comportamentais. A intervenção nutricional tem um papel de suma importância no tratamento e evolução, sendo estudada como agente adjuvante da terapia da TEA, devido aos casos com melhoras significativas e diminuição dos sintomas, diminuindo carências nutricionais e problemas associados. Este estudo buscou reunir informações acerca da relevância das estratégias nutricionais e das intervenções de educação nutricional no desenvolvimento de crianças com tea, a partir de uma revisão bibliográfica. Foi realizada uma busca de artigos publicados enre os anos de 2019 e 2024, nas bases de dados PubMed e Scielo, utilizando os termos de busca relevantes, como autismo, seletividade alimentar e comportamento alimentar. Foram incluídos estudos que abordassem especificamente a alimentação seletiva em crianças com TEA. Foram excluídos artigos duplicados, artigos que não abordavam a temática da pesquisa, estudos com amostras não representativas ou com métodos inadequados, restando em 11 artigos utilizados. Observou-se que intervenções nutricionais por meio de suplemento com nutrientes diversos, como probióticos, ômega 3, vitaminas do complexo B, vitamina D, carnitina, ácido fólico e carnosina, apresentou eficácia na redução de sintomas gastrointestinais destas crianças. prática de educação nutricional, para as crianças, pais e profissionais, é primordial no tratamento da seletividade alimentar apresentada pelas mesmas e que as estratégias nutricionais e comportamentis corretas contribuem para melhores escolhas alimentares, auxiliando em um desenvolvimento mais saudável, destacando a educação nutricional como importante meio de promoção de saúde e melhoria da qualidade de vida de crianças com TEA.
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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 (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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Regazzoni, Luca, Laura Fumagalli, Angelica Artasensi, et al. "Cyclo(His-Pro) Exerts Protective Carbonyl Quenching Effects through Its Open Histidine Containing Dipeptides." Nutrients 14, no. 9 (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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Babizhayev, Mark A. "The detox strategy in smoking comprising nutraceutical formulas of non-hydrolyzed carnosine or carcinine used to protect human health." Human & Experimental Toxicology 33, no. 3 (2013): 284–316. http://dx.doi.org/10.1177/0960327113493306.
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The increased oxidative stress in patients with smoking-associated disease, such as chronic obstructive pulmonary disease, is the result of an increased burden of inhaled oxidants as well as increased amounts of reactive oxygen species generated by various inflammatory, immune and epithelial cells of the airways. Nicotine sustains tobacco addiction, a major cause of disability and premature death. In addition to the neurochemical effects of nicotine, behavioural factors also affect the severity of nicotine withdrawal symptoms. For some people, the feel, smell and sight of a cigarette and the ritual of obtaining, handling, lighting and smoking a cigarette are all associated with the pleasurable effects of smoking. For individuals who are motivated to quit smoking, a combination of pharmacotherapy and behavioural therapy has been shown to be most effective in controlling the symptoms of nicotine withdrawal. In the previous studies, we proposed the viability and versatility of the imidazole-containing dipeptide-based compounds in the nutritional compositions as the telomere protection targeted therapeutic system for smokers in combination with in vitro cellular culture techniques being an investigative tool to study telomere attrition in cells induced by cigarette smoke (CS) and smoke constituents. Our working therapeutic concept is that imidazole-containing dipeptide-based compounds (non-hydrolyzed carnosine and carcinine) can modulate the telomerase activity in the normal cells and can provide the redox regulation of the cellular function under the terms of environmental and oxidative stress and in this way protect the length and the structure of telomeres from attrition. The detoxifying system of non-hydrolyzed carnosine or carcinine can be applied in the therapeutic nutrition formulations or installed in the cigarette filter. Patented specific oral formulations of non-hydrolyzed carnosine and carcinine provide a powerful manipulation tool for targeted therapeutic inhibition of cumulative oxidative stress and inflammation and protection from telomere attrition associated with smoking. It is demonstrated in this work that both non-hydrolyzed carnosine and carcinine are characterized by greater bioavailability than pure l-carnosine subjected to enzymatic hydrolysis with carnosinase, and perform the detoxification of the α,β-unsaturated carbonyl compounds present in tobacco smoke. We argue that while an array of factors has shaped the history of the ‘safer’ cigarette, it is the current understanding of the industry’s past deceptions and continuing avoidance of the moral implications of the sale of products that cause the enormous suffering and death of millions that makes reconsideration of ‘safer’ cigarettes challenging. In contrast to this, the data presented in the article show that recommended oral forms of non-hydrolyzed carnosine and carcinine protect against CS-induced disease and inflammation, and synergistic agents with the actions of imidazole-containing dipeptide compounds in developed formulations may have therapeutic utility in inflammatory lung diseases where CS plays a role.
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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 (2022): 50a—51a. http://dx.doi.org/10.1016/j.bpj.2021.11.2452.
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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 (2010): 1895–902. http://dx.doi.org/10.1007/s00253-009-2396-7.
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O’Toole, Timothy E., Xiaohong Li, Daniel W. Riggs, David J. Hoetker, Shahid P. Baba, and Aruni Bhatnagar. "Urinary Levels of the Acrolein Conjugates of Carnosine Are Associated with Cardiovascular Disease Risk." International Journal of Molecular Sciences 22, no. 3 (2021): 1383. http://dx.doi.org/10.3390/ijms22031383.
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Carnosine is a naturally occurring dipeptide (β-alanine-L-histidine) which supports physiological homeostasis by buffering intracellular pH, chelating metals, and conjugating with and neutralizing toxic aldehydes such as acrolein. However, it is not clear if carnosine can support cardiovascular function or modify cardiovascular disease (CVD) risk. To examine this, we measured urinary levels of nonconjugated carnosine and its acrolein conjugates (carnosine-propanal and carnosine-propanol) in participants of the Louisville Healthy Heart Study and examined associations with indices of CVD risk. We found that nonconjugated carnosine was significantly associated with hypertension (p = 0.011), heart failure (p = 0.015), those categorized with high CVD risk (p < 0.001), body mass index (BMI; p = 0.007), high sensitivity C-reactive protein (hsCRP; p = 0.026), high-density lipoprotein (HDL; p = 0.007) and certain medication uses. Levels of carnosine-propanal and carnosine-propanol demonstrated significant associations with BMI, blood glucose, HDL and diagnosis of diabetes. Carnosine-propanal was also associated with heart failure (p = 0.045) and hyperlipidemia (p = 0.002), but no associations with myocardial infarction or stroke were identified. We found that the positive associations of carnosine conjugates with diabetes and HDL remain statistically significant (p < 0.05) in an adjusted, linear regression model. These findings suggest that urinary levels of nonconjugated carnosine, carnosine-propanal and carnosine-propanol may be informative biomarkers for the assessment of CVD risk—and particularly reflective of skeletal muscle injury and carnosine depletion in diabetes.
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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 (2016): 2772–84. http://dx.doi.org/10.1021/acs.biochem.5b01263.
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Haneen Subhee Shaheed and Shatha H Ali. "Genetic Polymorphisms of Carnosine Synthase -1(ATPGD1) and Serum Carnosine Levels in Relation to Cardio Vascular Diseases in Iraqi Type 2 Diabetics." Iraqi Journal of Pharmaceutical Sciences( P-ISSN 1683 - 3597 E-ISSN 2521 - 3512) 33, no. 2 (2024): 179–89. http://dx.doi.org/10.31351/vol33iss2pp179-189.
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Diabetes mellitus (DM) is a metabolic disorder specified by persistent hyperglycemia that occurs when β-cell insulin production became unable to control blood glucose with deterioration of response for insulin. The consequent development of DM complications with increased risk for many diseases caused by damaged variety of biological systems, including blood vessels, eyes, kidneys, heart, and nerves. Carnosine is a natural dipeptide (β-alanyl-L-histidine) expressed in both the central nervous system and periphery, it occurs in several tissues most notably in muscle where they represent an appreciable fraction of the total water-soluble nitrogen-containing compounds. Carnosine is synthesized by a cytosolic amino acid ligase, carnosine synthase-1 (CARNS1; also known as ATP-grasp domain–containing protein 1, ATPGD1; EC 6.3.2.11).Several biological and physiological functions have been attributed to carnosine, such as being an anti-inflammatory and antioxidant agent, antiglycating actions, and as a modulator of mitochondrial metabolism. Carnosine level in human serum is affected by several enzymes like carnosine synthase-1 (responsible of carnosine synthesis),thus any genetic polymorphisms in these enzymes could have an impact on enzymes levels and therefore serum carnosine level with consequent increased risk for many diseases. This study was aimed to estimate the occurrence of Carnosine synthase -1 SNP (rs 1790733) on chromosom11 (intron –variant) in Iraqi type 2 diabetics with and without cardio vascular diseases and it’s correlation with serum levels of carnosine & carnosine synthase-1 and their association with CVD as T2DM complication. To achieve this aim Enzyme Linked Immunosorbent Assay (ELISA) specific kits were used to estimate serum levels of carnosine & carnosine synthase-1. High resolution melt technique (HRM) was applied for detecting gene polymorphism of carnosine synthase-1 gene (ATPGD1). The results showed that gene polymorphism of SNP (rs1790733) increased the chance of CVD in T2DM patients by 84.5% by its effect to decrease the mean of serum levels of carnosine by decreased carnosine synthase-1 level that may correlate to development of CVD in T2DM patients.
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Jukić, Ivana, Nikolina Kolobarić, Ana Stupin, et al. "Carnosine, Small but Mighty—Prospect of Use as Functional Ingredient for Functional Food Formulation." Antioxidants 10, no. 7 (2021): 1037. http://dx.doi.org/10.3390/antiox10071037.
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Carnosine is a dipeptide synthesized in the body from β-alanine and L-histidine. It is found in high concentrations in the brain, muscle, and gastrointestinal tissues of humans and is present in all vertebrates. Carnosine has a number of beneficial antioxidant properties. For example, carnosine scavenges reactive oxygen species (ROS) as well as alpha-beta unsaturated aldehydes created by peroxidation of fatty acid cell membranes during oxidative stress. Carnosine can oppose glycation, and it can chelate divalent metal ions. Carnosine alleviates diabetic nephropathy by protecting podocyte and mesangial cells, and can slow down aging. Its component, the amino acid beta-alanine, is particularly interesting as a dietary supplement for athletes because it increases muscle carnosine, and improves effectiveness of exercise and stimulation and contraction in muscles. Carnosine is widely used among athletes in the form of supplements, but rarely in the population of cardiovascular or diabetic patients. Much less is known, if any, about its potential use in enriched food. In the present review, we aimed to provide recent knowledge on carnosine properties and distribution, its metabolism (synthesis and degradation), and analytical methods for carnosine determination, since one of the difficulties is the measurement of carnosine concentration in human samples. Furthermore, the potential mechanisms of carnosine’s biological effects in musculature, metabolism and on immunomodulation are discussed. Finally, this review provides a section on carnosine supplementation in the form of functional food and potential health benefits and up to the present, neglected clinical use of carnosine.
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Tanida, Mamoru, Akira Niijima, Yutaka Fukuda, et al. "Dose-dependent effects of l-carnosine on the renal sympathetic nerve and blood pressure in urethane-anesthetized rats." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 288, no. 2 (2005): R447—R455. http://dx.doi.org/10.1152/ajpregu.00275.2004.
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The physiological function of l-carnosine (β-alanyl-l-histidine) synthesized in mammalian muscles has been unclear. Previously, we observed that intravenous (IV) injection of l-carnosine suppressed renal sympathetic nerve activity (RSNA) in urethane-anesthetized rats, and l-carnosine administered via the diet inhibited the elevation of blood pressure (BP) in deoxycorticosterone acetate salt hypertensive rats. To identify the mechanism, we examined effects of IV or intralateral cerebral ventricular (LCV) injection of various doses of l-carnosine on RSNA and BP in urethane-anesthetized rats. Lower doses (1 μg IV; 0.01 μg LCV) of l-carnosine significantly suppressed RSNA and BP, whereas higher doses (100 μg IV; 10 μg LCV) elevated RSNA and BP. Furthermore, we examined effects of antagonists of histaminergic (H1 and H3) receptors on l-carnosine-induced effects. When peripherally and centrally given, thioperamide, an H3 receptor antagonist, blocked RSNA and BP decreases induced by the lower doses of peripheral l-carnosine, whereas diphenhydramine, an H1 receptor antagonist, inhibited increases induced by the higher doses of peripheral l-carnosine. Moreover, bilateral lesions of the hypothalamic suprachiasmatic nucleus eliminated both effects on RSNA and BP induced by the lower (1 μg) and higher (100 μg) doses of peripheral l-carnosine. These findings suggest that low-dose l-carnosine suppresses and high-dose l-carnosine stimulates RSNA and BP, that the suprachiasmatic nucleus and histaminergic nerve are involved in the activities, and that l-carnosine acts in the brain and possibly other organs.
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Weigand, Tim, Benjamin Singler, Thomas Fleming, et al. "Carnosine Catalyzes the Formation of the Oligo/Polymeric Products of Methylglyoxal." Cellular Physiology and Biochemistry 46, no. 2 (2018): 713–26. http://dx.doi.org/10.1159/000488727.
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Background/Aims: Reactive dicarbonyl compounds, such as methylglyoxal (MG), contribute to diabetic complications. MG-scavenging capacities of carnosine and anserine, which have been shown to mitigate diabetic nephropathy, were evaluated in vitro and in vivo. Methods: MG-induced cell toxicity was characterized by MTT and MG-H1-formation, scavenging abilities by Western Blot and NMR spectroscopies, cellular carnosine transport by qPCR and microplate luminescence and carnosine concentration by HPLC. Results: In vitro, carnosine and anserine dose-dependently reduced N-carboxyethyl lysine (CEL) and advanced glycation end products (AGEs) formation. NMR studies revealed the formation of oligo/polymeric products of MG catalyzed by carnosine or anserine. MG toxicity (0.3-1 mM) was dose-dependent for podocytes, tubular and mesangial cells whereas low MG levels (0.2 mM) resulted in increased cell viability in podocytes (143±13%, p<0.001) and tubular cells (129±3%, p<0.001). Incubation with carnosine/anserine did not reduce MG-induced toxicity, independent of incubation times and across large ranges of MG to carnosine/anserine ratios. Cellular carnosine uptake was low (<0.1% in 20 hours) and cellular carnosine concentrations remained unaffected. The putative carnosine transporter PHT1 along with the taurine transporter (TauT) was expressed in all cell types while PEPT1, PEPT2 and PHT2, also belonging to the proton-coupled oligopeptide transporter (POT) family, were only expressed in tubular cells. Conclusion: While carnosine and anserine catalyze the formation of MG oligo/polymers, the molar ratios required for protection from MG-induced cellular toxicity are not achievable in renal cells. The effect of carnosine in vivo, to mitigate diabetic nephropathy may therefore be independent upon its ability to scavenge MG and/or carnosine is mainly acting extracellularly.