• Nutrition Research and Practice
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• v.8 no.1
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• pp.3-10
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• 2014

The rapid increase in the prevalence of metabolic syndrome, which is associated with a state of elevated systemic oxidative stress and inflammation, is expected to cause future increases in the prevalence of diabetes and cardiovascular diseases. Oxidation of polyunsaturated fatty acids and sugars produces reactive carbonyl species, which, due to their electrophilic nature, react with the nucleophilic sites of certain amino acids. This leads to formation of protein adducts such as advanced glycoxidation/lipoxidation end products (AGEs/ALEs), resulting in cellular dysfunction. Therefore, an effective reactive carbonyl species and AGEs/ALEs sequestering agent may be able to prevent such cellular dysfunction. There is accumulating evidence that histidine containing dipeptides such as carnosine (${\beta}$-alanyl-L-histidine) and anserine (${\beta}$-alanyl-methyl-L-histidine) detoxify cytotoxic reactive carbonyls by forming unreactive adducts and are able to reverse glycated protein. In this review, 1) reaction mechanism of oxidative stress and certain chronic diseases, 2) interrelation between oxidative stress and inflammation, 3) effective reactive carbonyl species and AGEs/ALEs sequestering actions of histidine-dipeptides and their metabolism, 4) effects of carnosinase encoding gene on the effectiveness of histidine-dipeptides, and 5) protective effects of histidine-dipeptides against progression of metabolic syndrome are discussed. Overall, this review highlights the potential beneficial effects of histidine-dipeptides against metabolic syndrome. Randomized controlled human studies may provide essential information regarding whether histidine-dipeptides attenuate metabolic syndrome in humans.

• Korean Journal of Veterinary Research
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• v.39 no.3
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• pp.478-488
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• 1999

The contents of histidine dipeptides, a metabolic products of muscle protein, were investigated to compare muscle composition among the 9 domestic animals including cattle. In major domestic animals, analyzed the effects of age, part and sex of the animals on their muscle composition. Large amounts of carnosine($68.63{\pm}17.41{\mu}mol/g$) were detected in cattle and it was higher than other animals. Whereas the content of anserine showed high level in order of turkey, chickens and duck. The ratio of carnosine and anserine(C/A ratio) was different depending on the animal species. Statistical data indicated that difference among species was significant(p < 0.05). The contents of histidine dipeptides in heated muscle by boiling for 40 minutes at $110^{\circ}C$ was similar to thoes of raw muscle. C/A ratio in heated muscle was not different from that of raw muscle, indicating that no change has been made after heating process. The contents of carnosine and anserine were different according to the parts of their muscle. Especially chuck of the mammalian showed extremely low level of histidine dipeptides compared with other parts, while C/A ratio maintained certain level regardless of age, part, sex. Therefore, based on the content of histidine dipeptides, could be found the difference of muscle composition among the species. Also C/A ratio of horse, pig, cattle, duck, sheep and turkey were characteristic respectively.

• BMB Reports
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• v.40 no.1
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• pp.125-129
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• 2007

Neurofilament-L (NF-L) is a major element of the neuronal cytoskeleton and is essential for neuronal survival. Moreover, abnormalities in NF-L result in neurodegenerative disorders. Carnosine and the related endogeneous histidine dipeptides prevent protein modifications such as oxidation and glycation. In the present study, we investigated whether histidine dipeptides, carnosine, homocarnosine, or anserine protect NF-L against oxidative modification during reaction between cytochrome c and $H_2O_2$. Carnosine, homocarnosine and anserine all prevented cytochrome c/$H_2O_2$-mediated NF-L aggregation. In addition, these compounds also effectively inhibited the formation of dityrosine, and this inhibition was found to be associated with the reduced formations of oxidatively modified proteins. Our results suggest that carnosine and histidine dipeptides have antioxidant effects on brain proteins under pathophysiological conditions leading to degenerative damage, such as, those caused by neurodegenerative disorders.

• Journal of Nutrition and Health
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• v.53 no.4
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• pp.356-368
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• 2020

Purpose: Histidine-containing dipeptides, which are rich in chicken, have been reported to reduce the risk of metabolic abnormalities via anticarbonylation mechanism in animal models. To determine the effect of dietary histidine-containing dipeptides on metabolic risk factors in humans, the relation between chicken consumption and insulin resistance were determined in a population consuming high carbohydrate and low protein. Methods: A total of 7,183 subjects (2,929 men and 4,254 women) aged ≥ 50 years from the Korea National Health and Nutrition Examination Survey (KNHANES) were divided into three groups according to chicken consumption (rarely, monthly, and weekly), and evaluated for the metabolic risk factors using homeostasis model assessment for insulin resistance (HOMA-IR) and quantitative insulin sensitivity check index (QUICKI) in this cross-sectional study. The fourth and fifth (IV-1-3 & V-1) KNHANES, which had blood insulin data, were chosen for the current study. Results: The chicken consumption was significantly associated with insulin (p for trend = 0.018) and HOMA-IR (p for trend = 0.023) in men. In particular, the 'weekly' chicken consuming men in the lowest tertile (< 65.0%) of carbohydrate intake group had significantly lower HOMA-IR (p for trend = 0.033) and higher QUICKI (p for trend = 0.043) than the 'rarely' intake group. In addition, the odds ratio for abnormal HOMA-IR was 0.55 (95% confidence interval [CI], 0.31-0.99) and QUICKI was 0.47 (95% CI, 0.26-0.86) for the 'weekly' chicken consuming group. Conclusion: The 'weekly' chicken consumption had a beneficial effect on insulin resistance and it may partially be due to the major bioactive components in chicken, histidine-containing dipeptides.

• Journal of Food Hygiene and Safety
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• v.35 no.5
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• pp.513-520
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• 2020

Here, we evaluated the functional properties of histidine-containing low-molecular-weight (LMW) peptides obtained from tuna waste meats. As with histidine-related components composed of histidine, 1-methyl histidine and anserine, histidine-containing LMW peptides exhibited high α,α-diphenyl-β-picrylhydrazyl (DPPH) radical scavenging effect in a dose-dependent manner. Among the histidine-related dipeptides, anserine exhibited the highest reducing power followed by carnosine. By comparison with dipeptides, tuna extracts also showed similar reducing power and the activity was in a dose-dependent manner. In addition, the antioxidant activities of tuna extracts such as DPPH radical scavenging effect, reducing power, superoxide dismutase activities, and peroxide value of linoleic acid were affected by the various extraction methods.

• Bulletin of the Korean Chemical Society
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• v.29 no.9
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• pp.1732-1736
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• 2008

The endogenous dipeptides, carnosine and related compounds, are the naturally occurring dipeptides with multiple neuroprotective properties. We have examined the protective effects of carnosine, homocarnosine and anserine on the aggregation of neurofilament-L (NF-L) induced by neurotoxin, acrolein. When NF-L was incubated with acrolein in the presence of carnosine, homocarnosine or anserine, protein aggregation was inhibited in a concentration-dependent manner. These compounds inhibited the formation of protein carbonyl compounds and dityrosine in acrolein-mediated NF-L aggregates. The aggregates of NF-L displayed thioflavin T reactivity, reminiscent of amyloid. This thioflavin T reactivity was inhibited by carnosine and related compounds. This effect was associated with decreased formation of oxidatively modified proteins. Our results suggested that carnosine and related compounds might have protective effects to brain proteins under pathophysiological conditions leading to degenerative damage such as neurodegenerative disorders.

• BMB Reports
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• v.32 no.4
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• pp.350-357
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• 1999

At concentrations of 1 mM, the protective effects of carnosine and related compounds including anserine, homocarnosine, histidine, ${\beta}$-alanine were investigated against copper-catalyzed oxidative damage to deoxyribose, ascorbic acid, human serum albumin, liposome, and erythrocytes. Carnosine and anserine reduced Cu (II) to bathocuproine-reactive Cu (I) in a time- a and a dose-dependent manner while the others did not. Carnosine reduced 86% of $100\;{\mu}M$ Cu (II) in 60 min. Carnosine, homocarnosine, anserine, and histidine inhibited copper-catalyzed deoxyribose degradation by 75, 66, 65, and 45%, respectively. In the presence of $1\;{\mu}M$ Cu (II), carnosine and related compounds inhibited ascorbic acid oxidation by 55-85% after incubation for 20 min. In the presence of 0.15 mM ascorbic acid and 0.8 mM $H_2O_2$, carnosine, anserine, homocarnosine, and histidine inhibited copper-catalyzed oxidation of human serum albumin by 41, 21, 29, and 24%, respectively, as determined by carbonyl formation. These compounds also significantly inhibited copper-catalyzed liposomal lipid peroxidation as measured by malondialehyde and lipid hydroperoxides. Carnosine, anserine, homocarnosine, and histidine inhibited hemolysis of bovine erythrocytes induced by 0.1 mM Cu (II). These results suggest that histidine-containing dipeptides may play an important role in protecting against free radical-mediated tissue damage.

• Journal of the Korean Chemical Society
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• v.5 no.1
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• pp.33-37
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• 1961

We have shown that carboxy-peptidase destroys the biological activity of angiotensin octa-and deca-peptides. Since Proline occurs as the seventh amino acid from the amino end of the chain and since carboxypeptidase does not cleave proline from a peptid chain, it is evident that the heptapeptid H.asp-arg-val-tyr-ileu-his-pro.OH is formed by this hydrolysis. This peptide must then be biologically inactive. In order to determine whether the phenyl group of the C-terminal amino acid was the necessary requirement for biological activity of the octapeptide, $ala^8$ angiotensin octapeptide(amino acids of peptides numbered from amino end) was synthesized. For this synthesis the four dipeptides were prepared: carbobenzoxy-L-prolyl-L-alanine-P-nitrobenzyl-ester, m.p. $134-135^{\circ}C,$ carbobenzoxy-L-isoleucyl-imidazole benzyl-L-histidine methyl ester, m.p. $114-116^{\circ}C,$ carbobenzoxy-L-valyl-L-tyrosine hydrazide and carbobenzoxy B-benzyl-L-aspartyl-nitro-L-arginine. The first three dipeptides were obtained as crystalline compounds. Imidazole-benzyl-L-histidine was used in the hope that it would block the histidine imidazole against side reactions in steps subsequent to the formation of the C-terminal tetrapeptide. Also, it was through that the imidazole benzylated peptides would be easier to crystallize. This, however, was not the case. The tetrapeptide, carbobenzoxy-L-isoleucyl-L-im, benzyl-histidyl, L-prolyl-L-alanine-nitrobenzyl ester was not obtained in a crystalline form. Neither could the mono-or dihydrobromide of the tetrapeptide free base be induced to crystallize. Carbobenzoxy-L-valyl-L-tyrosine azide was condensed with the tetrapeptide free base to yield the protected hexapeptide; carbobenzoxy-L-valyl-L-tyrosyl-L-isoleucyl-L-im, benzyl, histidyl-L-Prolyl-L-alanine-nitrobenzyl ester. Upon removal of the carbobenzoxy group with hydrogen bromide in acetic acid an amorphous free base hexapeptide ester was obtained. This compound gave the correct C, H, N analysis and contained the six amino acids in the correct ratio. The octapeptide was obtained by condensing this hexapeptide with carbobenzoxy-B-benzyl-L-aspartyl-nitro, L-arginine using the mixed anhydride method of condensation. This amorphous product was proven to be homogenous by chromatography in two solvent systems and upon hydrolysis yielded the eight amino acids in correct ratio. The five protecting groups were removed from the octapeptide by hydrogenolysis over palladium black catalyst. Biological assay of the free peptide indicated that it possessed less than 0.1 per cent of both pressor and oxytocic activity of the phenylalanine8 angiotensin. This suggests that the phenyl group is a point of attachment between angiotensin and its biological receptor site.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.22 no.5
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• pp.228-232
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• 1989

Katsuobushi has widely been used from olden times to prepare soup stock. This study was carried out to prepare stock of powdered Katsuobushi, and to examine the extractive conditions and the contribution of principal taste compounds to its characteristic taste. The extractive condition of powdered Katsuobushi in preparing stock was the most appropriate at $100^{\circ}C$ for 1 minute boiling water-steeping method in flavor, clearance of stock. From the chemical analysis and omission test, the principal taste-active components in $4\%$ solution powdered Katsuobushi under this extractive condition were nucleotides 93.6mg/100ml, free amino acids and imidazole dipeptides 41.3mg/100ml, and non-volatile organic acids 39.3mg/100l1 in order. IMP, inosine, AMP, histidine, anserine, taurine, carnosine and lactic acid were predominant among the detected compounds.

• The Korean Journal of Food And Nutrition
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• v.26 no.1
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• pp.117-124
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• 2013

근내지방도(IMF)가 한우육의 품질 및 기능성분에 미치는 영향을 조사하기 위하여, 250두의 한우를 근내지방 함량에 따라 Low(<14%, n=96), Medium(14~17%, n=83), High(>17%; n=71) 세 그룹으로 분류하고, 7일간 숙성 후 등심육의 품질 및 기능성분을 분석하였다. 한우 등심육의 수분 함량은 IMF와 반비례하였으며, High IMF 그룹은 Low IMP 그룹에 비하여 낮은 드립 감량을 나타내었다. 기능성 didpeptide 함량은 IMF에 따라 유의적 차이가 없었으나, High IMF 그룹은 다른 그룹보다 낮은 inosine monophosphate, 높은 hypoxanthine, 낮은 histidine 함량은 나타내었다. 불포화지방산의 비율은 IMF에 따라 유의적 차이가 없었다. 저지방육의 건강지향적 가치를 고려할 때 지나친 IMF를 목표로 하는 육종 및 사양은 지양되어야 할 것으로 판단되었다.