• Nutrition Research and Practice
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• 제8권1호
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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.

• 대한수의학회지
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• 제39권3호
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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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• 제40권1호
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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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• 제53권4호
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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.

• 한국식품위생안전성학회지
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• 제35권5호
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• pp.513-520
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• 2020

다랑어로부터 추출한 histidine 함유 저분자 peptide의 항산화능을 평가한 결과, histidine, 1-methylhistidine, carnosine과 anserine을 포함한 histidine 관련 화합물과 다랑어에서 추출한 histidine 함유 저분자 peptide는 DPPH 라디칼 소거능력을 지녔고, 농도가 증가함에 따라 효과 또한 증가하였다. 다랑어 추출물은 2차 이온교환 처리물이 carnosine과 anserine의 dipeptide와 유사한 결과를 나타냈으며, 가열처리와 한외여과를 병행한 경우와 이온교환과 한외여과 처리를 한 동결물의 경우 ascorbic acid와 유사한 라디칼 소거능을 나타냈다. Histidine 함유 dipeptide 중에서 anserine이 가장 높은 환원력을 나타내었으며, carnosine은 두 번째로 강한 환원력을 나타내었다. Dipeptide와 비교하여 황다랑어, 눈다랑어 추출물이 높은 환원력을 나타내었으며, 농도가 증가할수록 환원력이 증가하였다. 다랑어 추출물 원육에서의 SOD 유사활성은 약했으나, 가열처리와 한외여과를 병행하였을 때, 황다랑어 눈다랑어 추출물이 농도별로 4.0-19.4%, 5.7-20.6%로 나타났으며, 이온교환과 한외여과를 병행하였을 때, 8.3-27.9%, 5.4-25.0%, 2차 이온교환 처리를 하였을 때, 8.2-29.5%, 8.6-32.1%로 활성이 증가하였다. Linoleic acid를 기질로 하여 저장기간에 따른 자동산화의 중간생성물인 과산화물의 변화를 측정한 결과 CM-cellulose의 처리 동결건조물은 ascorbic와 유사하게 지질산화능이 높은 것으로 나타났다. 인체 내의 pH 변화를 고려하여 pH 1.2, pH 3.0, pH 4.2로 조절하여 아질산염의 소거능을 살펴보았을 때, 황다랑어 추출물의 경우 25.14%, 15.09%, 13.71%, 눈다랑어 추출물은 27.44%, 18,28%, 18.09%로 pH 1.2, pH 3.0에서 carnosine과 anserine보다 낮지만 pH 4.2에서 histidine 보다 높은 소거능을 보였다.

• Bulletin of the Korean Chemical Society
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• 제29권9호
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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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• 제32권4호
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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.

• 대한화학회지
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• 제5권1호
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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.

• 한국수산과학회지
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• 제22권5호
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• pp.228-232
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• 1989

분말가쓰오부시를 물로 우릴 때 최적추출조건을 구명하고 아울러 omission test 및 관능검사를 통해서 각 정미성분의 맛에 대한 기여도를 검토하였다. 분말가쓰오부시의 최적추출조건은 $100^{\circ}C$ 1분간 끓이는 고온단시간 추출이 유효하였으며, 특히 저온장시간 추출에 비해 중$\cdot$고비점 휘발성성분이 발생하여 특유의 풍미를 생성시켰고, 또한 국물의 투명감 면에서도 우수하였다. 상기의 조건하에서 추출한 분말가쓰오부시의 국물은 핵산관련물질이 93.6mg/100ml으로 함량이 가장 많았고 다음이 유리아미노산류로 41.3mg/100ml, 유기산류 39.3mg/100ml이었다. 핵산관련물질 중에서는 IMP, inosine, AMP가 주체이었으며, histidine, anserine, taurine, carnosine 및 lactic acid가 유리아미노산 및 유기산의 주성분이었다. Omission test 및 관능검사 결과 분말가쓰오부시 국물맛에 대한 각 정미성분의 기여도는 핵산관련물질이 가장 컸고, 다음이 유리아미노산, 유기산 순이었으나 어느 한 성분의 절대적인 기여보다는 각 성분이 서로 조화를 이루고 있었다.

• 한국식품영양학회지
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• 제26권1호
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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.