• Applied Microscopy
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• v.33 no.4
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• pp.299-313
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• 2003

The aim of the present study was to assess the role of protein kinase C (PKC) in the development of cardiac injury following scald burn. Sprague-Dawley rats were induced a scald burn a 15% total body surface area. Phorbol 12-myristate 13-acetate (PMA, 2 mg/kg) and bisindolylmaleimide (BIS, 0.05 mg/kg) were immediately administered i.p. after burn injury. 5 h and 24 h later, heart was removed and examined biochemical assay, ultrastructural changes and stereological analysis. The activity of serum aspartate aminotransferase was significantly increased at 5h (p<0.01) and 5h+BIS (p<0.001) after burn compared with that of control. The activity of serum creatinine was significantly decreased in PMA-treated groups after burn compared with postburn 5 h. PMA caused a decrease in MPO activity and induced wavy fibers in cardiac myocytes at postburn 5 and 24h. BIS induced contraction band, separation of intercalated disk and abnormal mitochondria in cardiac myocytes at postburn 5 and 24h. In stereological analysis, treatment of rats with PMA increased volume density of myofibril and mitochondria compared with postburn 5 and 24h. Our data suggest that the activation of PKC in scald burned heart decreases inflammation and protects the myocardium.

• Journal of the Korean Society of Food Culture
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• v.28 no.1
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• pp.78-88
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• 2013

Marinated beef galbi is a traditional Korean dish cooked with soy sauce, pear juice, onion, sesame oil, and sugar. However, there are many differences in beef galbi, including flavor and physicochemical aspects, depending on cooking conditions. Therefore, the physicochemical characteristics of marinated beef galbi prepared through various recipes was evaluated for its effects on pH, texture, aging, proteolysis, heating conditions, cooking time, and flavor compounds (pyrazines, IMPs, or FAAs). There were significant differences in salt concentration (0.8~3.03%), pH (4.89~6.22), and solid soluble contents (1.34-6.31 Brix) between recipes in this study. In the Pearson assay for sensory evaluation, overall preference correlated well with texture (a well-known sensory attribute in meat evaluation). Controlling the pH of meat through soaking in lemon solution, alkali water, phosphate, and baking powder solution, improved water holding capacity as much as 9 to 15% compared with the control. The myofibril index (MFI) of marinated meat stored at $4^{\circ}C$ increased 32% with 24 hours of aging and reached 39% at 48 hours of aging, and its fragmentation was observed through microscopy. SDS-PAGE showed hydrolysis of acid-soluble collagen by the pear juice, possibly related to meat tenderness. On the basis of surface temperature, the cooking time was estimated to be 8 minutes with pan heating at $170^{\circ}C$, 6 minutes at $270{\sim}300^{\circ}C$, and 4 minutes with charcoal at $700{\sim}900^{\circ}C$. Different pyrazine compounds, such as 2-methyl-3-phenylpyrrol(2,3-b) pyrazine (the typical product of the browning reaction) was mainly detected, and IMP (one of the main taste compounds in beef) was in higher amounts with the charcoal treatment, potentially related to its flavor preference among treatments. Our results demonstrate an effective case study and cooking system for beef galbi.

• Applied Microscopy
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• v.22 no.1
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• pp.42-54
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• 1992

To understand the structural changes of the myocardial myocytes and endothelial cells in ischemic and reperfused heart, and to elucidate their roles in those conditions, the authors observed cat and rat myocardium ultrastructurally and evaluated them with morphometric techniques. In cat, mild ischemia and moderate degree reperfusion injury was induced by ligation of the anterior interventricular branch of left coronary artery and reperfusion. In rat, severe ischemia and irreversible reperfusion iniury was made using in vitro Langendorff techniques. In normal cat myocytes, the volume densities of cytoplasm, myofibrils, mitochondria, sarcoplasmic reticulum and T tubules were $0.11{\pm}0.013,\;0.51{\pm}0.096,\;0.25{\pm}0.082,\;0.09{\pm}0.008,\;0.02{\pm}0.010$ (Mean${\pm}$S.D.) respectively, and the myofibril/mitochondria ratio was $2.33{\pm}1.379$. The numerical density and average volume of mitochondria were $0.76{\pm}0.210/{\mu}m^3$ and $0.33{\pm}0.057{\mu}m^3$ respectively. In normal cat endothelial cells, the volume densities of cytoplasm, cytoplasmic vesicles, tubular systems (including endoplasmic reticulum and Golgi apparatus) and mitochondria were $0.43{\pm}0.023,\;0.28{\pm}0.007,\;0.22{\pm}0.021,\;0.03{\pm}0.014$ respectively. The mean thickness of endothelial cells was $230{\pm}45.2{\mu}m$. The numerical density and average volume of cytoplasmic vesicles were $508{\pm}55.0/{\mu}m^3,\;578{\pm}104.8nm^3$ respectively. In cat myocytes which received mild ischemic injury, the volume densities of organelles were not changed significantly in ischemic and reperfusion states. In reperfusion group myocytes, the numerical density of mitochondria was decreased significantly and the average volume was increased significantly. In endothelial cells, the volume density of tubular system in ischemic group and the average volume of cytoplasmic vesicles in reperfusion group were increased significantly. In rat myocytes which received severe ischemic injury, the volume density and average volume of mitochondria were increased significantly, and the volume density of sarcoplasmic reticulum and numerical density of mitochondria were decreased significantly in both ischemic and reperfusion groups. In ischemic and reperfused endothelial cells, the volume density and numerical density of cytoplasmic vesicles, the volume density of cytoplasm were decreased significantly. The volume densities of tubular system were increased significantly in both ischemic and reperfused groups. The volume density of mitochondria in ischemic group and the average volume of cytoplasmic vesicles in reperfusion group showed significant increase. The authors, based on the above observations, conclude that the mitochondria of myocytes and the cytoplasmic vesicles of endothelia are the first group of targets in ischemic and reperfusion injury and in this respect, the degree of ischemic insult is not significant. The role of myocyte mitochondria in reperfusion injury may be insignificant, but endothelial cells may contribute actively to reperfusion injury.

• Applied Biological Chemistry
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• v.32 no.3
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• pp.278-285
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• 1989

Effects of cooking and drying methods on the taste component and microstructure of shrimp, Metapenaeus joyneri, were investigated. The nucleotides and their related compounds of fresh shirmp such as ATP, ADP, AMP, IMP, inosine and hypoxanthine were detected. AMP was detected as a trace amount in fresh shrimp, however, it increased up to $23.5{\sim}45.7{\mu}$ moles with cooking and drying due to the decomposition of ATP and ADP to AMP during cooking and drying. The major component of the free amino acids of fresh shrimp was arginine followed by glycine, lysine, proline and alanine. These free amino acids contents were 70% of the total free amino acids. One hundred grams of fresh shrimp contained 1,198mg (dry basis) of the total free amino acids. However, for hot air and freeze dried cooked shrimps it was decreased down to 342mg (dry basis) and 503mg (dry basis), respectively. It might be due to the dissolution of soluble amino acids during cooking. Hot air-and freeze-dried fresh shrimps was higher in hardness and brittleness but lower in cohesiveness and gumminess than hot air-and freeze-dried ones with boiling and microwave heating. Freeze dried shrimp had softer myofibril texture than hot air dried one. At the same time, more dense and multiporous structure in the tissue could be obtained from the hot air and freeze drying, respectively, after microwave heating of shrimps.

• Food Science of Animal Resources
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• v.41 no.4
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• pp.650-663
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• 2021

The objective of this study was to examine the relationship between meat quality attributes and the changes of sarcoplasmic protein acetylation and myofibrillar protein acetylation in lamb longissimus thoracis et lumborum muscles at different postmortem phases. Protein acetylation, color, pH, shear force, myofibril fragmentation index and cooking loss were measured. The total level of acetylated sarcoplasmic proteins showed a negative relation with pH, a positive relation with a^*, b^* and cooking loss at the pre-rigor phase. Sarcoplasmic proteins acetylation affected postmortem pH by regulating glycolysis, which in turn affects color and cooking loss. The total level of acetylated myofibrillar proteins showed a positive relation with shear force at the pre-rigor phase. Myofibrillar proteins acetylation affected meat tenderness by regulating muscle contraction. This study indicated that acetylation played a regulatory role of meat color, water-holding capacity, and tenderization process at early postmortem.

• The Korean Journal of Pharmacology
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• v.30 no.3
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• pp.321-330
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• 1994

The protective effect of 'ischemic preconditioning (PC)' on ischemia-reperfusion injury of heart has been reported in various animal species, but without known mechanisms in detail. In an attempt to investigate the cardioprotective mechanism of PC, we examined the effects of PC on the myocardial oxidative injuries and the oxygen free radical production in the ischemia-reperfusion model of isolated Langendorff preparations of rat hearts. PC was performed with three episodes of 5 min ischemia and 5 min reperfusion before the induction of prolonged ischemia (30 min)-reperfusion(20 min). PC prevented the depression of cardiac function (left ventricular pressure x heart rate) observed in the ischemic-reperfused heart, and reduced the release of lactate dehydrogenase during the reperfusion period. On electron microscopic pictures, myocardial ultrastructures were relatively well preserved in PC hearts as compared with non-PC ischemic-reperfused hearts. In PC hearts, lipid peroxidation of myocardial tissue as estimated from malondialdehyde production was markedly reduced. PC did not affect the activity of xanthine oxidase which is a major source of oxygen radicals in the ischemic rat hearts, but the myocardial content of hypoxanthine (a substrate for xanthine oxidase) was much lower in PC hearts. It is suggested from these results that PC brings about significant myocardial protection in ischemic-reperfused heart and this effect may be related to the suppression of oxygen free radical reactions.

• Journal of Life Science
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• v.28 no.4
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• pp.435-443
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• 2018

AMP-activated protein kinase (AMPK) functions as a metabolic master through regulating and restoring cellular energy balance. In skeletal muscle, AMPK increases myofibril protein degradation through the expression of muscle-specific ubiquitin ligases. Mori Folium, the leaf of Morus alba, is a traditional medicinal herb with various pharmacological functions; however, the effects associated with muscle atrophy have not been fully identified. In this study, we confirmed the effects of AMPK activation by examining the effects of 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR), an activator of AMPK, on the induction of atrophy and expression of atrophy-related genes in C2C12 myotubes. We also investigated the effects of the ethanol extract of Mori Folium (EEMF) on the recovery of AICAR-induced muscle atrophy in C2C12 myotubes. It was found that exposure to AICAR resulted in the stimulation of Forkhead box O3a (FOXO3a); an up-regulation of muscle-specific ubiquitin ligases such as Muscle Atrophy F-box (MAFbx)/atrogin-1 and muscle RING finger-1 (MuRF1), and a down-regulation of muscle-specific transcription factors, such as MyoD and myogenin; with the activation of AMPK. In addition, AICAR without cytotoxicity indicated a decrease in diameter of C2C12 myotubes. However, treatment with EEMF significantly suppressed AICAR-induced muscle atrophy of C2C12 myotubes in a dose-dependent manner as confirmed by a decrease in myotube diameter, which is associated with a reversed stimulation of FOXO3a by the inhibition of AMPK activation. These results indicate that the activation of AMPK by AICAR induces muscle atrophy, and EEMF has preeminent effects on the inhibition of AICAR-induced muscle atrophy through the AMPK signaling pathway.

• Korean Journal of Food Science and Technology
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• v.7 no.4
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• pp.229-237
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• 1975

An attempt was made to utilize the enzyme produced by Asp. oryzae as meat tenderizer. The production, purification, and various properties of proteinase produced by Asp. oryzae were investigated. Results obtained are as follow; 1. A strain which had the highest proteolytic activity was selected among 9 Aspergillus species. 2. Culture medium consisted of wheat bran 10g, 2% glucose, 0.03% urea and 0.1% $MgSO_4$ (pH 6.5). Mold was incubated at $30^{\circ}C$ for 3 days. 3. Enzyme extract from culture medium were fractionated with ammonium sulfate and purified by Sephadex G-75 column chromatography. 4. When pH of reaction mixture was controlled, maximal activity of proteinase by Asp. oryzae was obtained at pH 3, pH 6.6, $8.4{\sim}8.5$ and pH 10.0 to 10.5. Those results were interpreted to show that enzyme consists of acid proteinase, neutral proteinase and alkaline proteinase. Enzyme was stable at pH 6 to 10. 5. Opt. temperature for proteinase activity was $50^{\circ}C$, but enzyme was stable up to $40^{\circ}C$. 6. The proteinase was inhibited by $Ag^+$. It was also inhibited by EDTA. 7. When myofibrillar proteins were treated by proteinase from Asp. oryzae, ATPase activities of myofibrillar proteins changed remarkably. Accordingly, it was concluded that proteinase produced by Asp. oryzae were able to be used as meat tenderizer.