• Archives of Pharmacal Research
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• v.19 no.6
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• pp.502-506
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• 1996

Protein X is one of the subunits of pyruvate dehydrogenase complex. The biological role of this protein has not been fully elucidated, mainly because of the difficulty in its dissociation from the tightly bound dihydrolipoamide acetyltransferase-protein X subcomplex. We have found that the detachment of protein X from acetyltransferase subunit can be easily accomplished by the cycles of freezing and thawing proces. Several lines of evidence including sodium dodecyl sulfate-polyacrylamide gel electrophoresis, N-terminal amino acid sequence analysis and acetylation with $[2^{14}C]$ pyruvate confirmed that the purified protein is protein X. The purified intact form of protein X was acetylated by $[2^{14}C]$ pyruvate in the presence of py-ruvate dehydrogenase subunit.The acetylation efficiency of this protein was lower than that of acetyltransferase and was not affected by the presence of acetyltransferase.

• Asian-Australasian Journal of Animal Sciences
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• v.30 no.6
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• pp.857-864
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• 2017

Objective: The purpose of this study was to investigate the influence of AMP-activated protein kinase (AMPK) activation on protein acetylation and glycolysis in postmortem muscle to better understand the mechanism by which AMPK regulates postmortem glycolysis and meat quality. Methods: A total of 32 mice were randomly assigned to four groups and intraperitoneally injected with 5-Aminoimidazole-4-carboxamide1-${\beta}$-D-ribofuranoside (AICAR, a specific activator of AMPK), AICAR and histone acetyltransferase inhibitor II, or AICAR, Trichostatin A (TSA, an inhibitor of histone deacetylase I and II) and Nicotinamide (NAM, an inhibitor of the Sirt family deacetylases). After mice were euthanized, the Longissimus dorsi muscle was collected at 0 h, 45 min, and 24 h postmortem. AMPK activity, protein acetylation and glycolysis in postmortem muscle were measured. Results: Activation of AMPK by AICAR significantly increased glycolysis in postmortem muscle. At the same time, it increased the total acetylated proteins in muscle 45 min postmortem. Inhibition of protein acetylation by histone acetyltransferase inhibitors reduced AMPK activation induced increase in the total acetylated proteins and glycolytic rate in muscle early postmortem, while histone deacetylase inhibitors further promoted protein acetylation and glycolysis. Several bands of proteins were detected to be differentially acetylated in muscle with different glycolytic rates. Conclusion: Protein acetylation plays an important regulatory role in postmortem glycolysis. As AMPK mediates the effects of pre-slaughter stress on postmortem glycolysis, protein acetylation is likely a mechanism by which antemortem stress influenced postmortem metabolism and meat quality though the exact mechanism is to be elucidated.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.3
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• pp.219-223
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• 1990

Myofibrillar protein from Alaska pollack was modified with acetic anhydride at pH 7.5 and $25^{\circ}C$ and changes in functional properties as affected by the degree of modification were determined. Acetylation of myofibrillar protein resulted in protein with unique functional properties dependent upon the degree of acetylation. By selecting appropriate degree of modification it was possible to control protein solubility heat coagulability calcium precipitability foaming and emulsion capa-city.

• Journal of Environmental Health Sciences
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• v.30 no.4
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• pp.308-313
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• 2004

Native and acetylated soybean protein with acetylation percentage of $25\%$ were incubated with glucose to induce Maillard reaction. Acetylation of ${\varepsilon}$-amino group of lysine residues changed the conformation of soybean protein. The direct uv spectrum of native and acetylated soybean protein showed conformational changes with accessibility of tyrosine and tryptophan residues increased. Acetylation suppressed Maillard reaction between soybean protein and glucose. Acetylated soybean protein showed improved water sorption, fat binding, foam formation, and emulsion activity of the protein, but depressed brown pigment development and trypsin digestion. Thus aceylation prevented deterioration of certain functional characteristics that occurred during storage, besides causing functional characteristics to be improved on its own.

• Asian Pacific Journal of Cancer Prevention
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• v.14 no.4
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• pp.2255-2258
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• 2013

The activity of Rb proteins is controlled by post-translational modifications, especially through phosphorylation. Acetylation of Rb2/p130 was reported recently in NIH3T3 cells but its physiological relevance in cell cycle control and tumorigenesis is still unknown. Efforts are underway to investigate possible interplay between Rb2/p130 phosphorylation and acetylation. Here we hypothesized that Rb2/p130 acetylation, like p53 acetylation, may play a role in development of the tumor phenotype. The proposed hypothesis regarding acetylation of Rb2/p130 in tumor VS normal cells was found to be true in our case study of 36 tumor samples. Statistical analysis of results suggest strong correlation among Rb2/p130 acetylation and cancer phenotype.

• Biomolecules & Therapeutics
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• v.15 no.2
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• pp.78-82
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• 2007

The proto-oncogene protein DEK is a nuclear binding phosphoprotein that has been associated with various human diseases including leukemia. Histone acetylation is an important post-translational modification which plays important role in transcriptional regulation. Auto-acetylation of histone acetyltransferase PCAF results in increment of its HAT activity and facilitation of its nuclear localization. In this study, we report that DEK inhibits PCAF auto-acetylation through direct interaction. The C-terminal acidic domains of DEK are responsible for the interaction with PCAF. Using confocal microscopy, we have shown that nuclear localization of PCAF is severely inhibited by DEK. Taken together, our results suggest that DEK may be involved in various cellular signal transduction pathways accommodated by PCAF through the regulation of PCAF auto-acetylation.

• Korean Journal of Food Science and Technology
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• v.20 no.5
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• pp.625-630
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• 1988

Phosphorylation of soy protein by sodium trimetaphosphate and acetylation of soy protein by acetic anhydride were performed. Then, the functional properties of modified soy proteins were compared with that of unmodified soy protein. Isolated soy protein prepared from defatted soybean flake had protein content of 92.7% as moisture-free basis. The phosphorylated soy protein showed higher solubility, foaming properties, and water holding capacity than unmodified soy protein. Acetylation of soy protein increased emulsification activity and foaming properties greatly, whereas decreased the solubility at pH 8.0. Isoelectric pHs of phosphorylated and acetylated soy protein were shifted to acidic regions(pH 3.0 and pH 4.0) from pH 5.0, which was the isoelectric pH of unmodified soy protein. Soy protein seems to be aggregated during phosphorylation and acetylation procedure, judging form Sepharose CL-4B gel filtration profiles. The modified soy proteins showed increased mobilities to anode direction in disc-gel electrophoresis.

• Molecules and Cells
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• v.39 no.3
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• pp.169-178
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• 2016

Although $N{\alpha}$-terminal acetylation (Nt-acetylation) is a pervasive protein modification in eukaryotes, its general functions in a majority of proteins are poorly understood. In 2010, it was discovered that Nt-acetylation creates a specific protein degradation signal that is targeted by a new class of the N-end rule proteolytic system, called the Ac/N-end rule pathway. Here, we review recent advances in our understanding of the mechanism and biological functions of the Ac/N-end rule pathway, and its crosstalk with the Arg/N-end rule pathway (the classical N-end rule pathway).

• Journal of Pharmaceutical Investigation
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• v.36 no.2
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• pp.115-121
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• 2006

The aim of this study was to develop new protein/peptide depot system instead of poly(DL-lactic acid-coglycolic acid) (PLGA) microspheres. Pullulan was chemically modified by the addition of acetic anhydride (pullulan acetate; PA) and then investigated as new depot system for protein/peptide delivery. PA microspheres (PAM) with lysozyme as a model protein were prepared by w/o/w double emulsion method. The microspheres had a mean size of 10-50 mm with a spherical shape. The size distributions reduced with increasing the degree of acetylation. The loading efficiency of lysozyme was also increased. Lysozyme aggregation behavior in the microsphere was monitored to estimate the change of protein stability during preparation step. The ratios of protein aggregation in PAMs are lower than that of PLGA microsphere, in particular, PA 5 showed lowest as about 16%. The result indicated that the increase of acetylation suppressed the aggregation of protein. The release profiles of lysozyme from PAMs were significantly different. High acetylation effectively improved lysozyme release kinetics by reducing initial burst release and extending continuous release over a period of time. To check the effect of preservation for structural stability of lysozyme, the activity of lysozyme released from PA 5 was also observed. The activity of lysozyme was maintained almost 100% for 25 day. Therefore, PAM may become to a useful carrier for delivery of protein/peptide drugs, if it will be supported by biocompatibility and biodegradability results.

• 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.