• BMB Reports
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• v.38 no.1
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• pp.58-64
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• 2005

Myo-inositol monophosphate phosphatase (IMPP) is a key enzyme in the phosphoinositide cell-signaling system. This study found that incubating the IMPP from a porcine brain with pyridoxal-5'-phosphate (PLP) resulted in a time-dependent enzymatic inactivation. Spectral evidence showed that the inactivation proceeds via the formation of a Schiff's base with the amino groups of the enzyme. After the sodium borohydride reduction of the inactivated enzyme, it was observed that 1.8 mol phosphopyridoxyl residues per mole of the enzyme dimer were incorporated. The substrate, myo-inositol-1-phosphate, protected the enzyme against inactivation by PLP. After tryptic digestion of the enzyme modified with PLP, a radioactive peptide absorbing at 210 nm was isolated by reverse-phase HPLC. Amino acid sequencing of the peptide identified a portion of the PLP-binding site as being the region containing the sequence L-Q-V-S-Q-Q-E-D-I-T-X, where X indicates that phenylthiohydantoin amino acid could not be assigned. However, the result of amino acid composition of the peptide indicated that the missing residue could be designated as a phosphopyridoxyl lysine. This suggests that the catalytic function of IMPP is modulated by the binding of PLP to a specific lysyl residue at or near its substrate-binding site of the protein.

• Journal of the Korean Society of Food Science and Nutrition
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• v.13 no.3
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• pp.231-237
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• 1984

Changes in available lysine and water soluble proteins were checked to obtain the desirable condition of processing for boiled Neverita didyma under the various autoclaving temperatures and times. It was also carried out to assess the affect of heat treatments upon the solubility of coagulable substances in boiled products. In order to evaluate the nutritional quality of processed Neverita didyma under the highest available lysine retention and without bacteria, it was studied the value of pepsin-pancreatin digest residue index in comparison with unprocessed (raw) material. The crude protein content of raw material was higher than that of the other mollusks, while the content of crude fat was showing lower value. It was noticed that the higher contents of coagulable substances and water soluble proteins in processed Neverita didyma were obtained under the conditions, retort temperature at $120^{\circ}C$ above, and 40-60 min. sterilization. After the pannel test, the coagulable substances were not found below the level of $0.40{\pm}0.03$ gram nitrogen/ml of juice. The remarkable retention of available lysine (FDNB-reactive lysine) was resulted in the conditions of autoclaving at $115^{\circ}C$ for 40 minutes in boiled Neverita didyma products, and that processing condition was coincide with the condition of commercial sterilization for boiled top shell. It was revealed that the boiled meat of Neverita didyma showed the higher PPDRI(65.85) than that of raw material (63.16).

• BMB Reports
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• v.53 no.11
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• pp.576-581
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• 2020

Dimethylation of the histone H3 protein at lysine residue 9 (H3K9) is mediated by euchromatin histone methyltransferase II (EHMT2) and results in transcriptional repression of target genes. Recently, chemical inhibition of EHMT2 was shown to induce various physiological outcomes, including endoplasmic reticulum stress-associated genes transcription in cancer cells. To identify genes that are transcriptionally repressed by EHMT2 during apoptosis, and cell stress responses, we screened genes that are upregulated by BIX-01294, a chemical inhibitor of EHMT2. RNA sequencing analyses revealed 77 genes that were upregulated by BIX-01294 in all four hepatic cell carcinoma (HCC) cell lines. These included genes that have been implicated in apoptosis, the unfolded protein response (UPR), and others. Among these genes, the one encoding the stress-response protein Ras-related GTPase C (RRAGC) was upregulated in all BIX-01294-treated HCC cell lines. We confirmed the regulatory roles of EHMT2 in RRAGC expression in HCC cell lines using proteomic analyses, chromatin immune precipitation (ChIP) assay, and small guide RNA-mediated loss-of-function experiments. Upregulation of RRAGC was limited by the reactive oxygen species (ROS) scavenger N-acetyl cysteine (NAC), suggesting that ROS are involved in EHMT2-mediated transcriptional regulation of stress-response genes in HCC cells. Finally, combined treatment of cells with BIX-01294 and 5-Aza-cytidine induced greater upregulation of RRAGC protein expression. These findings suggest that EHMT2 suppresses expression of the RRAGC gene in a ROS-dependent manner and imply that EHMT2 is a key regulator of stress-responsive gene expression in liver cancer cells.

• The Korean Journal of Physiology and Pharmacology
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• v.3 no.3
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• pp.251-261
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• 1999

The effects of carnosine and related compounds (CRCs) including anserine, homocarnosine, histidine, and ${\beta}-alanine$ on monosaccharide autoxidation and $H_2O_2$ formation were investigated. The incubation of CRCs with D-glucose, D-glucosamine, and D, L-glyceraldehyde at $37^{\circ}C$ increased the absorption maxima at 285 nm, 273 nm, and $290{\sim}330$ nm, respectively. D, L-glyceraldehyde was the most reactive sugar with CRCs. The presence of copper strongly stimulated the reaction of carnosine and anserine with D-glucose or D-glucosamine. Carnosine and anserine stimulated $H_2O_2$ formation from D-glucose autoxidation in a dose-dependent manner in the presence of 10 ${\mu}M$ Cu (II). The presence of human serum albumin (HSA) decreased their effect on $H_2O_2$ formation. Carnosine and anserine has a biphasic effect on ${\alpha}-ketoaldehyde$ formation from glucose autoxidation. CRCs inhibited glycation of HSA as determined by hydroxymethyl furfural, lysine residue with free ${\varepsilon}-amino$ group, and fructosamine assay. These results suggest that CRCs may be protective against diabetic complications by reacting with sugars and protecting glycation of protein.