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TPA로 야기된 HL-60 세포의 기질부착 저해작용을 이용한 Protein Kinase C 저해 생약의 탐색
김선희,안종석,김삼용,유관희,안병준 충남대학교 약학대학 의약품개발연구소 1993 藥學論文集 Vol.9 No.-
Thirty-five kinds of herbal drugs, believed to be active for treatment of tumors, were selected as the experimental materials for observing their effects on TPA-induced adherence of HL-60 cell and activity of protein kinase C. They were extracted with ethyl ether(E) and ethyl acetate(EA), methanol(M) in sequence. Among the extracts, Sophorae Flos(EA), Paeoniae Radix(EA), Equisetum hiemale(EA), Phellodendri Cortex(E, EA), Mori Cortex radicis(EA), Ferula assafoetida(E, EA), Sophora subprostrata(EA, M) and Cnidium monnieri(E) inhibited the TPA-in-duced adherence of HL-60 cell more than 50% and Sophorae Flos(E, EA, M), Paeoniae Radix(E, EA, M), Eguisetum hiemale(E), Phellodenri Cortex(E,H), Mori Cortex radicis(M), Ferula assafoetida(M), Sophora subprostrata(EA, M), Cnidium monnieri(M) and Artemisia argyi(M) showed inhibiting effects on the activity of protein kinase C more than 50%. The extracts showing good inhibiting effects on the adherence and enzyme activity were Sophorae Flos(EA), Paeoniae Radix(EA), Phellodendri Cortex(E), Sophora subsprostrate(EA) and Equisetum hiemale(EA).
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실험적 뇌지주막하출혈 토끼에서의 Malonate 농도 측정
김재중,하영수,백승렬,장정순,김유삼 대한신경외과학회 1995 Journal of Korean neurosurgical society Vol.24 No.10
Malonate is regarded as a reversible competitive inhibitor of succinate dehydrogenase and malate transport in the Krebs cycle and showed neurotoxicity by persistent NMDA receptor activation due to inhibition of ATP production and glutamate utilization. However, little was known about its biological effects and the range of normal concentration of malonate in central nervous system. In order to understand the relationship between malonate and vasospsasm, malonate concentrations in rabbit model of experimental subarachnoid hemorrhage were measured at 0, 4th, and 7th day following SAH in serum, cerebrospinal fluid, and urine using malonyl-CoA synthetase. The results were as follows : 1) Malonate level is increased significantly in serum at the 4th day after subarachnoid hemorrhage that followed by vasospasm(p<0.01). 2) CSF malonate concentration tends to increase at post-SAH 7th day but statistically not significant. 3) The change of urine malonate concentration is not significant. These results suggest that early increase of serum malonate level is significant because clinically important vasospam begin from the fourth through the seven day after hemorrhage. The increased level of serum malonate at this time is due to impairment of cellular metabolism following delayed cerebral ischemia and may influence to development of vasospasm. In conclusion, the measurement of serum malonate concentration after subarachnoid hemorrhage is one of possible candidates for the early diagnosis of vasospasm.
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The Effect of ZD 1839 (Iressa) in the Treatment of RefractoryNon Small Cell Lung Cancer
Yong Tai Kim,Chul Kim,Joo Hyuk Sohn,So Young Park,Soo Young Park,Nae Choon Yu,Young Sam Kim,Se Kyu Kim,Joon Chang,Kil Dong Kim,Kyung Young Chung,Joo Hang Kim 대한암학회 2003 Cancer Research and Treatment Vol.35 No.6
Purpose: The aim of this study was to evaluate theefficacy and the safety of ZD 1839 (Iressa) as a 3rd or4th line chemotherapy regimen in NSCLC patients whoare refractory to a previous chemotherapy regimen.Materials and Methods: Twenty-five patients who wererefractory to previous chemotherapy were selected forthis study. The eligible patients had an ECOG performancestatus of 0 to 2, and an appropriate end organfunction. ZD 1839 (Iressa) 250 mg/d was orally administereduntil the patients experienced disease progressionor unacceptable toxicity.Results: Twenty-five patients were analyzed. The medianage of the patients was 57 years. The response ratewas 12.0% with partial responses in 3 patients. Fourteenpatients (56%) remained in the stable disease state and8 patients progressed. The median overall survival was9.0 months (95% CI 6.7~11.2). The median progressionfree survival was 3 months (95% CI 2.2~3.8). Hematologicaltoxicities of grade 3 or 4 neutropenia, anemia andthrombocytopenia were absent. Non-hematological toxicitieswere grade 2 or 3 skin rashes in 10 (40.0%) patientsand 1 (4.0%) patient and grade 3 nausea in 3 (12.0%) patients.No patient failed to continue chemotherapy due toany drug-related adverse events.Conclusion: The results suggest that ZD 1839 (Iressa)monotherapy is effective and tolerable as a 3rd or 4th linesalvage treatment for NSCLC patients refractory to previouschemotherapy regimens. (Cancer ResTreat. 2003;35:502-506)
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Kim Seong-Jin,Kim Young-Sam,Kim Sang-Eon,Jung Hyun-Kyoung,Park Jeeeun,Yu Min-Ju,Kim Kyoung-Ho 한국미생물학회 2022 The journal of microbiology Vol.60 No.11
A novel bacterium designated RR4-40T was isolated from a biofilter of seawater recirculating aquaculture system in Busan, South Korea. Cells are strictly aerobic, Gram-negative, irregular short rod, non-motile, and oxidase- and catalase-negative. Growth was observed at 15–30°C, 0.5–6% NaCl (w/v), and pH 5.0–9.5. The strain grew optimally at 28°C, 3% salinity (w/v), and pH 8.5. The phylogenetic analysis based on 16S rRNA gene sequences showed that strain RR4-40T was most closely related to Marinirhabdus gelatinilytica NH83T (94.16% of 16S rRNA gene similarity) and formed a cluster with genera within the family Flavobacteriaceae. The values of the average nucleotide identity (ANI), digital DNA-DNA hybridization (dDDH), and average amino acid identity (AAI) between genomes of strain RR4-40T and M. gelatinilytica NH83T were 72.91, 18.2, and 76.84%, respectively, and the values against the strains in the other genera were lower than those. The major fatty acids were iso-C15:0 (31.34%), iso-C17:0 3-OH (13.65%), iso-C16:0 3-OH (10.61%), and iso-C15:1 G (10.38%). The polar lipids comprised phosphatidylglycerol, diphosphatidylglycerol, aminophospholipid, aminolipid, glycolipid, and sphingolipid. The major respiratory quinone was menaquinone-6 (MK-6) and the DNA G + C content of strain RR4-40T was 37.4 mol%. According to the polyphasic analysis, strain RR4-40T is considered to represent a novel genus within the family Flavobacteriaceae, for which the name Rasiella rasia gen. nov, sp. nov. is proposed. The type strain is RR4-40T (= KCTC 52650T = MCCC 1K04210T).
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Kim, Yu Sam,Kim, Dae Jin,Eun, Suk Ho 생화학분자생물학회 1970 BMB Reports Vol.34 No.3
dTDP-rhamnose is synthesized from dTTP and glucose-1-phosphate by four enzymatic steps in the gram-negative bacteria. By using a homologous PCR product, a gene cluster encoding four genes (rfbA, rfbB, rfbC, rfbD) involved in L-rhamnose biosynthesis by Acinetobacter calcoaceticus was isolated and sequenced. The four genes were clustered on the biosynthefic operon in the order of rfbB, D, A, C. A gene, rfbA, encoding glucose-l-phosphate thymidylyltransferase (RfbA), was cloned from A. cakoaceticus pathogenic and encapsulated in the gramnegative bacterium. This enzyme catalyzes the formation of dTDP-D-glucose From α-D-glucose-1-phosphate and dTTP RJbA was amp66ed by PCR and inserted into the T_7 expression system. The activity of RfbA was determined by the capillary electrophoresis. The K_m values for dTTP and α-D-glucose-1-phosphate were calculated to be 1.27 mM and 0.80 mM, respectively by using the Line-Weaver Burk plot. R,fbA is inactivated by diethylpyrocarbonate.
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Kim, Yu Sam,Byun, Hye Sin 생화학분자생물학회 2000 BMB Reports Vol.30 No.4
Malonate decarboxylase from Acinetobacter calcoaceticus is shown to have malonyl-CoA: acetate CoA transferase. acetyl-CoA: malonate CoA transferase, and malonyl-CoA decarboxylase activity. These enzyme activities were elucidated by isotope exchange reactions. The enzyme modified by N-ethylmaleimide completely lost its malonate decarboxylase activity, whereas it still kept CoA transferases and malonyl-CoA decarboxylase activities. The existence of CoA transferases and malonyl-CoA decarboxylase activity is clear, but their physiological significance is obscure. The catalytic reactions for two CoA transfers and malonyl-CoA decarboxylation proceed via a cyclic mechanism, which is through two covalent intermediates, enzyme-S-malonyl and enzyme-S-acetyl, proposed for malonate decarboxylation of the enzyme.
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Kim, Yu Sam,Lee, Weon Tae,Bang, Eun Jung,An, Jae Hyung,Jung, Jin Won 생화학분자생물학회 2000 BMB Reports Vol.32 No.3
In order to understand the initial interaction of the substrates malonate, ATP, and CoA with malonyl-CoA synthetase, the catalytic product malonyl-CoA was characterized by NMR spectroscopy and molecular modeling. To assign proton and carbon chemical shifts, two-dimensional 1H-IH DQF-COSY and ¹H-^(13)C HMBC experiments were used. The structure of malonyl-CoA in the solution phase was determined based on distance constraints from NOESY and ROESY spectra. The structures were well-converged around the pantetheine region with the pairwise RMSD value of 0.08 nm. The solution structure exhibited a compact folded conformation with intramolecular hydrogen bonds among its carbonyl and hydroxyl groups. These findings will help us to understand the initial interaction of malonate and CoA with malonyl-CoA synthetase.
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Properties of Malonyl-CoA Decarboxylase from Rhizobium trifolii
Kim, Yu Sam,Lee, Dai Woon,An, Jae Hyung,Song, Jong Hee,Lee, Gha Young 생화학분자생물학회 2000 BMB Reports Vol.32 No.4
A novel gene for malonyl-CoA decarboxylase was discovered in the mat operon, which encodes a set of genes involved in the malonate metabolism of Rhizobium trifolii (An and Kim, 1998). The subunit mass determined by SDS-PAGE was 53 kDa, which correspond to the deduced mass from the sequence data. The molecular mass of the native enzyme determined by field flow fractionation was 208 kDa, indicating that R. trifolii malonyl-CoA decarboxylase is homotetrameric. R. trifolii malonyl-CoA decarboxylase converted malonyl-CoA to acetyl-CoA with a specific activity of 100 unit/㎎ protein. Methylmalonyl-CoA was decarboxylated with a specific activity of 0.1 unit/ ㎎ protein. p-Chloromercuribenzoate inhibited this enzyme activity, suggesting that thiol groups) is(are) essential for this enzyme catalysis. Database analysis showed that malonyl-CoA decarboxylase from R. trifolii shared 32.7 % and 28.1 % identity in amino acid sequence with those from goose and human, respectively, and it would be located in the cytoplasm. However, there is no sequence homology between this enzyme and that from Saccharopolyspora erythreus, suggesting that malonyl-CoA decarboxylases from human, goose, and R. trifolii are in the same class, whereas that from S. erythreus is in a different class or even a different enzyme, methylmalonyl-CoA decarboxylase. According to the homology analysis, Cys-214 among three cysteine residues in the enzyme was found in the homologous region, suggesting that the cysteine was located at or near the active site and plays a critical role in catalysis.
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Malonate Metabolism : Biochemistry, Molecular Biology, Physiology, and Industrial Application
Kim, Yu Sam 한국생화학분자생물학회 2002 BMB Reports Vol.35 No.5
Malonate is a three-carbon dicarboxylic acid. It is well known as a competitive inhibitor of succinate dehydrogenase. It occurs naturally in biological systems, such as legumes and developing rat brains, which indicates that it may play an important role in symbiotic nitrogen metabolism and brain development. Recently, enzymes that are related to malonate metabolism were discovered and characterized. The genes that encode the enzymes were isolated, and the regulation of their expression was also studied. The mutant bacteria, in which the malonatemetabolizing gene was deleted, lost its primary function, symbiosis, between Rhizobium leguminosarium by trifolii and clover. This suggests that malonate metabolism is essential in symbiotic nitrogen metabolism, at least in clover nodules. In addition to these, the genes matB and matC have been successfully used for generation of the industrial strain of Streptomyces for the production of antibiotics.
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