Lee SC

References (10)

Title : The lipoprotein-associated phospholipase A2 inhibitor Darapladib sensitises cancer cells to ferroptosis by remodelling lipid metabolism - Oh_2023_Nat.Commun_14_5728
Author(s) : Oh M , Jang SY , Lee JY , Kim JW , Jung Y , Kim J , Seo J , Han TS , Jang E , Son HY , Kim D , Kim MW , Park JS , Song KH , Oh KJ , Kim WK , Bae KH , Huh YM , Kim SH , Han BS , Lee SC , Hwang GS , Lee EW
Ref : Nat Commun , 14 :5728 , 2023
Abstract : Arachidonic and adrenic acids in the membrane play key roles in ferroptosis. Here, we reveal that lipoprotein-associated phospholipase A2 (Lp-PLA2) controls intracellular phospholipid metabolism and contributes to ferroptosis resistance. A metabolic drug screen reveals that darapladib, an inhibitor of Lp-PLA2, synergistically induces ferroptosis in the presence of GPX4 inhibitors. We show that darapladib is able to enhance ferroptosis under lipoprotein-deficient or serum-free conditions. Furthermore, we find that Lp-PLA2 is located in the membrane and cytoplasm and suppresses ferroptosis, suggesting a critical role for intracellular Lp-PLA2. Lipidomic analyses show that darapladib treatment or deletion of PLA2G7, which encodes Lp-PLA2, generally enriches phosphatidylethanolamine species and reduces lysophosphatidylethanolamine species. Moreover, combination treatment of darapladib with the GPX4 inhibitor PACMA31 efficiently inhibits tumour growth in a xenograft model. Our study suggests that inhibition of Lp-PLA2 is a potential therapeutic strategy to enhance ferroptosis in cancer treatment.
ESTHER : Oh_2023_Nat.Commun_14_5728
PubMedSearch : Oh_2023_Nat.Commun_14_5728
PubMedID: 37714840

Title : Antioxidant, ACE inhibitory, and acetylcholinesterase inhibitory activities of subcritical water extract of blue mussel - Han_2018_Food.Sci.Biotechnol_27_847
Author(s) : Han JK , Sung SC , Jo MJ , Lee SC
Ref : Food Sci Biotechnol , 27 :847 , 2018
Abstract : Subcritical water (SCW) extract of blue mussel was prepared at 100, 200, and 300 degrees C for 10, 30, and 60 min, respectively, and its effect on the activity of 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, angiotensin-converting enzyme (ACE), and acetylcholinesterase (AChE) was evaluated. We found that DPPH radical scavenging, ACE inhibitory, and AChE inhibitory activities significantly increased with increasing extraction temperature and duration. For example, AChE inhibitory activity of the extract at 300 degrees C for 60 min increased to 63.1 +/- 0.3%, while that at 100 degrees C for 10 min was 5.6 +/- 0.3%. The results suggested that SCW extraction is attractive processing methods for obtaining high valued extract from blue mussel.
ESTHER : Han_2018_Food.Sci.Biotechnol_27_847
PubMedSearch : Han_2018_Food.Sci.Biotechnol_27_847
PubMedID: 30263810

Title : New reference genome sequences of hot pepper reveal the massive evolution of plant disease-resistance genes by retroduplication - Kim_2017_Genome.Biol_18_210
Author(s) : Kim S , Park J , Yeom SI , Kim YM , Seo E , Kim KT , Kim MS , Lee JM , Cheong K , Shin HS , Kim SB , Han K , Lee J , Park M , Lee HA , Lee HY , Lee Y , Oh S , Lee JH , Choi E , Lee SE , Jeon J , Kim H , Choi G , Song H , Lee SC , Kwon JK , Koo N , Hong Y , Kim RW , Kang WH , Huh JH , Kang BC , Yang TJ , Lee YH , Bennetzen JL , Choi D
Ref : Genome Biol , 18 :210 , 2017
Abstract : BACKGROUND: Transposable elements are major evolutionary forces which can cause new genome structure and species diversification. The role of transposable elements in the expansion of nucleotide-binding and leucine-rich-repeat proteins (NLRs), the major disease-resistance gene families, has been unexplored in plants. RESULTS: We report two high-quality de novo genomes (Capsicum baccatum and C. chinense) and an improved reference genome (C. annuum) for peppers. Dynamic genome rearrangements involving translocations among chromosomes 3, 5, and 9 were detected in comparison between C. baccatum and the two other peppers. The amplification of athila LTR-retrotransposons, members of the gypsy superfamily, led to genome expansion in C. baccatum. In-depth genome-wide comparison of genes and repeats unveiled that the copy numbers of NLRs were greatly increased by LTR-retrotransposon-mediated retroduplication. Moreover, retroduplicated NLRs are abundant across the angiosperms and, in most cases, are lineage-specific. CONCLUSIONS: Our study reveals that retroduplication has played key roles for the massive emergence of NLR genes including functional disease-resistance genes in pepper plants.
ESTHER : Kim_2017_Genome.Biol_18_210
PubMedSearch : Kim_2017_Genome.Biol_18_210
PubMedID: 29089032
Gene_locus related to this paper: capch-q75qh4 , capan-a0a1u8fuf5 , capan-a0a1u8gmz3 , capch-a0a2g3bqp0 , capba-a0a2g2vcw4 , capan-a0a1u8flz5 , capch-a0a2g3bau3 , capch-a0a2g3b6c0 , capan-a0a2g2y016 , capch-a0a2g3cje8 , capba-a0a2g2xr67 , capan-a0a1u8fpc9 , capan-a0a1u8fqs3 , capan-a0a1u8ft99 , capan-a0a2g2xtt0 , capan-a0a1u8eu02 , capan-a0a1u8hd13 , capan-a0a2g2y0b6

Title : Low Levels of NDRG1 in Nerve Tissue Are Predictive of Severe Paclitaxel-Induced Neuropathy - Sundar_2016_PLoS.One_11_e0164319
Author(s) : Sundar R , Jeyasekharan AD , Pang B , Soong RC , Kumarakulasinghe NB , Ow SG , Ho J , Lim JS , Tan DS , Wilder-Smith EP , Bandla A , Tan SS , Asuncion BR , Fazreen Z , Hoppe MM , Putti TC , Poh LM , Goh BC , Lee SC
Ref : PLoS ONE , 11 :e0164319 , 2016
Abstract : INTRODUCTION: Sensory peripheral neuropathy caused by paclitaxel is a common and dose limiting toxicity, for which there are currently no validated predictive biomarkers. We investigated the relationship between the Charcot-Marie-Tooth protein NDRG1 and paclitaxel-induced neuropathy. METHODS/MATERIALS: Archived mammary tissue specimen blocks of breast cancer patients who received weekly paclitaxel in a single centre were retrieved and NDRG1 immunohistochemistry was performed on normal nerve tissue found within the sample. The mean nerve NDRG1 score was defined by an algorithm based on intensity of staining and percentage of stained nerve bundles. NDRG1 scores were correlated with paclitaxel induced neuropathy.
RESULTS: 111 patients were studied. 17 of 111 (15%) developed severe paclitaxel-induced neuropathy. The mean nerve NDRG1 expression score was 5.4 in patients with severe neuropathy versus 7.7 in those without severe neuropathy (p = 0.0019). A Receiver operating characteristic (ROC) curve analysis of the mean nerve NDRG1 score revealed an area under the curve of 0.74 (p = 0.0013) for the identification of severe neuropathy, with a score of 7 being most discriminative. 13/54 (24%) subjects with an NDRG1 score < = 7 developed severe neuropathy, compared to only 4/57 (7%) in those with a score >7 (p = 0.017). CONCLUSION: Low NDRG1 expression in nerve tissue present within samples of surgical resection may identify subjects at risk for severe paclitaxel-induced neuropathy. Since nerve biopsies are not routinely feasible for patients undergoing chemotherapy for early breast cancer, this promising biomarker strategy is compatible with current clinical workflow.
ESTHER : Sundar_2016_PLoS.One_11_e0164319
PubMedSearch : Sundar_2016_PLoS.One_11_e0164319
PubMedID: 27716814
Gene_locus related to this paper: human-NDRG1

Title : Anti-Amnesic Effect of Fermented Ganoderma lucidum Water Extracts by Lactic Acid Bacteria on Scopolamine-Induced Memory Impairment in Rats - Choi_2015_Prev.Nutr.Food.Sci_20_126
Author(s) : Choi YJ , Yang HS , Jo JH , Lee SC , Park TY , Choi BS , Seo KS , Huh CK
Ref : Prev Nutr Food Sci , 20 :126 , 2015
Abstract : This study investigated the anti-amnesic effect of fermented Ganoderma lucidum water extracts (GW) on scopolamine-induced memory impairment in rats. GW were fermented by the lactic acid bacterium Bifidobacterium bifidum (FGWB), followed by Lactobacillus sakei LI033 (FGWBL). To induce amnesia, scopolamine (1 mg/kg) was intraperitoneally injected into rats 30 min before the behavioral tests. Step-through latencies of rats treated with primary fermented extracts (300 mg/kg, FGWB) and secondary fermented extracts (300 mg/kg, FGWBL) were significantly longer than those of rats treated with GW (300 mg/kg) in the retention trial of the multiple trial passive avoidance test. In the Morris water maze task, FGWBL significantly shortened escape latencies in training trials. Furthermore, swimming times within the target zone during the probe trial with FGWBL were significantly higher than the GW and FGWB treatments. In addition, acetylcholinesterase activities were lower in the brains of scopolamine-treated rats treated with FGWBL. These results suggest that FGWBL could be useful to enhance learning memory and cognitive function via cholinergic dysfunction.
ESTHER : Choi_2015_Prev.Nutr.Food.Sci_20_126
PubMedSearch : Choi_2015_Prev.Nutr.Food.Sci_20_126
PubMedID: 26176000

Title : Interaction between salt-inducible kinase 2 and protein phosphatase 2A regulates the activity of calcium\/calmodulin-dependent protein kinase I and protein phosphatase methylesterase-1 - Lee_2014_J.Biol.Chem_289_21108
Author(s) : Lee CW , Yang FC , Chang HY , Chou H , Tan BC , Lee SC
Ref : Journal of Biological Chemistry , 289 :21108 , 2014
Abstract : Salt-inducible kinase 2 (SIK2) is the only AMP-activated kinase (AMPK) family member known to interact with protein phosphatase 2 (PP2A). However, the functional aspects of this complex are largely unknown. Here we report that the SIK2-PP2A complex preserves both kinase and phosphatase activities. In this capacity,SIK2 attenuates the association of the PP2A repressor, the protein phosphatase methylesterase-1 (PME-1), thus preserving the methylation status of the PP2A catalytic subunit. Furthermore, the SIK2-PP2A holoenzyme complex dephosphorylates and inactivates Ca2(+)/calmodulin-dependent protein kinase I (CaMKI), an upstream kinase for phosphorylating PME-1/Ser(15). The functionally antagonistic SIK2-PP2A and CaMKI and PME-1 networks thus constitute a negative feedback loop that modulates the phosphatase activity of PP2A. Depletion of SIK2 led to disruption of the SIK2-PP2A complex, activation of CaMKI, and downstream effects, including phosphorylation of HDAC5/Ser(259), sequestration of HDAC5 in the cytoplasm, and activation of myocyte-specific enhancer factor 2C (MEF2C)-mediated gene expression. These results suggest that the SIK2-PP2A complex functions in the regulation of MEF2C-dependent transcription. Furthermore, this study suggests that the tightly linked regulatory loop comprised of the SIK2-PP2A and CaMKI and PME-1 networks may function in fine-tuning cell proliferation and stress response.
ESTHER : Lee_2014_J.Biol.Chem_289_21108
PubMedSearch : Lee_2014_J.Biol.Chem_289_21108
PubMedID: 24841198
Gene_locus related to this paper: human-PPME1

Title : Exon sequencing and association analysis of EPHX1 genetic variants with maintenance warfarin dose in a multiethnic Asian population - Chan_2011_Pharmacogenet.Genomics_21_35
Author(s) : Chan SL , Thalamuthu A , Goh BC , Chia KS , Chuah B , Wong A , Lee SC
Ref : Pharmacogenet Genomics , 21 :35 , 2011
Abstract : BACKGROUND AND OBJECTIVES: Warfarin inhibits vitamin K epoxide reductase, of which microsomal epoxide hydrolase is a putative member. Several studies have found signals of association with warfarin maintenance dose in the EPHX1 gene. The aim of this study was to determine the effects of EPHX1 variants on warfarin maintenance dose in a multiethnic Asian population. METHODS: We sequenced the exons of EPHX1 using PCR and direct sequencing in 279 patients consisting of three major ethnic groups receiving maintenance warfarin with a stable international normalized ratio. The effects of EPHX1 variants were assessed using multiple linear regression. RESULTS: An association between an intronic SNP rs1877724 and warfarin maintenance dose was found, with homozygous variant carriers requiring approximately 0.5 mg/day lower than wild type and heterozygotes after adjustment for covariates. However, its contribution is small, explaining only an additional 0.8% of the dose variability. Rare variants were pooled but there was no association between their presence and warfarin maintenance dose. However, the presence of noncoding rare SNPs was significantly associated with warfarin maintenance dose. CONCLUSION: Despite a significant finding in rs1877724, which concurs with an earlier study, overall, genetic variants in EPHX1 do not have a clinically significant impact on warfarin dose requirements in our population.
ESTHER : Chan_2011_Pharmacogenet.Genomics_21_35
PubMedSearch : Chan_2011_Pharmacogenet.Genomics_21_35
PubMedID: 21192345

Title : Gene cloning, purification, and characterization of a cold-adapted lipase produced by Acinetobacter baumannii BD5 - Park_2009_J.Microbiol.Biotechnol_19_128
Author(s) : Park IH , Kim SH , Lee YS , Lee SC , Zhou Y , Kim CM , Ahn SC , Choi YL
Ref : J Microbiol Biotechnol , 19 :128 , 2009
Abstract : Acinetobacter baumannii BD5 was isolated from waters of Baek-du mountain, and the lipase gene was cloned using a PCR technique. The deduced amino acid sequence of the lipase and lipase chaperone were found to encode proteins of 325 aa and 344 aa with a molecular mass of 35 kDa and 37 kDa, respectively. The lipase gene was cloned and expressed in Escherichia coli BL21 (trxB) as an inclusion body, which was subsequently solubilized by urea, and then purified using Ni-affinity chromatography. After being purified, the lipase was refolded by incubation at 4oC in the presence of a 1:10 molar ratio of lipase:chaperone. The maximal activity of the refolded lipase was observed at a temperature of 35 degrees and pH 8.3 when p-NP caprate (C10) was used as a substrate; however, 28% of the activity observed at 35 degrees was still remaining at 0 degrees . The stability of the purified enzyme at low temperatures indicates that it is a cold-adapted enzyme. The refolded lipase was activated by Ca2+, Mg2+, and Mn2+, whereas Zn2+ and Cu2+ inhibited it. Additionally, 0.1% Tween 20 increased the lipase activity by 33%, but SDS and Triton X-100 inhibited the lipase activity by 40% and 70%, respectively.
ESTHER : Park_2009_J.Microbiol.Biotechnol_19_128
PubMedSearch : Park_2009_J.Microbiol.Biotechnol_19_128
PubMedID: 19307760
Gene_locus related to this paper: acicp-AbiS

Title : Discovery of three novel lipase ( lipA1 , lipA2 , and lipA3) and lipase-specific chaperone ( lipB) genes present in Acinetobacter sp. DYL129 - Kim_2008_Appl.Microbiol.Biotechnol_77_1041
Author(s) : Kim SH , Park IH , Lee SC , Lee YS , Zhou Y , Kim CM , Ahn SC , Choi YL
Ref : Applied Microbiology & Biotechnology , 77 :1041 , 2008
Abstract : A microbe isolated from a soil sample obtained on Deog-yu Mountain in Korea, was found to produce an extracellular lipase. This microbe, which was designated as DYL129, was identified as an Acinetobacter sp. based on phylogenetic analysis of its 16S rDNA. A genomic library was constructed by using DYL129 fragment digested with HindIII and a recombinant plasmid, pLip-1, was selected for further analysis by colony polymerase chain reaction (PCR). Sequencing of a 3.8-kb insert in the pLip-1 clone revealed the presence of one incomplete and three complete open reading frames (ORFs). The ORFs were predicted to encode a partial lipase, two putative lipases and a 50S ribosomal protein. Genome-walking PCR also identified transcripts encoding a complete lipase chaperone and three lipaseA proteins. The lipase structural gene present in Acinetobacter sp. DYL129 was similar to the lipase structural gene found in Acinetobacter calcoaceticus BD413 (lipBA). However, the three lipase genes were located downstream of the chaperone gene in Acinetobacter sp. DYL129 (lipBA (1) A (2) A (3)), which differs from the location of these genes in A. calcoaceticus BD413. Although the amino acid sequences of these lipases (LipA(1), LipA(2), and LipA(3)) differed, both strains had a common "GHSHG" consensus motif, which is the conserved active-site pentapeptide of lipaseA. Moreover, all three lipases were found to share a conserved domain, the so-called alpha/beta hydrolase fold.
ESTHER : Kim_2008_Appl.Microbiol.Biotechnol_77_1041
PubMedSearch : Kim_2008_Appl.Microbiol.Biotechnol_77_1041
PubMedID: 17962933

Title : Phosphoglucose isomerases of hagfish, zebrafish, gray mullet, toad, and snake, with reference to the evolution of the genes in vertebrates - Kao_2002_Mol.Biol.Evol_19_367
Author(s) : Kao HW , Lee SC
Ref : Molecular Biology Evolution , 19 :367 , 2002
Abstract : Phosphoglucose isomerase (PGI) is a protein with multiple functions. To infer its structure changes and evolution in vertebrates, we cloned cDNAs encoding PGI genes from hagfish (Paramyxine yangi), gray mullet (Mugil cephalus), zebrafish (Danio rerio), toad (Bufo melanosticus), and snake (Boiga kraepelini). Only one PGI gene was cloned in each of hagfish, toad, and snake, but two PGI genes were found in zebrafish and gray mullet, respectively. The PGI of hagfish encodes 554 amino acids, in contrast to the PGIs of bonyfishes, toad, and snake which encode 553 amino acids and the PGIs of mammals which encode 558 amino acids. Among 558 aligned amino acid sites, there are 314 sites (56.27%) totally conserved. To see if diversifying selection acts on PGI amino acids of vertebrates, we calculated the pairwise ratio of nonsynonymous versus synonymous substitution per site (Ka/Ks) and the ratio of radical amino acid changes versus conservative amino acid changes per sites (dR/dC) between PGI sequences. The average pairwise ratio between nonsynonymous substitutions per nucleotide (Ka) and synonymous substitutions per nucleotide (Ks) among vertebrate PGI sequences equals 0.047 +/- 0.019. The average pairwise ratio between radical amino acid changes and conservative amino acid changes (dR/dC) among the vertebrate PGIs equal 0.938 +/- 0.158 for charge changes, 0.558 +/- 0.085 for polarity changes, and 0.465 +/- 0.0714 when both polarity and volume are considered. There is no amino acid within the vertebrate PGIs under diversifying selection as analyzed by the method of Yang et al. (2000b). The results suggest that the present vertebrate PGIs are at evolutionary stasis and are being subjected to intense purifying selection. The purifying selection is to maintain polarity and volume of the protein but not the charge groups of amino acids. Phylogenetic analysis reveals that vertebrate PGIs can be classified into three major groups: the mammalian, amphibian-reptilian, and teleostean PGIs. The gene tree suggests that the gene duplication event of PGI in bonyfishes occurred before diversification of Acanthopterygii but after the split of bonyfishes and tetrapods. The evolution of multiple functions of PGI is discussed.
ESTHER : Kao_2002_Mol.Biol.Evol_19_367
PubMedSearch : Kao_2002_Mol.Biol.Evol_19_367
PubMedID: 11919278