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이재철,Periasamy Anbu,김원호,노명주,이수진,서정우,허병기 한국생물공학회 2008 Biotechnology and Bioprocess Engineering Vol.13 No.5
The Δ9-elongase isolated from Thraustochytrium aureum, which contains a high level of polyunsaturated fatty acids (PU-FAs), was demonstrated to be associated with the synthesis of C20 PUFAs. The TaELO gene contains a 825 bp ORF that encodes a protein of 274 amino acids that shares a high similarity with other PUFA elongases. The expression of the TaELO gene in Pichia pastoris resulted in the elongation of linoleic acid (LA, C18:2; n-6) and α-linolenic acid (ALA, C18:3; n-3) to ei-cosadienoic acid (EDA, C20:2; n-6) and eicosatrienoic acid (ETrA, C20:3; n-3), respectively. The endogenous conversion rate of LA and ALA to EDA and ETrA was 32.68 and 38.57%, respectively. In addition, TaELO was also able to synthesize eicosenoic acid (C20:1; n-9) from oleic acid (OA, C18:1; n-9), even though the conversion level was low (2.81%). Further-more, TaELO was able to carry out the Δ6-elongation of γ-linolenic acid (GLA, C18:3; n-6) to dihomo-γ-linolenic acid (DGLA, C20:3; n-6) and Δ5-elongation of eicosapentaenoic acid (EPA, C20:5; n-3) to docosapentaenoic acid (DPA, C22:5; n-3). The conversion rate of GLA to DGLA and EPA to DPA were 93 and 28.36%, respectively. The TaELO protein was confirmed to have multifunctional activities, such as Δ9, Δ6, and Δ5-elongations as well as the elongation of monounsaturated fatty acid.
Bajpai Vivek K.,Kim, Hak-Ryul,Kang, Sun-Chul The Korean Society for Applied Biological Chemistr 2006 Journal of Applied Biological Chemistry (J. Appl. Vol.49 No.4
The in vitro anti-fungal activity of hydroxylated fatty acids obtained from microbial conversion by Psuedomonas aeruginosa PR3 using ricinoleic acid(RA), eicosadienoic acid(EDA) and conjugated linoleic acid(CLA) as substrates, was investigated. Bioconverted hydroxylated fatty acids showed different anti-fungal activities potentials against the range of phytopathogenic fungi such as Botrytis cinerea, Rhizoctonia solani, Fusarium oxysporum, Sclerotonia sclerotiorum, Colletotricum capsici, Fusarium solani and Phytophthora capsici. RA and EDA showed up to 50% fungal mycelial inhibition at the concentration of $5{\mu}l\;ml^{-1}$. RA, EDA and CLA also exhibited anti-fungal activities with minimum inhibitory concentration(MIC), ranging from 500 to $1000{\mu}g\;ml^{-1}$. Screening was also carried out using varied concentrations of bioconverted RA and EDA for determining the anti-fungal effect on the spore germination of different fungi. Bioconverted RA and EDA showed a considerable degree of spore germination inhibition.
김용성,송현주,박선영,민영실,임병옥,고성권,왕완균,손의동 대한약학회 2007 Archives of Pharmacal Research Vol.30 No.12
We investigated the signaling pathway on sphingosinephosphorylcholine (SPC) -induced contraction in cat esophageal smooth muscle cells. SPC induced in a dose-dependent manner contractile effect. We have previously shown that lysophospholipid (LPL) receptor subtypes including the S1P1, S1P2, S1P3, and S1P5 receptor are present in esophageal smooth muscle. Only EDG-5 (S1P2) receptor antibody penetration into permeablilized cells inhibited the SPCinduced contraction. Pertussis toxin (PTX) and specific antibodies to Gi1, Gi2, Gi3 and Go inhibited the contraction, implying that SPC-induced contraction depends on PTX-sensitive Gi1, Gi2, Gi3, and Go protein. A phospholipase inhibitor U73122 and incubation of permeabilized cells with PLC-β3 antibody inhibited SPC-induced contraction. The PKC-mediated contraction may be isozyme specific since only PKCε antibody inhibited the contraction. Preincubation with MEK inhibitor PD98059 blocked the SPC-induced contraction, but p38 MAPK inhibitor SB202190 did not. Cotreatment with GF109203X and PD98059 did not show synergistic effects, suggesting that these two kinases are involved in the same signaling pathway in the SPC-induced contraction. The data suggest that S1P-induced contraction in feline esophageal smooth muscle cells depends on activation of the Gi1, Gi2, Gi3 and Go proteins and the PLCβ3 isozyme via the S1P2 receptor, leading to stimulation of a PKCε pathway, which subsequently activates a p44/p42 MAPK pathway.