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Kim, S.H.,Kim, S.H.,Palaniyandi, S.A.,Yang, S.H.,Suh, J.W. Gauthier-Villars ; Elsevier Science Ltd 2015 Vol. No.
S-adenosyl-l-methionine (SAM) synthase (SAMS) catalyze the biosynthesis of SAM, which is a precursor for ethylene and polyamines, and a methyl donor for a number of biomolecules. A full-length cDNA of SAMS from Solanum brevidens was expressed in Arabidopsis thaliana to study its physiological function. RT-PCR analysis showed that SbSAMS expression was enhanced significantly in S. brevidens leaves upon treatment with salt, mannitol, ethephon, IAA and ABA. The transgenic SbSAMS overexpression lines accumulated higher levels S-adenosyl homocysteine (SAHC) and ethylene concomitantly with increased SAM level. Expression levels of genes related to ethylene biosynthesis such as ACC synthase, but not polyamine biosynthesis genes were enhanced in SbSAMS overexpressing Arabidopsis lines. In addition, ABA responsive, wound and pathogen-inducible genes were upregulated in SbSAMS transgenic Arabidopsis plants. Transgenic Arabidopsis lines exhibited higher salt and drought stress tolerance compared to those of vector control. Based on these results we conclude that SbSAMS is expressed under abiotic stress to produce SAM as a broad-spectrum signal molecule to upregulate stress-related genes including ethylene and ABA biosynthetic pathway genes responsible for ABA, pathogen and wound responses.
임정규,홍사악,박찬웅,김명석,서유헌,신상구,김용식,김혜원,이정수,장기철,이상국,장우현,김익상,Lim J.K.,Hong S.A.,Park C.W.,Kim M.S.,Suh Y.H.,Shin S.G.,Kim Y.S.,Kim H.W.,Lee J.S.,Chang K.C.,Lee S.K.,Chang K.C.,Kim I.S. 대한약리학회 1980 대한약리학잡지 Vol.16 No.2
The pharmacological and microbiological studies of Cefoperazone (T-1551, Toyama Chemical Co., Japan) were conducted in vitro and in vivo. The studies included stability and physicochemical characteristics, antimicrobial activity, animal and human pharmacokinetics, animal pharmacodynamics and safety evaluation of Cefoperazone sodium for injection. 1) Stability and physicochemical characteristics. Sodium salt of cefoperazone for injection had a general appearance of white crystalline powder which contained 0.5% water, and of which melting point was $187.2^{\circ}C$. The pH's of 10% and 25% aqueous solutions were 5.03 ana 5.16 at $25^{\circ}C$. The preparations of cefoperazone did not contain any pyrogenic substances and did not liberate histamine in cats. The drug was highly compatible with common infusion solutions including 5% Dextrose solution and no significant potency decrease was observed in 5 hours after mixing. Powdered cefoperazone sodium contained in hermetically sealed and ligt-shielded container was highly stable at $4^circ}C{\sim}37^{\circ}C$ for 12 weeks. When stored at $4^{\circ}C$ the potency was retained almost completely for up to one year. 2) Antimicrobial activity against clinical isolates. Among the 230 clinical isolates included, Salmonella typhi was the most susceptible to cefoperazone, with 100% inhibition at MIC of ${\leq}0.5{\mu}g/ml$. Cefoperazone was also highly active against Streptococcus pyogenes(group A), Kletsiella pneumoniae, Staphylococcus aureus and Shigella flexneri, with 100% inhibition at $16{\mu}g/ml$ or less. More than 80% of Escherichia coli, Enterobacter aerogenes and Salmonella paratyphi was inhibited at ${\leq}16{\mu}/ml$, while Enterobacter cloaceae, Serratia marcescens and Pseudomonas aerogenosa were somewhat less sensitive to cefoperagone, with inhibitions of 60%, 55% and 35% respectively at the same MIC. 3) Animal pharmacokinetics Serum concentration, organ distritution and excretion of cefoperazone in rats were observed after single intramuscular injections at doses of 20 mg/kg and 50 mg/kg. The extent of protein binding to human plasma protein was also measured in vitro br equilibrium dialysis method. The mean Peak serum concentrations of $7.4{\mu}g/ml$ and $16.4{\mu}/ml$ were obtained at 30 min. after administration of cefoperazone at doses of 20 mg/kg and 50 mg/kg respectively. The tissue concentrations of cefoperazone measured at 30 and 60 min. were highest in kidney. And the concentrations of the drug in kidney, liver and small intestine were much higher than in blood. Urinary and fecal excretion over 24 hours after injetcion ranged form 12.5% to 15.0% in urine and from 19.6% to 25.0% in feces, indicating that the gastrointestinal system is more important than renal system for the excretion of cefoperazone. The extent of binding to human plasma protein measured by equilibrium dialysis was $76.3%{\sim}76.9%$, which was somewhat lower than the others utilizing centrifugal ultrafiltration method. 4) Animal pharmacodynamics Central nervous system : Effects of cefoperazone on the spontaneous movement and general behavioral patterns of rats, the pentobarbital sleeping time in mice and the body temperature in rabbits were observed. Single intraperitoneal injections at doses of $500{\sim}2,000mg/kg$ in rats did not affect the spontaneous movement ana the general behavioral patterns of the animal. Doses of $125{\sim}500mg/kg$ of cefoperazone injected intraperitonealy in mice neither increased nor decreased the pentobarbital-induced sleeping time. In rabbits the normal body temperature was maintained following the single intravenous injections of $125{\sim}2,000mg/kg$ dose. Respiratory and circulatory system: Respiration rate, blood pressure, heart rate and ECG of anesthetized rabbits were monitored for 3 hours following single intravenous inje
Lee, S.J.,Kim, H.S.,Kim, D.J.,Yoon, H.J.,Kim, K.H.,Yoon, J.Y.,Suh, S.W. North-Holland Pub ; Elsevier Science Ltd 2011 FEBS letters Vol.585 No.2
Staphylococcus aureus LacD, a Class I tagatose-1,6-bisphosphate (TBP) aldolase, shows broadened substrate specificity by catalyzing the cleavage of 1,6-bisphosphate derivatives of d-tagatose, d-fructose, d-sorbose, and d-psicose. LacD.1 and LacD.2 are two closely-related Class I TBP aldolases in Streptococcus pyogenes. Here we have determined the crystal structures of S. aureus LacD and S. pyogenes LacD.1. Monomers of both enzymes are folded into a (β/α)<SUB>8</SUB> barrel and two monomers associate tightly to form a dimer in the crystals. The structures suggest that the residues E189 and S300 of rabbit muscle Class I fructose-1,6-bisphosphate (FBP) aldolase are important for substrate specificity. When we mutated the corresponding residues of S. aureus LacD, the mutants (L165E, L275S, and L165E/L275S) showed enhanced substrate specificity toward FBP. Structured summary: lacDbinds to lacD by X-ray crystallography(View interaction) lacD1binds to lacD1 by X-ray crystallography(View interaction)
Kim, T.,Kim, J.,Kim, Y.,Lee, T.,Kim, W.,Suh, K.S. Elsevier 2009 CURRENT APPLIED PHYSICS Vol.9 No.1
An aqueous dispersion of poly(3,4-ethylenedioxythiophene) (PEDOT) was prepared using a partially sulfonated poly(styrene-b-butadiene-b-styrene) (s-SBS) as a polyanion. For the preparation of s-SBS, poly(styrene-b-butadiene-b-styrene) was sulfonated to four different levels ranging from 44.1 to 64.8mol%. These sulfonated polymers were characterized with IR spectroscopy and <SUP>1</SUP>H NMR analysis to confirm sulfonation reaction. The preparation of the PEDOT complex was carried out through the chemical polymerization method in which the EDOT monomer starts to polymerize in the presence of s-SBS, resulting in an aqueous dispersion of PEDOT/s-SBS complex. The DC conductivities of PEDOT/s-SBS complexes were found to increase from 0.0003 to 0.05s/cm as the sulfonation level of the corresponding s-SBS increases, which is consistent with the data recorded by UV-vis spectrophotometer. From the XPS experiments, it was concluded that the concentration of PEDOT-rich phase in the PEDOT/s-SBS increases as the sulfonation level of s-SBS increase, thus facilitating the charge transport along the doped PEDOT chains.
Jang, J.Y.,Koh, M.,Bae, H.,An, D.R.,Im, H.N.,Kim, H.S.,Yoon, J.Y.,Yoon, H.J.,Han, B.W.,Park, S.B.,Suh, S.W. Elsevier Science 2017 Biochimica et biophysica acta. Proteins and proteo Vol.1865 No.6
<P>Peroxisome proliferator-activated receptor gamma (PPAR gamma) is a member of the nuclear receptor superfamily. It functions as a ligand-activated transcription factor and plays important roles in the regulation of adipocyte differentiation, type 2 diabetes mellitus, and inflammation. Many PPAR gamma agonists bind to the canonical ligand-binding pocket near the activation function-2 (AF-2) helix (i.e., helix H12) of the ligand-binding domain (LBD). More recently, an alternate ligand-binding site was identified in PPAR gamma LBD; it is located beside the 52 loop between the helices H2 ' and H3. We reported previously that the chirality of two optimized enantiomeric PPAR gamma ligands (S35 and R35) differentiates their PPAR gamma transcriptional activity, binding affinity, and inhibitory activity toward Cdk5 (cyclin-dependent kinase 5)-mediated phosphorylation of PPAR gamma at Ser245 (in PPAR gamma 1 numbering; Ser273 in PPAR gamma 2 numbering). S35 is a PPAR gamma phosphorylation inhibitor with promising glucose uptake potential, whereas R35 behaves as a potent conventional PPAR gamma agonist. To provide a structural basis for understanding the differential activities of these enantiomeric ligands, we have determined crystal structures of the PPAR gamma LBD in complex with either S35 or R35. S35 and R35 bind to the PPAR gamma LBD in significantly different manners. The partial agonist S35 occupies the alternate site near the Omega loop, whereas the full agonist R35 binds entirely to the canonical LBP. Alternate site binding of S35 affects the PPAR gamma transactivation and the inhibitory effect on PPAR gamma Ser245 phosphorylation. This study provides a useful platform for the development of a new generation of PPAR gamma ligands as anti-diabetic drug candidates.</P>