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Rat Malonyl-CoA Decarboxylase; Cloning, Expression in E. coli and its Biochemical Characterization
Lee, Gha-Young,Bahk, Young-Yil,Kim, Yu-Sam Korean Society for Biochemistry and Molecular Biol 2002 Journal of biochemistry and molecular biology Vol.35 No.2
Malonyl-CoA decarboxylase (E.C.4.1.1.9) catalyzes the conversion of malonyl-CoA to acetyl-CoA. Although the metabolic role of this enzyme has not been fully defined, it has been reported that its deficiency is associated with mild mental retardation, seizures, hypotonia, cadiomyopathy, developmental delay, vomiting, hypoglycemia, metabolic acidosis, and malonic aciduria. Here, we isolated a cDNA clone for malonyl CoA decarboxylase from a rat brain cDNA library, expressed it in E. coli, and characterized its biochemical properties. The full-length cDNA contained a single open-reading frame that encoded 491 amino acid residues with a calculated molecular weight of 54, 762 Da. Its deduced amino acid sequence revealed a 65.6% identity to that from the goose uropigial gland. The sequence of the first 38 amino acids represents a putative mitochondrial targeting sequence, and the last 3 amino acid sequences (SKL) represent peroxisomal targeting ones. The expression of malonyl CoA decarboxylase was observed over a wide range of tissues as a single transcript of 2.0 kb in size. The recombinant protein that was expressed in E. coli was used to characterize the biochemical properties, which showed a typical Michaelis-Menten substrate saturation pattern. The $K_m$ and $V_{max}$ were calculated to be $68\;{\mu}M$ and $42.6\;{\mu}mol/min/mg$, respectively.
Use of Li-K-Cd Alloy to Remove MCl3 in LiCl-KCl Eutectic Salt
Gha-Young Kim,Tack-Jin Kim,Junhyuk Jang,Si-Hyung Kim,Chang Hwa Lee,Sung-Jai Lee 한국방사성폐기물학회 2018 방사성폐기물학회지 Vol.16 No.3
Li-Cd 합금을 이용한 환원추출방식을 LiCl-KCl 기반의 drawdown 공정에 적용하게 되면, LiCl-KCl 공융염의 조성이 파괴되므로 공정온도를 높여야 하며, 전해정련 및 전해제련과 같은 공정에 LiCl-KCl 용융염을 재사용할 수 없게 된다. 따라서, 본 연구에서는 공융염 조성에 적합한 Li-K-Cd 합금을 제조하였으며, 이를 이용하여 U와 Nd가 포함된 LiCl-KCl 염에 투입하여 용 융염 내 UCl3의 제거가 가능한지 평가하였다. In this study, we prepared Li-K-Cd alloy, which meets the requirement of eutectic ratio of Li:K, to maintain the operating temperature of the drawdown process at 500℃ and to achieve the reuse of LiCl-KCl molten salt. The prepared Li-K-Cd alloys were added to LiCl-KCl salt bearing U and Nd at 500℃ to investigate the removal of UCl3 in the salt. The reduction of UCl3 in the salt was examined by measuring the OCP value of salt and analyzing the salt composition by ICP-OES. Reduction was also visually confirmed by change of salt color from dark purple to white. The experimental results reveal that the prepared Li-K-Cd alloy has reductive extractability for UCl3 in salt. By improving the preparation method, the Li-K-Cd alloy can be applied to the drawdown process.
PIASy-Mediated Sumoylation of SREBP1c Regulates Hepatic Lipid Metabolism upon Fasting Signaling
Lee, Gha Young,Jang, Hagoon,Lee, Jae Ho,Huh, Jin Young,Choi, Sekyu,Chung, Jongkyeong,Kim, Jae Bum American Society for Microbiology 2014 Molecular and cellular biology Vol.34 No.6
<P>SREBP1c is a key transcription factor that regulates <I>de novo</I> lipogenesis during anabolic periods. However, the molecular mechanisms involved in the suppression of SREBP1c under nutritional deprivation are largely unknown. In this study, we demonstrate that the small ubiquitin-related modifier (SUMO) E3 ligase, a protein inhibitor of activated STAT Y (PIASy), sumoylates SREBP1c at Lys98, leading to suppression of the hepatic lipogenic program upon fasting-induced signals. In primary hepatocytes, ablation of PIASy stimulated intracellular lipid accumulation through the induction of SREBP1c and its target genes. Given that protein kinase A (PKA) plays important roles in catabolic responses, activated PKA enhances the sumoylation of SREBP1c and potentiates the interaction between SREBP1c and PIASy. Notably, overexpression of PIASy in obese <I>db/db</I> mice ameliorated hepatic steatosis, while suppression of PIASy in lean (wild-type) mice stimulated hepatic lipogenesis with increased expression of SREBP1c target genes. Furthermore, PKA-mediated SREBP1c phosphorylation augmented SREBP1c sumoylation, subsequently leading to degradation of SREBP1c via ubiquitination. Together, these data suggest that PKA-induced SREBP1c sumoylation by PIASy is a key regulatory mechanism to turn off hepatic lipogenesis during nutritional deprivation.</P>
Jeong, Hyun Woo,Lee, Joo-Won,Kim, Woo Sik,Choe, Sung Sik,Kim, Kyung-Hee,Park, Ho Seon,Shin, Hyun Jung,Lee, Gha Young,Shin, Dongkyu,Lee, Hanjae,Lee, Jun Hee,Choi, Eun Bok,Lee, Hyeon Kyu,Chung, Heekyoun American Diabetes Association 2011 Diabetes Vol.60 No.2
<P><B>OBJECTIVE</B></P><P>Peroxisome proliferator–activated receptor (PPAR)-α/γ dual agonists have been developed to alleviate metabolic disorders. However, several PPARα/γ dual agonists are accompanied with unwanted side effects, including body weight gain, edema, and tissue failure. This study investigated the effects of a novel PPARα/γ dual agonist, CG301269, on metabolic disorders both in vitro and in vivo.</P><P><B>RESEARCH DESIGN AND METHODS</B></P><P>Function of CG301269 as a PPARα/γ dual agonist was assessed in vitro by luciferase reporter assay, mammalian one-hybrid assay, and analyses of PPAR target genes. In vitro profiles on fatty acid oxidation and inflammatory responses were acquired by fatty acid oxidation assay and quantitative (q)RT-PCR of proinflammatory genes. In vivo effect of CG301269 was examined in <I>db/db</I> mice. Total body weight and various tissue weights were measured, and hepatic lipid profiles were analyzed. Systemic glucose and insulin tolerance were measured, and the in vivo effect of CG301269 on metabolic genes and proinflammatory genes was examined by qRT-PCR.</P><P><B>RESULTS</B></P><P>CG301269 selectively stimulated the transcriptional activities of PPARα and PPARγ. CG301269 enhanced fatty acid oxidation in vitro and ameliorated insulin resistance and hyperlipidemia in vivo. In <I>db/db</I> mice, CG301269 reduced inflammatory responses and fatty liver, without body weight gain.</P><P><B>CONCLUSIONS</B></P><P>We demonstrate that CG301269 exhibits beneficial effects on glucose and lipid metabolism by simultaneous activation of both PPARα and PPARγ. Our data suggest that CG301269 would be a potential lead compound against obesity and related metabolic disorders.</P>