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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/01/29 21:32:29」(JST)
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- 1. Pathogenesis of primary biliary cholangitis (primary biliary cirrhosis)
- 2. Clinical significance of antinuclear antibody staining patterns and associated autoantibodies
- 3. Carrier screening for genetic disease in the Ashkenazi Jewish population
English Journal
- A strategically designed small molecule attacks alpha-ketoglutarate dehydrogenase in tumor cells through a redox process.
- Stuart SD, Schauble A, Gupta S, Kennedy AD, Keppler BR, Bingham PM1, Zachar Z.Author information 1Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794, USA. paul.bingham@stonybrook.edu.AbstractBACKGROUND: Targeting cancer cell metabolism is recognized as a promising arena for development of cancer chemotherapeutics. Moreover, redox metabolism is also systematically altered in tumor cells. Indeed, there is growing reason to believe that tumor-specific alteration of redox control of metabolism will be central to understanding and attacking malignancy. We report here that lipoate analog CPI-613 attacks a gate-keeping, lipoate-using metabolic enzyme, alpha-ketoglutarate dehydrogenase (KGDH), by a redox mechanism selectively in tumors cells.
- Cancer & metabolism.Cancer Metab.2014 Mar 10;2(1):4. doi: 10.1186/2049-3002-2-4.
- BACKGROUND: Targeting cancer cell metabolism is recognized as a promising arena for development of cancer chemotherapeutics. Moreover, redox metabolism is also systematically altered in tumor cells. Indeed, there is growing reason to believe that tumor-specific alteration of redox control of metabol
- PMID 24612826
- Comparative proteome analysis of two Streptococcus agalactiae strains from cultured tilapia with different virulence.
- Li W1, Su YL2, Mai YZ1, Li YW1, Mo ZQ3, Li AX4.Author information 1Key Laboratory for Aquatic Products Safety of Ministry of Education/State Key Laboratory of Biocontrol, The School of Life Sciences, Sun Yat-sen University, 135 Xingang West Street, Haizhu District, Guangzhou 510275, Guangdong Province, PR China.2Key Laboratory for Aquatic Products Safety of Ministry of Education/State Key Laboratory of Biocontrol, The School of Life Sciences, Sun Yat-sen University, 135 Xingang West Street, Haizhu District, Guangzhou 510275, Guangdong Province, PR China; Key Laboratory of South China Sea Fishery Resources Exploitation & Utilization, Ministry of Agriculture, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, Guangdong Province, PR China.3College of Animal Science, South China Agricultural University, Guangzhou, Guangdong Province, PR China.4Key Laboratory for Aquatic Products Safety of Ministry of Education/State Key Laboratory of Biocontrol, The School of Life Sciences, Sun Yat-sen University, 135 Xingang West Street, Haizhu District, Guangzhou 510275, Guangdong Province, PR China. Electronic address: lianxing@mail.sysu.edu.cn.AbstractStreptococcus agalactiae is a major piscine pathogen, which causes significant morbidity and mortality among numerous fish species, and results in huge economic losses to aquaculture. Many S. agalactiae strains showing different virulence characteristics have been isolated from infected tilapia in different geographical regions throughout South China in the recent years, including natural attenuated S. agalactiae strain TFJ0901 and virulent S. agalactiae strain THN0901. In the present study, survival of tilapia challenged with S. agalactiae strain TFJ0901 and THN0901 (107CFU/fish) were 93.3% and 13.3%, respectively. Moreover, there are severe lesions of the examined tissues in tilapia infected with strain THN0901, but no significant histopathological changes were observed in tilapia infected with the strain TFJ0901. In order to elucidate the factors responsible for the invasive potential of S. agalactiae between two strains TFJ0901 and THN0901, a comparative proteome analysis was applied to identify the different protein expression profiles between the two strains. 506 and 508 cellular protein spots of S. agalactiae TFJ0901 and THN0901 were separated by two dimensional electrophoresis, respectively. And 34 strain-specific spots, corresponding to 27 proteins, were identified successfully by MALDI-TOF mass spectrometry. Among them, 23 proteins presented exclusively in S. agalactiae TFJ0901 or THN0901, and the other 4 proteins presented in different isomeric forms between TFJ0901 and THN0901. Most of the strain-specific proteins were just involved in metabolic pathways, while 7 of them were presumed to be responsible for the virulence differences of S. agalactiae strain TFJ0901 and THN0901, including molecular chaperone DnaJ, dihydrolipoamide dehydrogenase, thioredoxin, manganese-dependent inorganic pyrophosphatase, elongation factor Tu, bleomycin resistance protein and cell division protein DivIVA. These virulence-associated proteins may contribute to identify new diagnostic markers and help to understand the pathogenesis of S. agalactiae.
- Veterinary microbiology.Vet Microbiol.2014 Feb 7. pii: S0378-1135(14)00068-6. doi: 10.1016/j.vetmic.2014.01.033. [Epub ahead of print]
- Streptococcus agalactiae is a major piscine pathogen, which causes significant morbidity and mortality among numerous fish species, and results in huge economic losses to aquaculture. Many S. agalactiae strains showing different virulence characteristics have been isolated from infected tilapia in d
- PMID 24594355
- Elevated plasma citrulline: look for dihydrolipoamide dehydrogenase deficiency.
- Haviv R1, Zeharia A, Belaiche C, Haimi Cohen Y, Saada A.Author information 1Monique and Jacques Roboh Department of Genetic Research, Hadassah, Hebrew University Medical Center, Jerusalem, Israel.AbstractThe E3 subunit of the pyruvate dehydrogenase complex (dihydrolipoamide dehydrogenase/dihydrolipoyl dehydrogenase/DLD/lipoamide dehydrogenase/LAD), is a mitochondrial matrix enzyme and also a part of the branched-chain ketoacid dehydrogenase and alpha-ketoglutarate dehydrogenase complexes. DLD deficiency (MIM #246900), is relatively frequent in the Ashkenazi Jewish population but occurs in other populations as well. Early diagnosis is important to prevent episodes of metabolic decompensation, liver failure, and encephalopathy. The clinical presentations are varied and may include Reye-like syndrome, hepatic failure, myopathy, and myoglobinuria. Laboratory markers, such as elevated urinary alpha-ketoglutarate, blood pyruvate, lactate, and ammonia, are mostly nonspecific and not always present, making the diagnosis difficult. Since we observed elevated plasma citrulline levels in a number of confirmed cases, we retrospectively examined the value of citrulline as a biochemical marker for DLD deficiency. Data was gathered from the files of 17 pediatric patients with DLD deficiency, confirmed by enzymatic and genetic analysis. The control group included 19 patients in whom urea cycle defects were ruled out but DLD deficiency was suspected. Seven of the DLD-deficient patients presented with elevated plasma citrulline levels (median value 205 μM, range 59-282 μM) (normal range 1-45 μM) while none in the control patient group. In five patients, elevated citrulline was associated with elevated plasma glutamine and metabolic acidosis. Interestingly, elevated plasma citrulline was associated with the common G229C mutation. In conclusion, we suggest that elevated plasma citrulline in the absence of urea cycle defects warrants an investigation for DLD deficiency.
- European journal of pediatrics.Eur J Pediatr.2014 Feb;173(2):243-5. doi: 10.1007/s00431-013-2153-x. Epub 2013 Aug 31.
- The E3 subunit of the pyruvate dehydrogenase complex (dihydrolipoamide dehydrogenase/dihydrolipoyl dehydrogenase/DLD/lipoamide dehydrogenase/LAD), is a mitochondrial matrix enzyme and also a part of the branched-chain ketoacid dehydrogenase and alpha-ketoglutarate dehydrogenase complexes. DLD defici
- PMID 23995961
Japanese Journal
- 低強度・長時間水泳運動トレーニングによりラット骨格筋で発現するタンパク質のプロテオミクス ; 2D-DIGE解析
- 山口 航,藤本 恵理,樋口 満 [他],田畑 泉
- 体力科學 60(5), 511-518, 2011-10-01
- … All proteins were identified by MALDI-TOF/MS. Conclusion: The proteomic 2D-DIGE analysis following LIT identified expressions of skeletal muscle proteins, includingATPsynα, UQCRC1, dihydrolipoamide dehydrogenase, dihydrolipoamide acetyltransferase, that were not previously reported to change their expressions after exercise-training. …
- NAID 10030027192
- Nongradient blue native gel analysis of serum proteins and in-gel detection of serum esterase activities
- THANGTHAENG Nopporn,SUMIEN Nathalie,FORSTER Michael J.,SHAH Ruchir A.,YAN Liang-Jun
- Journal of chromatography. B, Analytical technologies in the biomedical and life sciences 879(5), 386-394, 2011-02-15
- NAID 10029517013
- Gene cloning and characterization of dihydrolipoamide dehydrogenase from Microbacterium luteolum : A useful enzymatic regeneration system of NAD^+ from NADH(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Kurokawa Junji,Asano Manabu,Nomoto Shunsuke [他],Makino Yoshihide,Itoh Nobuya
- Journal of bioscience and bioengineering 109(3), 218-223, 2010-03-00
- … Dihydrolipoamide dehydrogenase (LPD), a useful biocatalyst for regenerating NAD^+, was purified from Microbacterium luteolum JCM 9174, and the gene encoding LPD was cloned from the genomic DNA. …
- NAID 110007612425
Related Links
- Dihydrolipoamide is a molecule produced by the action of dihydrolipoyl dehydrogenase upon lipoamide. ... Type of Activity: independent Audience: Teacher Student Subjects: Molecules Delocalisation Characteristics of pure ...
- Showing metabocard for Dihydrolipoamide (HMDB00985) Identification Taxonomy Ontology Physical properties Spectra Biological properties Concentrations Links References enzymes (4) Show 4 proteins XML enzymes (4) 3.6 ...
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★リンクテーブル★
| リンク元 | 「ジヒドロリポアミド」 |
| 拡張検索 | 「dihydrolipoamide acetyltransferase」「dihydrolipoamide dehydrogenase」 |
「ジヒドロリポアミド」
「dihydrolipoamide acetyltransferase」
ジヒドロリ・アミドアセチルトランスフェラーゼ
- 関
- dihydrolipoyl acetyltransferase、dihydrolipoyllysine-residue acetyltransferase
「dihydrolipoamide dehydrogenase」
ジヒドロリ・アミドデヒドロゲナーゼ、ジヒドロリ・アミド脱水素酵素