scholarly journals Strategic Feeding of Ammonium and Metal Ions for Enhanced GLA-Rich Lipid Accumulation inCunninghamella bainieri2A1

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Shuwahida Shuib ◽  
Wan Nazatul Naziah Wan Nawi ◽  
Ekhlass M. Taha ◽  
Othman Omar ◽  
Abdul Jalil Abdul Kader ◽  
...  
Keyword(s):  
Metal Ions ◽  
Lipid Content ◽  
Lipid Accumulation ◽  
Malic Enzyme ◽  
Fatty Acid Synthase ◽  
Ammonium Tartrate ◽  
Atp Citrate Lyase ◽  
Enzymes Activities ◽  
Citrate Lyase ◽  
Strategic Feeding

Strategic feeding of ammonium and metal ions (Mg2+, Mn2+, Fe3+, Cu2+, Ca2+, Co2+, and Zn2+) for enhanced GLA-rich lipid accumulation inC. bainieri2A1 was established. When cultivated in nitrogen-limited medium, the fungus produced up to 30% lipid (g/g biomass) with 12.9% (g/g lipid) GLA. However, the accumulation of lipid stopped at 48 hours of cultivation although glucose was abundant. This event occurred in parallel to the diminishing activity of malic enzyme (ME), fatty acid synthase (FAS), and ATP citrate lyase (ACL) as well as the depletion of metal ions in the medium. Reinstatement of the enzymes activities was achieved by feeding of ammonium tartrate, but no increment in the lipid content was observed. However, increment in lipid content from 32% to 50% (g/g biomass) with 13.2% GLA was achieved when simultaneous feeding of ammonium, glucose, and metal ions was carried out. This showed that the cessation of lipid accumulation was caused by diminishing activities of the enzymes as well as depletion of the metal ions in the medium. Therefore, strategic feeding of ammonium and metal ions successfully reinstated enzymes activities and enhanced GLA-rich lipid accumulation inC. bainieri2A1.

The role of ATP citrate lyase, malic enzyme and fatty acid synthase in the regulation of lipid accumulation in Cunninghamella sp. 2A1

2010 ◽  
Vol 61 (3) ◽  
pp. 463-468 ◽  
Author(s):  
Aidil Abdul Hamid ◽  
Noor Fatmawati Mokhtar ◽  
Ekhlass M. Taha ◽  
Othman Omar ◽  
Wan Mohtar Wan Yusoff
Keyword(s):  
Fatty Acid ◽  
Lipid Accumulation ◽  
Malic Enzyme ◽  
Fatty Acid Synthase ◽  
Atp Citrate Lyase ◽  
Citrate Lyase

scholarly journals Influence of N-limitation on Malic Enzyme Isoforms and Lipogenesis of Cunninghamella bainieri 2A1

2014 ◽  
Vol 67 (1) ◽  
Author(s):  
Aidil Abdul Hamid ◽  
Shuwahida Shuib ◽  
Ekhlass M. Taha ◽  
Othman Omar ◽  
Mohd Sahaid Khalil ◽  
...  
Keyword(s):  
Lipid Content ◽  
Lipid Accumulation ◽  
Malic Enzyme ◽  
Lipid Synthesis ◽  
Lower Activity ◽  
Ammonium Tartrate ◽  
Ammonium Ions ◽  
Activity Staining ◽  
N Limitation ◽  
Enzyme Isoforms

The influence of the presence of ammonium ions in growth culture on malic enzyme (ME) isoforms activity and lipogenesis in Cunninghamella bainieri 2A1 was investigated. The fungus was cultivated in a nitrogen-limiting medium for 120 h at 30oC under two conditions. One of the cultures was intermittently fed with ammonium tartrate to maintain the ammonium concentrations above 0.5 g/L. The second culture was performed without any feeding to allow N limitation, thus promoting lipid accumulation. Activity staining of ME isoforms was carried out for both cultures. The culture which was not intermittently fed with ammonium tartrate achieved a maximum lipid content of 35% (g/g biomass) at 48 h. This culture possessed five ME isoforms (A, B, C, D and E) with isoform E showing a parallel correlation to lipid accumulation profile. In contrast, intensity of bands representing isoform D decreased as lipid accumulated. No appreciable differences of all other isoforms were observed. However, the culture which was intermittently fed with ammonium tartrate, accumulated only up to 16% lipid (g/g biomass). All isoforms were present but with a more pronounced activity of isoform D and a lower activity of isoform E was observed. These findings support further evidence that isoform E is the key isoform for lipid synthesis in C. bainieri 2A1.

scholarly journals In Steatotic Cells, ATP-Citrate Lyase mRNA Is Efficiently Translated through a Cap-Independent Mechanism, Contributing to the Stimulation of De Novo Lipogenesis

2020 ◽  
Vol 21 (4) ◽  
pp. 1206 ◽  
Author(s):  
Luisa Siculella ◽  
Laura Giannotti ◽  
Mariangela Testini ◽  
Gabriele V. Gnoni ◽  
Fabrizio Damiano
Keyword(s):  
Lipid Accumulation ◽  
De Novo ◽  
Cell Model ◽  
Mrna Translation ◽  
De Novo Lipogenesis ◽  
Atp Citrate Lyase ◽  
Entry Site ◽  
Alcoholic Fatty Liver ◽  
Citrate Lyase ◽  
Independent Mechanism

Non-alcoholic fatty liver disease (NAFLD) is a chronic disease in which excessive amount of lipids is accumulated as droplets in hepatocytes. Recently, cumulative evidences suggested that a sustained de novo lipogenesis can play an important role in NAFLD. Dysregulated expression of lipogenic genes, including ATP-citrate lyase (ACLY), has been found in liver diseases associated with lipid accumulation. ACLY is a ubiquitous cytosolic enzyme positioned at the intersection of nutrients catabolism and cholesterol and fatty acid biosyntheses. In the present study, the molecular mechanism of ACLY expression in a cell model of steatosis has been reported. We identified an internal ribosome entry site (IRES) in the 5′ untranslated region of the ACLY mRNA, that can support an efficient mRNA translation through a Cap-independent mechanism. In steatotic HepG2 cells, ACLY expression was up-regulated through IRES-mediated translation. Since it has been demonstrated that lipid accumulation in cells induces endoplasmic reticulum (ER) stress, the involvement of this cellular pathway in the translational regulation of ACLY has been also evaluated. Our results showed that ACLY expression was increased in ER-stressed cells, through IRES-mediated translation of ACLY mRNA. A potential role of the Cap-independent translation of ACLY in NAFLD has been discussed.

scholarly journals RNA-seq reveals novel mechanistic targets of withaferin A in prostate cancer cells

2020 ◽  
Vol 41 (6) ◽  
pp. 778-789 ◽  
Author(s):  
Su-Hyeong Kim ◽  
Eun-Ryeong Hahm ◽  
Krishna B Singh ◽  
Sruti Shiva ◽  
Jacob Stewart-Ornstein ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Acid Synthesis ◽  
Acetyl Coa Carboxylase ◽  
Rna Seq ◽  
Atp Citrate Lyase ◽  
Acetyl Coa ◽  
Citrate Lyase

Abstract Withaferin A (WA) is a promising phytochemical exhibiting in vitro and in vivo anticancer activities against prostate and other cancers, but the mechanism of its action is not fully understood. In this study, we performed RNA-seq analysis using 22Rv1 human prostate cancer cell line to identify mechanistic targets of WA. Kyoto Encyclopedia of Genes and Genomes pathway analysis of the differentially expressed genes showed most significant enrichment of genes associated with metabolism. These results were validated using LNCaP and 22Rv1 human prostate cancer cells and Hi-Myc transgenic mice as models. The intracellular levels of acetyl-CoA, total free fatty acids and neutral lipids were decreased significantly following WA treatment in both cells, which was accompanied by downregulation of mRNA (confirmed by quantitative reverse transcription-polymerase chain reaction) and protein levels of key fatty acid synthesis enzymes, including ATP citrate lyase, acetyl-CoA carboxylase 1, fatty acid synthase and carnitine palmitoyltransferase 1A. Ectopic expression of c-Myc, but not constitutively active Akt, conferred a marked protection against WA-mediated suppression of acetyl-CoA carboxylase 1 and fatty acid synthase protein expression, and clonogenic cell survival. WA was a superior inhibitor of cell proliferation and fatty acid synthesis in comparison with known modulators of fatty acid metabolism including cerulenin and etomoxir. Intraperitoneal WA administration to Hi-Myc transgenic mice (0.1 mg/mouse, three times/week for 5 weeks) also resulted in a significant decrease in circulating levels of total free fatty acids and phospholipids, and expression of ATP citrate lyase, acetyl-CoA carboxylase 1, fatty acid synthase and carnitine palmitoyltransferase 1A proteins in the prostate in vivo.

scholarly journals Normal Flux through ATP-Citrate Lyase or Fatty Acid Synthase Is Not Required for Glucose-stimulated Insulin Secretion

2007 ◽  
Vol 282 (43) ◽  
pp. 31592-31600 ◽  
Author(s):  
Jamie W. Joseph ◽  
Matthew L. Odegaard ◽  
Sarah M. Ronnebaum ◽  
Shawn C. Burgess ◽  
Jeffrey Muehlbauer ◽  
...  
Keyword(s):  
Insulin Secretion ◽  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Atp Citrate Lyase ◽  
Citrate Lyase ◽  
Glucose Stimulated Insulin Secretion

Triiodothyronine Control of ATP-Citrate Lyase and Malic Enzyme During Differentiation of a Murine Preadipocyte Cell Line

1991 ◽  
Vol 23 (09) ◽  
pp. 423-427 ◽  
Author(s):  
J. Gharbi-Chihi ◽  
T. Facchinetti ◽  
J. Bergé-Lefranc ◽  
J. Bonne ◽  
J. Torresani
Keyword(s):  
Cell Line ◽  
Malic Enzyme ◽  
Atp Citrate Lyase ◽  
Citrate Lyase

scholarly journals Prognostic Value of Malic Enzyme and ATP-Citrate Lyase in Non-Small Cell Lung Cancer of the Young and the Elderly

PLoS ONE ◽  
2015 ◽  
Vol 10 (5) ◽  
pp. e0126357 ◽  
Author(s):  
Agnes Csanadi ◽  
Claudia Kayser ◽  
Marcel Donauer ◽  
Vera Gumpp ◽  
Konrad Aumann ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Malic Enzyme ◽  
Prognostic Value ◽  
The Elderly ◽  
Small Cell ◽  
Small Cell Lung ◽  
Atp Citrate Lyase ◽  
Citrate Lyase

Glucocorticoid regulation of fatty acid synthase gene expression in fetal rat lung

1993 ◽  
Vol 265 (2) ◽  
pp. L140-L147 ◽  
Author(s):  
Z. X. Xu ◽  
W. Stenzel ◽  
S. M. Sasic ◽  
D. A. Smart ◽  
S. A. Rooney
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Fatty Acid Biosynthesis ◽  
Fetal Lung ◽  
Acetyl Coa Carboxylase ◽  
Rat Lung ◽  
Acid Biosynthesis ◽  
Atp Citrate Lyase ◽  
Acetyl Coa ◽  
Citrate Lyase

There are developmental and glucocorticoid-induced increases in the rate of fatty acid biosynthesis and in the activity of fatty acid synthase in late gestation fetal lung. We have now measured mRNA levels of fatty acid synthase and of two other enzymes of fatty acid biosynthesis, ATP citrate lyase and acetyl-CoA carboxylase, in developing fetal and postnatal rat lung and in fetal lung explants cultured with and without dexamethasone. There was a developmental increase in the mRNA for fatty acid synthase with the maximum level being reached on fetal day 21 (term is fetal day 22). This profile was similar to that reported for de novo fatty acid synthesis and fatty acid synthase activity. There was a similar but less pronounced developmental increase in the mRNA for ATP citrate lyase and a corresponding increase in its activity. There was no developmental change in the mRNA for acetyl-CoA carboxylase. Dexamethasone increased the level of fatty acid synthase mRNA approximately threefold but had no effect on those for ATP citrate lyase and acetyl-CoA carboxylase. The effect of dexamethasone on fatty acid synthase mRNA was rapid, biphasic, and partly inhibited by actinomycin D and cycloheximide. We conclude that glucocorticoids increase expression of the gene for fatty acid synthase in fetal lung. The effect of the hormone appears to be due to increased transcription and post-transcriptional events and is dependent on protein synthesis.

scholarly journals Zonation of hepatic lipogenic enzymes identified by dual-digitonin-pulse perfusion

1989 ◽  
Vol 259 (3) ◽  
pp. 821-829 ◽  
Author(s):  
J L Evans ◽  
B Quistorff ◽  
L A Witters
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Fatty Acid Synthase ◽  
Acid Synthesis ◽  
Male Rats ◽  
Male Rat ◽  
Acetyl Coa Carboxylase ◽  
Atp Citrate Lyase ◽  
Acetyl Coa ◽  
Citrate Lyase

The zonal distribution within rat liver of acetyl-CoA carboxylase, ATP citrate-lyase and fatty acid synthase, the principal enzymes of fatty acid synthesis, was investigated by using dual-digitonin-pulse perfusion. Analysis of enzyme mass by immunoblotting revealed that, in normally feeding male rats, the periportal/perivenous ratio of acetyl-CoA carboxylase mass was 1.9. The periportal/perivenous ratio of ATP citrate-lyase mass was 1.4, and fatty acid synthase exhibited the largest periportal/perivenous mass gradient, having a ratio of 3.1. This pattern of enzyme distribution was observed in male rats only; in females, the periportal/perivenous ratio of enzyme mass was nearly equal. The periportal/perivenous gradients for acetyl-CoA carboxylase, ATP citrate-lyase and fatty acid synthase observed in fed (and fasted) males were abolished when animals were fasted (48 h) and refed (30 h) with a high-carbohydrate/low-fat diet. As determined by enzyme assay of eluates obtained from the livers of normally feeding male rats, there is also periportal zonation of acetyl-CoA carboxylase activity, expressed either as units per mg of eluted protein or units per mg of acetyl-CoA carboxylase protein, suggesting the existence of gradients in both enzyme mass and specific activity. From these results, we conclude that the enzymes of fatty acid synthesis are zonated periportally in the liver of the normally feeding male rat.

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