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AKGs enriched transcripts associated with PC-, lyso-PC and PAF metabolism

ABSTRACT: AKGs enriched transcripts associated with PC-, lyso-PC and PAF metabolism

PROVIDER: PRJNA516229 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8467860.fastq.gz	Fastqsanger.gz
	SRR8467870.fastq.gz	Fastqsanger.gz
	SRR8467861.fastq.gz	Fastqsanger.gz
	SRR8467871.fastq.gz	Fastqsanger.gz
	SRR8467862.fastq.gz	Fastqsanger.gz

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AKGs enriched transcripts associated with PC-, lyso-PC and PAF metabolism

Project description:AKGs enriched transcripts associated with PC-, lyso-PC and PAF metabolism. Moreover, AKGs suppressed interferon response genes. We submit heren three sets of NGS analyses. Experiment 1: We treated mouse adipose tissue macrophages (ATMs) with vehicle (ethanol) or 100 nM alkylglycerols (AKGs) for 18h in vitro. Experiment 2: We treated mouse 3T3-L1 preadipocytes with 1 nM neuropeptide FF (NPFF) for 18 h. Experiment 3: we isolated white adipose tissue from C57Black/6 male mice at 8 weeks of age, and brown adipose tissue from the same mice.

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Project description:Protein-protein interaction analysis for RNA Polymerase II and its elongation factors including: the PAF Complex, the FACT Complex, casein kinase II, DSIF, and TFIIF. These studies also characterized a number of casein kinase II phosphorylation sites on the subunits of the PAF Complex.

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Metabolism of platelet-activating factor (PAF; 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine) and lyso-PAF (1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine) by cultured rat Kupffer cells.

Project description:The metabolism of platelet-activating factor (PAF; identified as AGEPC: 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine) and lyso-PAF (lyso-GEPC: 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine) was investigated in cultured rat Kupffer cells. The rat Kupffer cells accumulated [3H]AGEPC and deacetylated this compound to the corresponding [3H]lyso-GEPC, which was the major metabolic product of [3H]AGEPC. [3H]Lyso-GEPC was distributed primarily in the supernatant fraction of incubated cells throughout the experimental interval. Only a very small portion of the [3H]lyso-GEPC was further converted to 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine (alkylacyl-GPC), indicating that this acylation process was not particularly active in these cells. When [3H]lyso-GEPC was incubated with Kupffer cells, the conversion of lyso-GEPC to AGEPC via the acetyltransferase reaction increased up to 30 min and declined thereafter. Bovine serum albumin (BSA) had a substantial influence on both the cellular uptake and the metabolism of [3H]AGEPC. An increase in the BSA concentration in the incubation media reduced the cellular uptake of [3H]AGEPC and the subsequent formation of lyso-GEPC. The results of this study suggest that the hepatic Kupffer cells play an important role in the metabolism of PAF. Moreover, these results infer that the regulation of the PAF level in certain hepatic pathophysiological situations may be a consequence of the production and subsequent metabolism of this potent lipid autacoid in the Kupffer cells of the liver.

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