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Gene expression analysis of bone marrow cells with high aldehyde dehydrogenase activity (ALDHbr) obtained from male and female mice.

ABSTRACT: Gene expression analysis of bone marrow cells with high aldehyde dehydrogenase activity (ALDHbr) obtained from male and female mice.

PROVIDER: PRJNA1156171 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR30534140_1.fastq.gz	Fastqsanger.gz
	SRR30534140_2.fastq.gz	Fastqsanger.gz
	SRR30534141_1.fastq.gz	Fastqsanger.gz
	SRR30534141_2.fastq.gz	Fastqsanger.gz
	SRR30534142_1.fastq.gz	Fastqsanger.gz

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Gene expression analysis of bone marrow cells with high aldehyde dehydrogenase activity (ALDHbr) obtained from male and female mice.

Project description:To investigate the difference of male and female murine bone marrow ALDHbr cells collected by fluorescence activated cell sorting, gene expression analysis was performed.

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Role of aldehyde dehydrogenase on the metabolic regulation in Clostridium ljungdahlii fermentation

Project description:Clostridium ljungdahlii not only utilizes CO, but also H2 as energy source during autotrophic growth. And C. ljungdahlii also grows in fructose fermentation. In theory, fructose is a more energetically favourable energy source than syngas in the fermentation of C. ljungdahlii. However, C. ljungdahlii grows insufficiently in fructose and produces less acetate and ethanol, compared to syngas fermentation. In this study, C. ljungdahlii wild type and mutants were fermented on fructose. C. ljungdahlii produced less ethanol than the ΔadhE1 mutant and consumed less fructose. The ΔadhE1+2 mutant cannot grow in the syngas fermentation and produced less ethanol among the three strains. The results showed that aldehyde dehydrogenase inactivation led to efficient metabolism in C. ljungdahlii and the bifunctional aldehyde/alcohol dehydrogenases inactivation led to decrease metabolism. Thus, comparative transcriptomes among cells grown on fructose of three strains were performed to investigate gene expression profiles based on three biological replicates.

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Nuclear receptor NHR-49 promotes peroxisome proliferation to compensate for aldehyde dehydrogenase deficiency in C. elegans

Project description:The intracellular level of fatty aldehydes is tightly regulated to minimize the formation of toxic aldehyde adducts of cellular components. Accordingly, deficiency of a fatty aldehyde dehydrogenase FALDH causes the neurologic disorder Sjögren-Larsson syndrome (SLS) in humans. However, cellular responses to unresolved, elevated fatty aldehyde levels are poorly understood. Based on lipidomic and imaging analysis, we report that the loss of endoplasmic reticulum-, mitochondria- and peroxisomes-associated ALH-4, the C. elegans FALDH ortholog, increases fatty aldehyde levels and reduces fat storage. ALH-4 deficiency in the intestine, cell-nonautonomously induces NHR-49/NHR-79-dependent hypodermal peroxisome proliferation. This is accompanied by the upregulation of catalases and fatty acid catabolic enzymes, as indicated by RNA sequencing. Such a response is required to counteract ALH-4 deficiency since alh-4; nhr-49 double mutant animals are not viable. Our work reveals unexpected inter-tissue communication of fatty aldehyde levels, and suggests pharmacological modulation of peroxisome proliferation as a therapeutic strategy for SLS.

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2 Role of aldehyde dehydrogenase on the metabolic regulation in Clostridium ljungdahlii fermentation

Project description:Clostridium ljungdahlii can utilize CO as energy source during autotrophic growth. C. ljungdahlii grows sufficiently in CO and produces ethanol as the main product. In this study, C. ljungdahlii wild type and mutant were fermented on CO. C. ljungdahlii produced more ethanol than the ΔadhE1 mutant. The results showed that aldehyde dehydrogenase inactivation led to inefficient metabolism in C. ljungdahlii. Thus, comparative transcriptomes among cells grown on CO of WT and ΔadhE1 mutant were performed to investigate gene expression profiles based on three biological replicates.

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Role of aldehyde dehydrogenase on the metabolic regulation in Clostridium ljungdahlii fermentation

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