β-Oxidation in hepatocyte cultures from mice with peroxisomal gene knockouts

Dirkx, Ruud; Meyhi, Els; Asselberghs, Stanny; Reddy, Janardan K.; Baes, Myriam; Veldhoven, Paul P. Van

doi:10.1016/j.bbrc.2007.03.198

Cited by 41 publications

(39 citation statements)

References 39 publications

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“…The phosphorylated form of ACC, a key enzyme in lipogenesis, is inactive, which results in reduced generation of malonyl-CoA. This is in agreement with reduced lipid synthesis in L-Pex5 Ϫ/Ϫ mice (32) and with increased fatty acid oxidation as has been observed both in primary hepatocytes (28) and in vivo (32). …”

Section: L-pex5supporting

confidence: 74%

“…A striking observation is that hepatic PEX5 deficiency activates catabolic processes such as glycolysis and fatty acid oxidation (28,32), while impairing anabolic processes such as glycogen synthesis and gluconeogenesis, but also de novo fatty acid synthesis (as already previously reported (32)). This array of metabolic adaptations is compatible with activation of AMPK, which is driven by an increased cellular AMP/ATP ratio (52).…”

Section: Discussionsupporting

confidence: 59%

“…With regard to the consequences of activated AMPK on lipid metabolism, we previously documented in L-Pex5 Ϫ/Ϫ mice that lipogenesis is reduced (32) and that fatty acid oxidation is stimulated in vitro (28) and in vivo (32), in agreement with increased phosphorylation of ACC. Nonetheless, despite this increased capacity for lipid catabolism, L-Pex5 Ϫ/Ϫ hepatocytes are unable to maintain their energy balance.…”

Section: L-pex5mentioning

confidence: 79%

“…Hepatocyte Isolation-Hepatocytes were isolated as described previously (28) and seeded at 0.15 million cells/cm 2 . For some experiments, hepatocytes were infected with adenovirus expressing PGC-1␣ (derived from Addgene plasmid 14426) (29) and with control adenovirus (30 pfu/cell) or treated with the AMPK inhibitor compound c (10 M).…”

Section: Analysis In Primary Hepatocytesmentioning

confidence: 99%

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Carbohydrate Metabolism Is Perturbed in Peroxisome-deficient Hepatocytes Due to Mitochondrial Dysfunction, AMP-activated Protein Kinase (AMPK) Activation, and Peroxisome Proliferator-activated Receptor γ Coactivator 1α (PGC-1α) Suppression

Peeters

Fraisl

Berg

et al. 2011

Journal of Biological Chemistry

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Background:It is not known whether peroxisomes influence hepatic carbohydrate metabolism. Results: Carbohydrate metabolism is perturbed in peroxisome-deficient mouse liver through mitochondrial deficits, AMPK, and PGC-1␣. Conclusion: Dysfunctional peroxisome metabolism disrupts carbohydrate homeostasis by indirect mechanisms. Significance: The impact of peroxisome deficiency on liver metabolism is broader than expected.

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Section: L-pex5supporting

confidence: 74%

Section: Discussionsupporting

confidence: 59%

Section: L-pex5mentioning

confidence: 79%

Section: Analysis In Primary Hepatocytesmentioning

confidence: 99%

See 2 more Smart Citations

Carbohydrate Metabolism Is Perturbed in Peroxisome-deficient Hepatocytes Due to Mitochondrial Dysfunction, AMP-activated Protein Kinase (AMPK) Activation, and Peroxisome Proliferator-activated Receptor γ Coactivator 1α (PGC-1α) Suppression

Peeters

Fraisl

Berg

et al. 2011

Journal of Biological Chemistry

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“…However recent studies using human skin fibroblasts showed that the β-oxidation of C16 dicarboxylic acids occurs only in peroxisomes [99]. Dicarboxylic acids enter peroxisomes, likely as the CoA ester, and are then chain shortened by β-oxidation, involving the straight chain acyl-CoA oxidase, the D-and L-specific bifunctional proteins and SCPx [99,100]. Medium-and long-chain dicarboxylic acids are formed from ω-oxidation as described above, whereas short chain dicarboxylic acids (such as adipic, suberic and sebacic acid) are formed from chain shortening of longer chain dicarboxylic acids by β-oxidation.…”

Section: Involvement Of Acot4 and Acot8 In Regulation Of Peroxisomal mentioning

confidence: 99%

Novel functions of acyl-CoA thioesterases and acyltransferases as auxiliary enzymes in peroxisomal lipid metabolism

Hunt

Alexson

2008

Progress in Lipid Research

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Differential activities of peroxisomes along the mouse intestinal epithelium

Morvay

Baes

Veldhoven

2017

Cell Biochemistry & Function

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The presence of peroxisomes in mammalian intestine has been revealed formerly by catalase staining combined with electron microscopy. Despite the central role of intestine in lipid uptake and the established importance of peroxisomes in different lipid-related pathways, few data are available on the physiological role of peroxisomes in intestinal metabolism, more specifically, α-, β-oxidation, and etherlipid synthesis. Hence, the peroxisomal compartment was analyzed in more detail in mouse intestine. On the basis of immunohistochemistry, the organelles are mainly confined to the epithelial cells. The expression of the classical peroxisome marker catalase was highest in the proximal part of jejunum and decreased along the tract. PEX14 showed a similar profile, but was still substantial expressed in large intestinal epithelium. Immunoblotting of epithelial cells, isolated from the different segments, showed also such gradient for some enzymes, ie, catalase, ACOX1, and D-specific multifunctional protein 2, and for the ABCD1 transporter, being high in small and low or absent in large intestine. Other peroxisomal enzymes (PHYH, HACL1, and ACAA1), the ABCD2 and ABCD3 transporters, and peroxins PEX13 and PEX14, however, did not follow this pattern, displaying rather constant signals throughout the intestinal epithelium. The small intestine displayed the highest peroxisomal β-oxidation activity and is particularly active on dicarboxylic acids. Etherlipid synthesis was high in the large intestine, and colonic cells had the highest content of plasmalogens. Overall, these data suggest that peroxisomes exert different functions according to the intestinal segment.

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β-Oxidation in hepatocyte cultures from mice with peroxisomal gene knockouts

Cited by 41 publications

References 39 publications

Carbohydrate Metabolism Is Perturbed in Peroxisome-deficient Hepatocytes Due to Mitochondrial Dysfunction, AMP-activated Protein Kinase (AMPK) Activation, and Peroxisome Proliferator-activated Receptor γ Coactivator 1α (PGC-1α) Suppression

Carbohydrate Metabolism Is Perturbed in Peroxisome-deficient Hepatocytes Due to Mitochondrial Dysfunction, AMP-activated Protein Kinase (AMPK) Activation, and Peroxisome Proliferator-activated Receptor γ Coactivator 1α (PGC-1α) Suppression

Novel functions of acyl-CoA thioesterases and acyltransferases as auxiliary enzymes in peroxisomal lipid metabolism

Differential activities of peroxisomes along the mouse intestinal epithelium

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