| http://purl.uniprot.org/citations/32335291 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32335291 | http://www.w3.org/2000/01/rdf-schema#comment | "Although obesity contributes to the onset and pathogenesis of metabolic diseases, it has been repeatedly demonstrated that being overweight or mildly obese carries a survival advantage compared with being thin or normal-weight. This relationship is called the obesity paradox. Hence, it is necessary to clarify the underlying mechanism of obesity onset for the prevention and treatment of these diseases. Catalase is distributed in peroxisomes under normal redox conditions and catalase activity is increased during the differentiation of 3T3-L1 preadipocytes to adipocytes. Although peroxisomes are responsible for lipid metabolism, the role of peroxisomal catalase in the process of lipid accumulation remains unclear. The present study aimed to investigate the relationships among catalase activity, peroxisome content, and lipid accumulation during the differentiation of 3T3-L1 preadipocytes to adipocytes. Increased catalase activity and lipid accumulation were observed during the differentiation of preadipocytes. Silencing of catalase by small interfering RNA or treatment with 3-amino-1,2,4-triazole (3-AT), a catalase inhibitor, resulted in reduced lipid accumulation. Inhibition of catalase activity in peroxisomes increases hydrogen peroxide (H2O2) levels, which results in a reduction of peroxisome content. Extracellular H2O2 had no influence on lipid accumulation during differentiation. The occurrence of autophagy was clearly enhanced in cells treated with 3-AT. Spautin-1, an inhibitor of autophagy flux, protected against a reduction in lipid accumulation by treatment with 3-AT. Our data provide evidence that catalase protects against the degradation of peroxisomes via the occurrence of autophagy triggered by the generation of H2O2 in peroxisomes. These results suggest that catalase in peroxisomes is crucial to adipogenesis."xsd:string |
| http://purl.uniprot.org/citations/32335291 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbalip.2020.158726"xsd:string |
| http://purl.uniprot.org/citations/32335291 | http://purl.uniprot.org/core/author | "Sakurai K."xsd:string |
| http://purl.uniprot.org/citations/32335291 | http://purl.uniprot.org/core/author | "Nitta Y."xsd:string |
| http://purl.uniprot.org/citations/32335291 | http://purl.uniprot.org/core/author | "Muraoka-Hirayama S."xsd:string |
| http://purl.uniprot.org/citations/32335291 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32335291 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta Mol Cell Biol Lipids"xsd:string |
| http://purl.uniprot.org/citations/32335291 | http://purl.uniprot.org/core/pages | "158726"xsd:string |
| http://purl.uniprot.org/citations/32335291 | http://purl.uniprot.org/core/title | "Catalase is required for peroxisome maintenance during adipogenesis."xsd:string |
| http://purl.uniprot.org/citations/32335291 | http://purl.uniprot.org/core/volume | "1865"xsd:string |
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