Previously, we identified a peroxisome-specific isoform of Lon protease using subcellular proteomics. In the present study, we investigated changes in the level of the Lon protease in peroxisomes during recovery from peroxisomal proliferation induced by di-(2-ethylhexyl)phthalate (DEHP) to elucidate the function of peroxisomal Lon protease (PSLP). Following a 2-week treatment with DEHP, the level of PSLP was monitored for 15 days. The amount of protease was greatly increased after the 2-week treatment, followed by a further increase 3 days after cessation of the treatment. Afterward, it decreased and reached the control level on day 15. On the other hand, level peroxisomal beta-oxidation enzymes induced to express by DEHP started to decrease soon after discontinuation of treatment. The results suggest that PSLP functions to degrade beta-oxidation enzymes induced by DEHP during recovery from perxisomal proliferation.
Induction of peroxisomal Lon protease in rat liver after di-(2-ethylhexyl)phthalate treatment. Publishing Authors By Initials
Induction of peroxisomal Lon protease in rat liver after di-(2-ethylhexyl)phthalate treatment. Journal Published:
PUBLICATION TYPE: Journal Article
Journal: Histochemistry and cell biology
VOLUME: 129
Page Numbers: 73-83
Journal Abbreviation: Histochem. Cell Biol.
ISSN: 0948-6143
DAY: 11
MONTH: 10
YEAR: 2007
Induction of peroxisomal Lon protease in rat liver after di-(2-ethylhexyl)phthalate treatment. Information
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LANGUAGE: eng
NlmUniqueID: 9506663
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Grant and Affiliation Information for Induction of peroxisomal Lon protease in rat liver after di-(2-ethylhexyl)phthalate treatment.
AFFILIATION: Department of Functional Morphology, Faculty of Pharmaceutical Science, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo, Nagasaki, 859-3298, Japan, syokota@niu.ac.jp.
Country: Germany
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MEDLINETA: Histochem Cell Biol
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