Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis

Mitsuru Ishizuka, Yoshiro Toyama, Hiroyuki Watanabe, Yukio Fujiki, Arata Takeuchi, Sho Yamasaki, Shigeki Yuasa, Masaru Miyazaki, Nobuyuki Nakajima, Shinsuke Taki, Takashi Saito

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


The biological functions of human acyl-CoA thioesterase III (ACTEIII/PTE-1), initially identified as an HIV-1 Nef binding protein, have remained unclear. We report herein that the stable overexpression of ACTEIII/PTE-1 in human and murine T-cell lines resulted in an increase in both peroxisome number and lipid droplet formation in a manner dependent on the amount of the protein. Peroxisome proliferation was evidenced by immunofluorescence staining for catalase, a peroxisome marker protein, as well as by direct peroxisome enumeration on electron micrographs. Consistently, the amount of catalase was elevated as the amount of ACTEIII/PTE-1 was increased. ACTEIII/PTE-1 mutants with reduced enzymatic activity or with the defect in peroxisome localization did not induce peroxisome proliferation, indicating that peroxisome proliferation was mediated by metabolites generated by ACTEIII/PTE-1 within peroxisomes. Finally, thymocytes isolated from a T-cell-specific ACTEIII/PTE-1 transgenic mouse as well as human and murine cell lines of lymphoid and non-lymphoid origins exhibited a similar proliferation of peroxisomes. Thus, ACTEIII/PTE-1 may be involved in the metabolic regulation of peroxisome proliferation.

Original languageEnglish
Pages (from-to)127-141
Number of pages15
JournalExperimental Cell Research
Issue number1
Publication statusPublished - Jul 1 2004
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Cell Biology


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