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Major ATPases on clofibrate-induced rat liver peroxisomes are not associated with 70 kDa peroxisomal membrane protein

S Shimizu1, T Imanaka, T Takano

  • 1Department of Biochemistry, Faculty of Pharmaceutical Sciences, Kanazawa University.

Journal of Biochemistry
|December 1, 1992
PubMed

Insights

Novel Mg(2+)-ATPases in rat liver peroxisomes, induced by clofibrate, are not the 70-kDa peroxisomal membrane protein (PMP70). Further characterization distinguishes these enzymes from PMP70.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Novel Mg(2+)-ATPases are induced in rat liver peroxisomes by clofibrate.
  • These activities comprise N-ethylmaleimide (NEM)-sensitive and -resistant enzymes.

Purpose of the Study:

  • To determine if the major peroxisomal ATPases are associated with the 70-kDa peroxisomal membrane protein (PMP70).

Main Methods:

  • Differential proteinase K treatment of peroxisomes.
  • Immunoprecipitation assays using anti-PMP70 IgG.
  • Native polyacrylamide gel electrophoresis (PAGE) of solubilized ATPases.
  • Gel filtration chromatography to separate ATPases and PMP70.

Main Results:

  • Proteinase K inactivated NEM-sensitive ATPase but completely degraded PMP70.
  • NEM-sensitive ATPase showed minimal immunoprecipitation with anti-PMP70 IgG.
  • Solubilized ATPases exhibited different migration patterns from PMP70 on native PAGE.
  • Gel filtration chromatography separated the major peroxisomal ATPases from PMP70.

Conclusions:

  • The major peroxisomal Mg(2+)-ATPases are distinct entities from PMP70.
  • These findings clarify the molecular identity of peroxisomal ATPases involved in clofibrate-induced responses.

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