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Related Experiment Videos

Histone II-A activates the glucose-6-phosphatase system without microsomal membrane permeabilization

B A Pederson1, J D Foster, R C Nordlie

  • 1Department of Biochemistry and Molecular Biology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, North Dakota 58202, USA.

Archives of Biochemistry and Biophysics
|August 29, 1998
PubMed
Summary

Histone II-A activates the glucose-6-phosphatase (Glc-6-Pase) system without permeabilizing microsomal membranes, unlike alamethicin. This study clarifies the distinct mechanisms by which these agents modulate Glc-6-Pase activity.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Membrane Biology

Background:

  • The glucose-6-phosphatase (Glc-6-Pase) system's latent activity is modulated by various agents.
  • Detergents and alamethicin activate Glc-6-Pase by disrupting microsomal membranes.
  • Histone II-A also activates Glc-6-Pase, but its mechanism of action is debated.

Purpose of the Study:

  • To investigate whether histone II-A activates the Glc-6-Pase system through microsomal membrane permeabilization.
  • To compare the mechanisms of activation by histone II-A, alamethicin, and Triton X-100.

Main Methods:

  • Treatment of rat liver microsomes with Triton X-100, alamethicin, or histone II-A.
  • Assessment of Glc-6-Pase system activation.
  • Evaluation of the effects of alamethicin and histone II-A on inhibition by thiol-directed reagents (N-bromoacetylethanolamine phosphate and 3-mercaptopicolinate).

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Main Results:

  • Triton X-100, alamethicin, and histone II-A equally activated the Glc-6-Pase system.
  • Alamethicin abolished the inhibitory effects of thiol-directed reagents, indicating membrane permeabilization.
  • Histone II-A did not abolish the inhibitory effects of thiol-directed reagents, suggesting activation without membrane permeabilization.

Conclusions:

  • Histone II-A activates the Glc-6-Pase system without altering microsomal membrane integrity.
  • Alamethicin activates Glc-6-Pase by permeabilizing microsomal membranes, consistent with previous findings.
  • The study elucidates distinct mechanisms for Glc-6-Pase activation by different agents.