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Related Experiment Videos

Changes in the glucose-6-phosphatase complex in hepatomas

Q Xiao1, I Jaspers, E Matthew

  • 1Department of Biochemistry and Molecular Biology, University of Medicine and Dentistry of New Jersey-New Jersey Medical School, Newark 07103.

Molecular and Cellular Biochemistry
|May 12, 1993
PubMed
Summary

Morris hepatomas exhibit reduced glucose-6-phosphatase activity, affecting both translocase and hydrolase functions. This impairment is observed in microsomal preparations and is influenced by histone interactions.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Hepatomas often display altered glucose metabolism.
  • Glucose-6-phosphatase (G6Pase) activity is typically decreased in hepatomas.
  • The specific impact on G6Pase translocase and hydrolase functions remains unclear.

Purpose of the Study:

  • To investigate whether the decreased G6Pase activity in hepatomas affects its translocase or hydrolase functions.
  • To compare G6Pase activity in liver and hepatoma microsomes using different substrates and histone treatments.

Main Methods:

  • Compared G6Pase and mannose-6-phosphatase (M6Pase) activities in rat hepatoma and liver microsomes.
  • Utilized glucose-6-phosphate and mannose-6-phosphate as substrates.
  • Assessed the effect of histone pre-incubation on microsomal enzyme activities.

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Main Results:

  • Five out of seven hepatoma lines showed lower microsomal M6Pase activity compared to normal or tumor-bearing rat liver.
  • Histone pre-incubation significantly increased M6Pase activity more than G6Pase activity in both liver and hepatoma microsomes.
  • Arginine-rich histones and polylysine showed greater activation than lysine-rich histones or protamine.

Conclusions:

  • Rat hepatoma microsomes exhibit decreased translocase and hydrolase functions of G6Pase.
  • Histone interactions modulate G6Pase and M6Pase activities, with differential effects observed.