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Related Experiment Videos

Insulin-induced decrease in 5'-nucleotidase activity in skeletal muscle membranes.

A Klip1, T Ramlal, A G Douen

  • 1Department of Cell Biology, Hospital for Sick Children, Toronto, Canada.

FEBS Letters
|October 10, 1988
PubMed
Summary
This summary is machine-generated.

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Insulin may release 5'-nucleotidase from muscle cell membranes. This enzyme, anchored by phospholipid-glycans, showed reduced activity after insulin exposure, suggesting insulin activates an endogenous phospholipase C.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Endocrinology

Background:

  • Insulin triggers the release of inositol phosphoglycans from cultured myocytes, which exhibit insulin-like effects.
  • 5'-nucleotidase is a membrane-bound enzyme attached via inositol-containing phospholipid glycans.

Purpose of the Study:

  • To investigate if insulin can release 5'-nucleotidase from cell membranes.
  • To explore the mechanism by which insulin affects membrane-bound enzymes.

Main Methods:

  • Preparing membranes from rat hindquarter muscles perfused with insulin.
  • Measuring 5'-nucleotidase activity in isolated muscle membranes exposed to insulin in vitro.
  • Assessing the effect of Staphylococcus aureus phospholipase C on membrane-bound 5'-nucleotidase.

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Main Results:

  • Insulin perfusion of rat hindquarter muscles led to a 23% decrease in membrane-bound 5 '-nucleotidase activity.
  • In vitro exposure of isolated muscle membranes to insulin caused a 9% reduction in 5 '-nucleotidase activity.
  • Staphylococcus aureus phospholipase C released 60% of the membrane-bound 5 '-nucleotidase, indicating its anchor mechanism.

Conclusions:

  • Insulin may induce the release of 5 '-nucleotidase from the cell membrane.
  • The findings suggest insulin activates an endogenous phospholipase C.
  • This enzyme activation likely cleaves phospholipid-glycan anchors of membrane proteins.