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Decrease in cytoskeleton-bound phosphofructokinase in muscle induced by high intracellular calcium, serotonin and

G Lilling1, R Beitner

  • 1Department of Life Sciences, Bar-Ilan University, Ramat-Gan, Israel.

The International Journal of Biochemistry
|January 1, 1990
PubMed
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Bound phosphofructokinase (PFK) in muscle is not allosterically regulated. Increased intracellular calcium reduces PFK and aldolase binding to cytoskeletal proteins, potentially damaging muscle.

Area of Science:

  • Muscle physiology
  • Biochemistry
  • Cell biology

Background:

  • Phosphofructokinase (PFK) is a key glycolytic enzyme.
  • Enzyme binding to the cytoskeleton influences cellular function.
  • Allosteric regulation controls enzyme activity.

Purpose of the Study:

  • To investigate the properties of particulate (cytoskeleton-bound) and soluble PFK.
  • To determine the effect of agents that increase intracellular calcium on enzyme binding.
  • To explore the role of calcium in muscle damage.

Main Methods:

  • Separation of particulate and soluble PFK from rat muscle.
  • Treatment of muscle with Ca2(+)-ionophore A23187, serotonin, and phospholipase A2.
  • Direct addition of Ca2+ to muscle particulate fractions.

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Main Results:

  • Particulate PFK showed different allosteric properties compared to soluble PFK; bound PFK was not allosterically regulated.
  • Agents increasing intracellular calcium (A23187, serotonin, phospholipase A2) reduced PFK and aldolase binding.
  • Direct addition of Ca2+ to muscle particulate fractions solubilized bound PFK and aldolase.

Conclusions:

  • PFK binding to cytoskeletal proteins is sensitive to intracellular calcium levels.
  • Reduced enzyme binding due to calcium may impair muscle function and structure.
  • Calcium-mediated changes in enzyme binding could contribute to muscle damage in pathological conditions.