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Related Experiment Videos

High-affinity Ca2+-binding site inhibiting Ca2+ release from sarcoplasmic reticulum.

A Argaman1, V Shoshan-Barmatz

  • 1Department of Biology, Ben Gurion University of the Negev, Beer Sheva, Israel.

FEBS Letters
|January 16, 1989
PubMed
Summary

Alkaline pH triggers calcium-2+ release from sarcoplasmic reticulum, but this release is inhibited by low calcium-2+ concentrations. High-affinity calcium-2+ binding sites likely regulate this process.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Physiology

Background:

  • Sarcoplasmic reticulum (SR) is crucial for calcium-2+ (Ca2+) homeostasis in muscle cells.
  • Alkaline pH is known to activate Ca2+ release from SR membranes.

Purpose of the Study:

  • To investigate the role of Ca2+ concentration in modulating alkaline pH-activated Ca2+ release from SR.
  • To identify potential regulatory mechanisms controlling Ca2+ release.

Main Methods:

  • Experiments were conducted using isolated sarcoplasmic reticulum membranes.
  • Calcium-2+ release was activated by alkaline pH and modulated by varying Ca2+ concentrations, using EGTA or CDTA for buffering.
  • The effects of other divalent cations were also assessed.

Main Results:

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  • Alkaline pH-induced Ca2+ release from SR membranes was observed only when EGTA was present.
  • Low concentrations of Ca2+ (5-20 nM) inhibited Ca2+ release, irrespective of the buffering agent (EGTA or CDTA).
  • Other divalent cations (Mn2+, Ba2+, Cu2+, Cd2+, Mg2+) also inhibited release with varying potencies, and the Ca2+-mediated inhibition was reversible.

Conclusions:

  • Ca2+ release activated by alkaline pH is subject to inhibition by free Ca2+ at nanomolar concentrations.
  • The findings suggest the involvement of high-affinity Ca2+-binding sites in the regulation of Ca2+ release from SR.
  • These regulatory sites may play a significant role in controlling intracellular Ca2+ levels during muscle function.