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Protons induce calsequestrin conformational changes

C Hidalgo1, P Donoso, P H Rodriguez

  • 1Departamento de Fisiología y Biofísica, Facultad de Medicina, Universidad de Chile, Santiago. ch@cecs.cl

Biophysical Journal
|October 1, 1996
PubMed
Summary
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pH significantly impacts calsequestrin's calcium binding. Lowering pH reduces calcium-induced fluorescence and heat changes, suggesting proton binding alters protein structure.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Calsequestrin is a key calcium-binding protein in the sarcoplasmic reticulum lumen.
  • It exhibits calcium-induced conformational changes and intrinsic fluorescence variations at neutral pH.

Purpose of the Study:

  • To investigate the effect of pH on calcium-induced conformational changes in calsequestrin.
  • To determine how pH influences calsequestrin's intrinsic fluorescence and calorimetric responses to calcium.

Main Methods:

  • Spectrofluorometry was used to measure intrinsic fluorescence changes.
  • Microcalorimetry was employed to assess heat production upon calcium addition.
  • Experiments were conducted across a range of pH values (e.g., pH 8.0 to 6.0) and ionic strengths.

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Main Results:

  • Calcium addition at neutral pH caused a cooperative increase in calsequestrin fluorescence.
  • At pH 6.0, calcium failed to induce significant fluorescence changes.
  • Both fluorescence and calorimetric responses to calcium diminished with decreasing pH and increasing potassium or proton concentrations.

Conclusions:

  • pH significantly modulates calsequestrin's response to calcium binding.
  • Proton binding to calsequestrin induces conformational changes affecting its structure and function.
  • These findings highlight the critical role of pH in regulating sarcoplasmic reticulum calcium dynamics.