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Related Concept Videos

Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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ATP Driven Pumps II: P-type Pumps01:34

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Calcium occlusion in plasma membrane Ca2+-ATPase.

Mariela S Ferreira-Gomes1, Rodolfo M González-Lebrero, María C de la Fuente

  • 1Instituto de Química y Fisicoquímica Biologicas, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas, Junín 956, 1113 Buenos Aires, Argentina.

The Journal of Biological Chemistry
|July 29, 2011
PubMed
Summary

Researchers identified a key calcium-bound state in the plasma membrane calcium ATPase (PMCA) pump. This finding reveals how the PMCA enzyme facilitates calcium transport across cell membranes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Physiology

Background:

  • The plasma membrane Ca(2+)-ATPase (PMCA) is crucial for maintaining intracellular calcium homeostasis.
  • Understanding the intermediate states of PMCA is essential for elucidating its transport mechanism.

Purpose of the Study:

  • To identify and characterize calcium-occluded intermediates of PMCA.
  • To investigate the mechanism of calcium transport by PMCA.

Main Methods:

  • Developed a novel procedure for measuring Ca(2+) occlusion in PMCA-containing microsomes.
  • Utilized enzyme overexpression, rapid mixing, and filtration techniques for enzyme isolation and calcium quantification.
  • Analyzed enzyme phosphorylation and retained calcium kinetics in the presence of La(III).

Main Results:

  • Established a hyperbolic dependence of retained Ca(2+) on Ca(2+) concentration with an apparent dissociation constant of 12 ± 2.2 μM.
  • Observed similar apparent rate constants for enzyme phosphorylation and retained calcium accumulation.
  • Determined a stoichiometry of one mole of occluded calcium per mole of phosphoenzyme (EP).

Conclusions:

  • Demonstrated that one calcium ion is occluded in the E(1)P-phosphorylated intermediate of PMCA.
  • Provided the first direct evidence for a calcium-occluded intermediate in the PMCA transport cycle.
  • Offered new insights into the molecular mechanism of calcium transport by PMCA.