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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
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.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...

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Related Experiment Video

Updated: Jun 25, 2026

Imaging Local Ca2+ Signals in Cultured Mammalian Cells
09:30

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Published on: March 3, 2015

Indo-1 derivatives for local calcium sensing.

Michael Bannwarth1, Ivan R Correa, Monika Sztretye

  • 1Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH-1015, Lausanne, Switzerland.

ACS Chemical Biology
|February 6, 2009
PubMed
Summary

Researchers developed a new method to measure calcium (Ca2+) concentrations in specific cell locations using SNAP-tag fusion proteins and Indo-1 dye. This technique offers improved spatial and temporal resolution for studying cellular signaling.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Imaging

Background:

  • Precise spatial and temporal control of calcium (Ca2+) concentration is crucial for cellular signal transduction.
  • Current methods for detecting Ca2+ fluctuations lack adequate temporal and spatial resolution.
  • Limitations in existing Ca2+ detection technologies hinder a comprehensive understanding of cellular processes.

Purpose of the Study:

  • To introduce a novel method for measuring Ca2+ concentrations in defined intracellular locations.
  • To combine the spatial specificity of genetically encoded indicators with the spectroscopic advantages of synthetic dyes.
  • To develop a tool for high-resolution monitoring of calcium dynamics in living cells.

Main Methods:

  • Linking the Ca2+-sensitive dye Indo-1 to SNAP-tag fusion proteins to create SNAP-Indo-1 conjugates.
  • Utilizing fluorescence spectroscopy to confirm the Ca2+-sensing ability of the conjugates in vitro.
  • Applying confocal microscopy with shifted excitation and emission ratioing for in-cell Ca2+ measurements in SNAP-tag expressing cells.

Main Results:

  • SNAP-Indo-1 conjugates retained the Ca2+-sensing capabilities of the original Indo-1 dye.
  • Proof-of-principle experiment successfully demonstrated local Ca2+ sensing within the nuclei of mouse muscle cells.
  • Nuclear Ca2+ changes were detected and preliminarily calibrated in response to external solution modifications.

Conclusions:

  • The developed SNAP-tag-based Ca2+ indicators effectively combine spatial targeting with robust spectroscopic properties.
  • This novel technique provides a powerful tool for precise measurement of intracellular Ca2+ concentrations.
  • The method advances the study of calcium signaling pathways with enhanced spatial and temporal resolution.