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Updated: Aug 8, 2026
07:51
Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Calmodulin in rat enterocyte: an immunogold electron-microscope study
S J Weinman1, J S Weinman, D P Rainteau
1Département de Biochimie, UFR Biomédicale des Saints-Pères, Université René Descartes, Paris, France.
Cell and Tissue Research
|May 1, 1994
Summary
This study reveals calmodulin
Area of Science:
- Cell Biology
- Epithelial Biology
- Protein Localization
Background:
- Calmodulin is a vital calcium-binding protein.
- Its role in enterocytes requires further ultrastructural investigation.
Purpose of the Study:
- To determine the precise location of calmodulin within rat enterocytes.
- To elucidate the function of calmodulin in enterocyte membrane dynamics.
Main Methods:
- Immunogold labeling technique was employed.
- Ultrathin sections of rat small intestine epithelium were analyzed using electron microscopy.
Main Results:
- Calmodulin predominantly localizes to the microvillous core periphery, aligning with the 110-kDa calmodulin complex.
- Trace amounts of calmodulin were observed along the basolateral membrane.
Conclusions:
- Calmodulin is crucial for regulating the mechanochemical activity of myosin I in enterocytes.
- Calmodulin's role in basolateral membrane processes appears minimal.
Related Concept Videos
01:16Calmodulin-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,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
01:20Immunogold Electron Microscopy
Immunoelectron microscopy utilizes immunogold labeling of endogenous proteins with specific antibodies to detect and localize these proteins in cells and tissues. The procedure provides insights into the distribution and quantification of protein under different stimulation conditions offering clues about their functions. Conjugating highly electron-dense gold particles with primary or secondary antibodies allow antigen detection on and within cells, with high resolution and specificity.