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Updated: Aug 8, 2026

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.
Insights
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.
Abstract:
Immunogold labeling of ultrathin sections of the epithelium of rat small intestine has been used to obtain insights into the ultrastructural localization and possible function of calmodulin in the enterocyte. Calmodulin is found mainly overlying the periphery of the microvillous core, in agreement with the location of the 110-kDa calmodulin complex. Extremely small amounts of calmodulin can be detected along the interdigitating basolateral membrane. This immunogold electron-microscope study suggests that calmodulin plays an important role in regulating the mechanochemical activity of myosin I but not in processes associated with the basolateral membrane of rat enterocyte.
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