Skip to main content
Log in

Immunocytochemical demonstration of caldesmon (a calmodulin-binding, F-actin-interacting protein) in smooth muscle fibers and absorptive epithelial cells in the small intestine of the rat

  • Short Communication
  • Published:
Cell and Tissue Research Aims and scope Submit manuscript

Summary

The distribution of caldesmon (a calmodulin-binding, F-actin-interacting protein) (Sobue et al. 1982) and of actin was studied in the rat's small intestine by means of light-microscopic immunocytochemistry. Positive immunostaining for caldesmon was seen in smooth muscle cells of the intestinal wall, and of blood vessels, and in the apical portion of the absorptive epithelial cells. The immunoreactivity in goblet cells was difficult to recognize. The positive reaction to immunostaining for actin showed almost the same pattern as that for caldesmon. These results suggest that this calmodulin-binding protein may play an important role in the control of actin-myosin interaction in smooth muscle cells and in non-muscle cells.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

References

  • Howe CL, Mooseker MS, Graves TA (1980) Brush-border calmodulin: a major component of the isolated microvillous core. J Cell Biol 85:916–923

    Google Scholar 

  • Kakiuchi R, Inui M, Morimoto K, Kanda K, Sobue K, Kakiuchi S (1983) Caldesmon, a calmodulin-binding, F actin-interacting protein, is present in aorta, uterus and platelets. FEBS Lett 154:351–356

    Google Scholar 

  • Kakiuchi S, Sobue K (1983) Control of the cytoskeleton by calmodulin and calmodulin-binding proteins. Trends Biochem Sci 8:59–62

    Google Scholar 

  • McLean IW, Nakane PK (1974) Periodate-lysine-paraformaldehyde fixative: a new fixative for immunoelectron microscopy. J Histochem Cytochem 22:1077–1083

    CAS  PubMed  Google Scholar 

  • Mooseker MS, Tilney LG (1975) Organization of an actin filament-membrane complex. Filament polarity and membrane attachment in the microvilli of intestinal epithelial cells. J Cell Biol 67:725–743

    Google Scholar 

  • Sobue K, Muramoto Y, Fujita M, Kakiuchi S (1981) Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc Natl Acad Sci USA 78:5652–5655

    Google Scholar 

  • Sobue K, Morimoto K, Kanda K, Maruyama K, Kakiuchi S (1982a) Reconstitution of Ca2+-sensitive gelation of actin filaments with filamin, caldesmon and calmodulin. FEBS Lett 138:289–292

    Google Scholar 

  • Sobue K, Morimoto K, Inui M, Kanda K, Kakiuchi S (1982b) Control of actin-myosin interaction of gizzard smooth muscle by calmodulin- and caldesmon-linked flip-flop mechanism. Biomed Res 3:188–196

    Google Scholar 

  • Sternberger LA, Hardy PH Jr, Cuculis JJ, Meyer HG (1970) The unlabeled antibody enzyme method of immunohistochemistry: preparation and properties of soluble antigen-antibody complex (horseradish peroxidase-anti-horseradish peroxidase) and its use in identification of spirochetes. J Histochem Cytochem 18:315–333

    Google Scholar 

  • Zamboni L, DeMartino C (1967) Buffered picric-acid formaldehyde: a new rapid fixation for electron microscopy. J Cell Biol 35:148A

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

This study was supported by grants (No. 56370002, 57480092, 58770019) from the Ministry of Education, Science and Culture

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ishimura, K., Fujita, H., Ban, T. et al. Immunocytochemical demonstration of caldesmon (a calmodulin-binding, F-actin-interacting protein) in smooth muscle fibers and absorptive epithelial cells in the small intestine of the rat. Cell Tissue Res. 235, 207–209 (1984). https://doi.org/10.1007/BF00213742

Download citation

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00213742

Key words

Navigation