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Developmental pattern of calmodulin-binding proteins in rat jejunal epithelial cells
1Unité INSERM 61, Biologie Cellulaire et Physiopathologie Digestives, Strasbourg, France.
Differentiation; Research in Biological Diversity
|January 1, 1987
Summary
Calmodulin-binding proteins, including caldesmon and fodrin, change in rat jejunal development. Their distribution shifts to the apical brush border by birth, mirroring intestinal differentiation.
Area of Science:
- Cell Biology
- Developmental Biology
- Biochemistry
Background:
- Calmodulin-binding proteins play crucial roles in cellular processes.
- Understanding their developmental expression is key to comprehending tissue maturation.
Purpose of the Study:
- To investigate the developmental expression and localization of calmodulin-binding proteins in rat jejunal epithelial cells and brush borders.
Main Methods:
- Utilized [125I]calmodulin for binding assays on nitrocellulose replicas.
- Employed antisera against caldesmon, fodrin, and a 110K microvillus protein.
- Performed immunocytochemical localization studies.
Main Results:
- Identified distinct calmodulin-binding proteins (145 kDa, 135 kDa) in early fetal stages, with additional proteins (240 kDa, 110 kDa) appearing by day 19.
- Caldesmon and fodrin were identified as the 145 kDa and 240 kDa bands, respectively.
- A 135 kDa immunoreactive polypeptide, associated with the 110K microvillus complex, was present until birth but absent in adults.
Conclusions:
- Calmodulin-binding protein composition and localization undergo significant changes during rat jejunal development.
- The expression and apical localization of caldesmon, fodrin, and a 110K protein correlate with brush border differentiation.
- These findings highlight the dynamic role of calmodulin-binding proteins in intestinal epithelial maturation.