Abstract
Calmodulin is a ubiquitous calcium binding protein (Cheung 1980; Means and Dedman 1980), which in the adult intestinal epithelial cells has been shown to be localized preferentially at the brush border level (Howe et al. 1980; Glenney et al. 1980). In the intestinal epithelial cells, calmodulin functions mainly as a calcium buffer (Glenney and Glenney 1985), activates the actomyosin based contractility system (Mooseker et al. 1983) and interacts with a number of actin binding proteins. These proteins with both actin and calmodulin binding capacities are mainly the 110 kDa protein (Coudrier et al. 1981; Glenney and Glenney 1984; Howe and Mooseker 1983), cal-desmon (Bretscher and Lynch 1985) and fodrin (Glenney et al. 1982; Hirokawa et al. 1983). They have been extensively studied and characterized in the intestinal brush borders of avians (Glenney and Weber 1980; Mooseker 1985) but not in humans. The aim of the present chapter is to provide some current views of the human intestinal development and to attempt a correlation between the developmental pattern of calmodulin and calmodulin binding proteins, and the epithelial differentiation accompanying intestinal ontogenic maturation.
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Rochette-Egly, C., Lacroix, B., Kedinger, M., Haffen, K. (1988). Calmodulin and Calmodulin Binding Proteins During Differentiation of Human Intestinal Brush Borders. In: Gerday, C., Bolis, L., Gilles, R. (eds) Calcium and Calcium Binding Proteins. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73042-9_13
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DOI: https://doi.org/10.1007/978-3-642-73042-9_13
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