Springer Online Journal Archives 1860-2000
Abstract Mammalian taste buds consist of 50–150 pear- or spindle-shaped taste receptor cells which contain, at their apical cell surface, a bundle of microvillar projections. The microvilli probably serve to increase the receptive membrane surface of the chemosensory receptor cells. The molecular basis controlling the ultrastructure of taste receptor microvilli is present unknown. In the present study we analysed, by immunostaining at the light and electron microscopic levels and by immunoblotting, components of the cytoskeleton of these microvilli. We show here that taste cell microvilli contain the major cytoskeletal proteins of intestinal microvilli, actin, fimbrin and villin. Another actin-binding, peripheral membrane protein of intestinal microvilli, ezrin, was also localised to taste cell microvilli, where ezrin might play a role, for example, in placement of specific membrane proteins to the microvillus membrane. In search of further linkage proteins, we found ankyrin localised along the basolateral cell surface of taste receptor cells, where ankyrin might be involved in the immobilisation of the Na+, K+-ATPase or other ion-translocating proteins of taste cells to the membrane cytoskeleton.
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