Recent electron studies with special refernce to respiratory cilia.
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Efficient cleansing of the upper and lower respiratory surfaces by the mucociliary apparatus is essential to health. Failure of the cleansing allows contaminants prolonged residence on the mucosal respiratory surfaces and thus penetration into the mucosa and possibly inauguration of disease. For some years, genetic ultrastructural ciliary alterations have been recognized, with symptoms dating from early life. It is only in recent years, however, that evidence has shown that ultrastructural ciliary alterations can be acquired later in life and that these alterations in turn lead to a deterioration of efficient ciliary cleansing. A discussion of the ultrastructure of the normal mammalian cilium will be given, as well as a listing of the genetic ciliary disease and their characteristic morphologic alterations. A more complete review will be made in regard to acquired ciliary defects, their cause, the ultrastructural changes, and the relation to clinical disease.
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Paramecium bursaria is photosensitive and accumulates in a lighted area. The cells can be deciliated by a brief suspension in dilute ethanol. Both intact and deciliated cells showed depolarization in response to light stimulation by a step-increase from dark to above 0.7 mW cm-2 (550 nm). On the other hand, after a step-increase to below 0.4 mW cm-1, intact cells showed hyperpolarization, while the deciliated cells showed no change in membrane potential. This difference in membrane potential response between ciliated and deciliated cells suggests that both somatic and ciliary structures are photosensitive. In our search for the photoreceptive molecules, a polyclonal antibody induced in rabbits against frog rhodopsin was found to cross-react with a 63x10(3) Mr protein of P. bursaria, by immunoelectrophoresis. Immunocytochemical studies showed that the antibody labeling was localized on both the ciliary and the somatic membranes. These results raise the possibility that P. bursaria may contain a rhodopsin-like protein as a photoreceptor molecule.
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