Immunoelectron microscopy of fodrin in the rat uriniferous and collecting tubular epithelium.
Open Access
- 1 September 1989
- journal article
- research article
- Published by SAGE Publications in Journal of Histochemistry & Cytochemistry
- Vol. 37 (9) , 1345-1352
- https://doi.org/10.1177/37.9.2671151
Abstract
We examined the localization of fodrin in epithelial cells of rat uriniferous and collecting tubules by immunofluorescence and immunoelectron microscopy of frozen sections. In the uriniferous tubule, fodrin was found along the cell membrane and in the well-developed terminal web, as previously reported in other epithelial cells: in the terminal web and along the basolateral cell membrane in the proximal tubule; all around the cell surface in the thin limb of Henle; along the basolateral surface in the thick limb of Henle's thick segment and the distal tubule. In the intercalated cells of the collecting tubule, fodrin was found not only along the basolateral cell membrane but also in the apical cytoplasm. The most peculiar labeling was obtained in the principal cells of the collecting tubule. In addition to labeling in the basolateral cell membrane, fodrin was found diffusely in the cytoplasmic matrix. Association of fodrin with any particular structure could not be identified, but the Golgi area was apparently free of labeling. Cytoplasmic labeling was more conspicuous in the principal cells of the medulla than in those of the cortex. The present results show that fodrin need not always exist in association with the cell membrane or the cytoskeleton but can occur in the cytoplasmic matrix, at least in epithelial cells. We discuss the possible physiological significance of the latter distribution.This publication has 23 references indexed in Scilit:
- Redistribution of fodrin (a component of the cortical cytoplasm) accompanying capping of cell surface molecules.Proceedings of the National Academy of Sciences, 1983
- Nonerythrocyte spectrins: actin-membrane attachment proteins occurring in many cell typesThe Journal of cell biology, 1982
- Erythroid spectrin, brain fodrin, and intestinal brush border proteins (TW-260/240) are related molecules containing a common calmodulin-binding subunit bound to a variant cell type-specific subunit.Proceedings of the National Academy of Sciences, 1982
- Widespread occurrence of avian spectrin in nonerythroid cellsCell, 1982
- Stimulation of Actomyosin Mg2+-ATPase Activity by a Brain Microtubule-Associated Protein Fraction. High-Molecular-Weight Actin-Binding Protein Is the Stimulating FactorThe Journal of Biochemistry, 1981
- Fodrin: axonally transported polypeptides associated with the internal periphery of many cells.The Journal of cell biology, 1981
- Skin Calcium Binding Protein is Localized in the Cytoplasm of the Basal Layer of the EpidermisJournal of Investigative Dermatology, 1981
- Immunoelectron microscope studies of membrane-microfilament interactions: distributions of alpha-actinin, tropomyosin, and vinculin in intestinal epithelial brush border and chicken gizzard smooth muscle cells.The Journal of cell biology, 1981
- Immunochemistry on ultrathin frozen sectionsJournal of Molecular Histology, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979