Literature DB >> 8018340

Fodrin and actin in the normal, metaplastic, and dysplastic respiratory epithelium and in lung carcinoma.

R Sormunen1, P Pääkkö, R Palovuori, Y Soini, V P Lehto.   

Abstract

Distribution of actin and fodrin, a nonerythroid analogue of spectrin, was studied in cytocentrifuge preparations and in tissue sections of normal and pathologic respiratory epithelium by using immunofluorescence and immunoelectron microscopy. In ciliated epithelial cells and in goblet cells of normal bronchial epithelium, fodrin and actin were located in the apical parts and along the lateral walls of the cells. In basal cells, fodrin and actin were also seen diffusely in the cytoplasm. Immunoelectron microscopy showed fodrin in close association with the basal bodies and rootlets of the cilia and microvilli in the ciliated cells. In alveolar epithelium, fodrin and actin were located at the apical membrane in type I pneumocytes and along the apical and lateral membranes in type II pneumocytes. In type II pneumocytes, fodrin was also seen in close association with the secretory vacuoles. In metaplastic and dysplastic bronchial epithelium, a diffuse cytoplasmic and a circumferential, membrane-associated staining for fodrin and actin was seen. In all types of carcinomas, fodrin was seen along the lateral walls and diffusely in the cytoplasm. The staining was more intense than in the normal cells. In immunoblotting of the normal bronchial epithelium, and peripheral lung and lung carcinomas, a single 240 kD band was recognized with antibodies to fodrin. The results show distinct differences in the distribution of fodrin in the various cell types of the respiratory epithelium. In ciliated cells, the close relationship with cytoskeleton suggests a role of fodrin in the establishment of the elaborate structural architecture of the apical compartment. In type II pneumocytes, on the other hand, fodrin probably plays a role in secretion of the surfactant. In basal cells, the diffuse distribution of fodrin probably reflects the high proliferative capacity of this cell compartment. Interestingly, a similar distribution was also seen in premalignant and malignant cells.

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Year:  1994        PMID: 8018340     DOI: 10.1165/ajrcmb.11.1.8018340

Source DB:  PubMed          Journal:  Am J Respir Cell Mol Biol        ISSN: 1044-1549            Impact factor:   6.914


  6 in total

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Review 4.  The Role of Nonerythroid Spectrin αII in Cancer.

Authors:  Anne Ackermann; Angela Brieger
Journal:  J Oncol       Date:  2019-05-02       Impact factor: 4.375

5.  α-Fodrin in Cytoskeletal Organization and the Activity of Certain Key Microtubule Kinesins.

Authors:  Jamuna S Sreeja; Athira Jyothy; Suparna Sengupta
Journal:  Genes (Basel)       Date:  2021-05-17       Impact factor: 4.096

6.  An SH3 binding region in the epithelial Na+ channel (alpha rENaC) mediates its localization at the apical membrane.

Authors:  D Rotin; D Bar-Sagi; H O'Brodovich; J Merilainen; V P Lehto; C M Canessa; B C Rossier; G P Downey
Journal:  EMBO J       Date:  1994-10-03       Impact factor: 11.598

  6 in total

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