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Reorganization of cytoskeleton and lung surfactant secretion in alveolar type II cells

Reorganization of cytoskeleton and lung surfactant secretion in alveolar type II cells

FASEB Journal 15(4): A495

ISSN/ISBN: 0892-6638

Secretion of lung surfactant requires the movement of lamellar bodies to the plasma membrane through cytoskeletal barrier at the cell cortex. We hypothesized that the cortical cytoskeleton undergoes a transient disassembly/reassembly in the stimulated type II cells. therefore allowing lamellar bodies access to the plasma membrane. Stabilization of cytoskeleton with Jasplakinolinde, a novel cell permeable actin microfilament stabilizer, caused a dose-dependent inhibition of lung surfactant secretion. Stimulation of A549 cells, a lung epithelium-derived cell, with terbutaline exhibited a transient disassembly of the F-actin as determined by the DNase I inhibition assay and staining with Oregon Green 488 Phalloidin. A similar result was also observed in primary culture of lung type II cells. Western blot analysis using anti-actin and anti-annexin II antibodies showed a transient increase of G-actin and annexin II in the soluble fraction of terbutaline-stimulated type II cells. Phorborl 12-myristate 13-acetate, an activator of protein kinase C, also decreased cortical fluorescence staining by phalloidin in type II cells. Treatment of type II cells with N-ethylmaleimide (NEM), a sulfhydryl reagent, resulted in a disruption of the cortical actin. The results suggest that cytoskeleton undergoes reorganization in the stimulated type II cells and annexin II tetramer plays a role in this process.

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Accession: 035649213

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