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Binding and uptake of pulmonary surfactant protein (SP-A) by pulmonary type II epithelial cells

RM Ryan, RE Morris, WR Rice, G Ciraolo and JA Whitsett

University of Cincinnati College of Medicine, Department of Pediatrics, Ohio 45267-0541.

A glycoprotein of Mr 26-36,000 (SP-A) is an abundant phospholipid- associated protein in pulmonary surfactant. SP-A enhances phospholipid reuptake and inhibits secretion by Type II epithelial cells in vitro. We have used two electron microscopic cytochemical methods to demonstrate selective binding and uptake of SP-A by rat pulmonary Type II epithelial cells. Using an immunogold bridging technique, we showed that SP-A binding was selective for Type II cell surfaces. Binding was dose dependent and saturable, reaching maximal binding at approximately 10 ng/ml. On warming to 23 degrees C, SP-A binding sites were clustered in coated pits on the cell surface. To characterize the internalization and intracellular routing of SP-A, we used the biotinyl ligand-avidin- gold technique. Biotinyl SP-A was bound by rat Type II epithelial cells as described above. On warming, biotinyl SP-A was seen in association with coated vesicles and was subsequently located in endosomes and multivesicular bodies. Biotinyl SP-A-gold complexes were seen in close approximation to lamellar bodies 10-60 min after warming. Binding of biotinyl SP-A was inhibited by competition with unlabeled SP-A. These results support the concept that Type II epithelial cells bind and internalize SP-A by receptor-mediated endocytosis. This newly described uptake system may play a role in the recycling of surfactant components or mediate the actions of SP-A on surfactant phospholipid secretion.

Volume 37, Issue 4, pp. 429-440, 04/01/1989
Copyright © 1989 by The Histochemical Society


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The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 1989