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Lectin activity of the major surfactant protein (SP-A) may participate in, but is not required for, binding to rat type II cells
T Thorkelsson, GM Ciraolo, GF Ross, JA Whitsett and RE Morris
Department of Pediatrics, University of Cincinnati College of Medicine, Ohio 45267.
Pulmonary surfactant is a complex mixture of lipids and proteins, of which surfactant protein A (SP-A) is the most abundant glycoprotein. The SP-A molecule has several distinct structural features that include a lectin-like domain, sharing structural features with other mammalian lectins. We have tested the hypothesis that lectin activity of the SP-A molecule is required for the binding to its receptor on the surface of alveolar Type II cells. By using colloidal gold immunocytochemistry in conjunction with electron microscopy, we evaluated the ability of mannosylated proteins to inhibit canine SP-A binding to rat Type II cells in vitro. After preincubation of SP-A with the mannosylated protein horse-radish peroxidase (HRP), SP-A was incubated with isolated filter-grown Type II cells. HRP did not alter the binding of SP-A to the Type II cell surface. Evidence that SP-A did bind to HRP was shown by coincident observation of gold-labeled SP-A and HRP precipitates. These results provide visual evidence that the lectin activity associated with SP-A is not required for its binding to receptor on rat alveolar Type II epithelial cells.
Volume 40,
Issue 5,
pp. 643-649,
05/01/1992
Copyright © 1992 by The Histochemical Society
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  Z. C. Chroneos, R. Abdolrasulnia, J. A. Whitsett, W. R. Rice, and V. L. Shepherd Purification of a Cell-surface Receptor for Surfactant Protein A J. Biol. Chem., July 5, 1996; 271(27): 16375 - 16383. [Abstract] [Full Text] [PDF]
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