Abstract
Interaction of extracellular lung surfactant-specific protein SP-A with type II pneumocytes is involvod in modulating alveolar surfactant metabolism. SP-A enhances uptake and subsequent recycling of surfactant towards lamellar bodies, the secretory organelles of the type II cells. It is also involved in regulating surfactant secretion by these cells.
The nature of the type II cell component(s) interacting with SP-A has been unclear. After immunizing mice with SP-A we developed a panel of anti-SP-A antibodies as well as two monoclonal antibodies (mAbs) against type II pneumocyte cell membrane components (but not SP-A). In vitro immunization with these mAbs produced anti-SP-A antibodies, demonstrating the auto-antiidiotypic nature of the mAbs.
With the use of these mAbs we identified a specific SP-A-binding protein (MW 180-210,000) on type II pneumocyte cell membranes. As shown by 1- and 2-D gel electrophoresis, this protein consists of subunits, MW 55,000. (Biochemical characterization of the protein and its subunits will be presented.) Our results indicate lhat this protein may be involved in surfactant metabolism regulation. Supported by DFG Grant Ste 459/1-1 and BMFT Proiect “Risikoneugeborcnes”
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Steven, P., Meienreis-Sudau, V. & Rustow, B. CHARACTERIZATION OF A SP-A-BINDING PRRTEIN AT THE CELL MEMBRANE OF TYPE 11 PNEUMOCYTES WITH THE USE OF AUTO-ANTIDIOTYPIC ANTIBODIES. Pediatr Res 35, 278 (1994). https://doi.org/10.1203/00006450-199402000-00145
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DOI: https://doi.org/10.1203/00006450-199402000-00145
