Surfactant protein A modulates release of reactive oxygen species from alveolar macrophages

S Weissbach, A Neuendank… - … of Physiology-Lung …, 1994 - journals.physiology.org
S Weissbach, A Neuendank, M Pettersson, T Schaberg, U Pison
American Journal of Physiology-Lung Cellular and Molecular …, 1994journals.physiology.org
The production and release of reactive oxygen species (the respiratory burst) is a common
metabolic pathway linked to several macrophage-related reactions. The most abundant
surfactant protein A (SP-A) binds to alveolar macrophages (AM) through a specific surface
receptor with high affinity. Because such binding might initiate or modulate the respiratory
burst, we wanted to know whether and how SP-A affects the oxygen radical release from
AM. To answer these questions, we measured the release of reactive oxygen species from …
The production and release of reactive oxygen species (the respiratory burst) is a common metabolic pathway linked to several macrophage-related reactions. The most abundant surfactant protein A (SP-A) binds to alveolar macrophages (AM) through a specific surface receptor with high affinity. Because such binding might initiate or modulate the respiratory burst, we wanted to know whether and how SP-A affects the oxygen radical release from AM. To answer these questions, we measured the release of reactive oxygen species from rat AM under various in vitro conditions using enhanced chemiluminescence systems. We prepared SP-A from pulmonary surfactant isolated either from silica-treated rats or adult dogs. Resident AM were harvested from pathogen-free Wistar rats by lung lavage. Adhered and nonadhered AM were assessed on protein-free or protein-coated surfaces of 96-well microtiter plates. On protein-free surfaces, the sole addition of SP-A failed to induce measurable oxygen radical release from 2 x 10(5) adhered or nonadhered AM, while zymosan opsonized with SP-A induced a marked increase over control. On protein-coated surfaces, AM respond differently depending on the coated protein: on SP-A-coated surfaces, a dose-dependent enhancement of oxygen radical release with a mean effective concentration of approximately 1.15 micrograms/ml was found. No such enhancement was seen on plates coated with similar amounts of either human fibronectin or collagen, and the enhancement with serum albumin was not dose related. Our data demonstrate that SP-A only enhances oxygen radical release from AM if SP-A is fixed to zymosan or the surface of the reaction vial in vitro.(ABSTRACT TRUNCATED AT 250 WORDS)
American Physiological Society