Am. J. Respir. Cell Mol. Biol., Vol 10, No. 4, 04 1994, 413-418.
Surfactant protein A labeling kinetics in newborn and adult rabbits
M Ikegami, T Ueda, J Purtell, E Woods and A Jobe
Department of Pediatrics and Obstetrics and Gynecology, Harbor-UCLA Medical Center, UCLA School of Medicine, Torrance 90502.
Surfactant protein A (SP-A), the major hydrophilic protein specifically
associated with surfactant, has multiple metabolic and host defense
functions as well as primary surfactant biophysical functions in
association with the other surfactant proteins and lipids. To characterize
its kinetics of secretion and clearance from the airspace, we measured
specific activity-time curves for alveolar and lamellar body associated
SP-A following the intravascular and/or intratracheal administration of the
radiolabeled precursors Tran 35S-label containing primarily methionine and
cysteine or [3H]methionine to newborn and adult rabbits. Alveolar SP-A
specific activity peaked 30 min after precursor injection in both newborn
and adult rabbits, and labeled SP-A was not detected in lamellar bodies
until after 2 h. In newborns, a second peak of labeled SP-A appeared at 15
h. In both newborns and adult rabbits, lamellar body specific activity-time
curves were most consistent with SP-A entering lamellar bodies via a
recycling pathway from the airspaces. The airspace clearance of SP-A in
adult rabbits had a biologic half-life of about 4.5 h. There was very
little decrease in SP-A specific activity in the newborn rabbits,
indicating minimal catabolism. These studies demonstrate secretion of
endogenously synthesized SP-A by a pathway separate from lamellar bodies.
The kinetics of secretion of SP-A and the surfactant phospholipid in
newborn and adult rabbits indicate separate metabolic pathways.
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Copyright © 1994 American Thoracic Society.
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