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1 Department of Anesthesiology and Intensive Care Medicine, Graduate School of Medicine, Kanazawa University, Kanazawa 920-8641, Japan; and 2 Department of Ultramicrostructural Research, Institute for Frontier Medical Science, Kyoto University, Kyoto 606-8397, Japan
Surfactant protein (SP)-C
is characterized by
-helix structure and palmitoyl groups attached
to two cysteine residues. We examined the function of palmitoylation
and dimerization in promotion of tidal volume in immature newborn
rabbits. Reconstituted surfactants were made from a mixture of
synthetic phospholipids and porcine SP-B (basic mixture) by adding
various forms of SP-Cs: normal SP-C isolated from porcine lungs and
monomeric or dimeric forms of SP-C. These latter two were isolated from
patients with pulmonary alveolar proteinosis and were less
palmitoylated. Animals were ventilated at an inspiratory pressure of 25 cmH2O. Median tidal volumes were <2 ml/kg in nontreated
controls, 7.7 ml/kg in animals receiving the basic mixture without
SP-C, and >18 ml/kg in animals treated with reconstituted surfactants
containing 3% normal or 2% dimeric SP-C (P < 0.05 vs. basic mixture). The physiological effect of basic mixture was
not improved by monomeric SP-C. We conclude that palmitoyl groups are
important for the physiological effects of SP-C and that the dimeric
form also improves physiological effects.
circular dichroism; palmitoylation; pulmonary alveolar proteinosis; pulmonary surfactant; surface tension
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