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Volume 270, Number 27, Issue of July 07, pp. 16225-16229, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Lambert A. J. M. Creuwels , Esther H. Boer , Rudy A. Demel , Lambert M. G. van Golde , Henk P. Haagsman

Pulmonary surfactant protein C (SP-C) is a small, extremely hydrophobic peptide with a highly conservative primary structure. The protein is characterized by two adjacent palmitoylated cysteine residues, two positively charged residues (one arginine residue and one lysine residue) in the N-terminal region, and a long hydrophobic stretch. SP-C enhances the adsorption of phospholipids into an air-water interface. To determine the importance of the positively charged residues, we carried out experiments with natural porcine SP-C and modified porcine SP-C (SP-C) in which the positive charges had been blocked by phenylglyoxal. Circular dichroism experiments showed that SP-C had an increased content of -helix. Natural SP-C, but not SP-C, catalyzed insertion of phospholipids into a monolayer at the air-water interface. This reduced insertion was due to a strong reduction of binding of phospholipid vesicles to the monolayer. The insertion catalyzed by the natural porcine SP-C was decreased by an increased pH of the subphase. In contrast to natural SP-C, SP-C induced lipid mixing between phospholipid vesicles. The extent of lipid mixing was a function of the SP-C content. We conclude that the positively charged residues of SP-C are important for the binding of phospholipid vesicles to the monolayer, a process that precedes the insertion of phospholipids into the monolayer.

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				Z. Wang, O. Gurel, J. E. Baatz, and R. H. Notter Acylation of Pulmonary Surfactant Protein-C Is Required for Its Optimal Surface Active Interactions with Phospholipids J. Biol. Chem., August 9, 1996; 271(32): 19104 - 19109. [Abstract] [Full Text] [PDF]