HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Yu, S.-H. Articles by Possmayer, F. Search for Related Content PubMed PubMed Citation Articles by Yu, S.-H. Articles by Possmayer, F. Social Bookmarking                      What's this?

The Journal of Lipid Research, Vol. 39, 555-568, March 1998
Copyright © 1998 by Lipid Research, Inc.

Original Article

Interaction of pulmonary surfactant protein A with dipalmitoylphosphatidylcholine and cholesterol at the air/water interface

Correspondence to: Shou-Hwa Yu.

Interaction of pulmonary surfactant protein A (SP-A) with pure and binary mixed dipalmitoylphosphatidylcholine (DPPC) and cholesterol (3.5 wt%) at the air/saline, 1.5 mM CaCl₂ interface was investigated using a rhomboid surface balance at 37°C. Surface tension–area isotherms were measured to access the surface active properties of the monolayers. The organization of DPPC and cholesterol in DPPC and DPPC/cholesterol mixed monolayers with or without SP-A at equilibrium surface tension (23 mN/N) was revealed by autoradiographs of Langmuir-Blodgett (L-B) films deposited from [¹⁴C]DPPC or [¹⁴C]cholesterol-labeled monolayers. The results showed that SP-A can interact with the polar head groups of DPPC monolayers and aggregate DPPC molecules. SP-A decreased the surface area reduction required for DPPC monolayers to achieve near zero surface tension from 30 to 25% of the area at equilibrium. SP-A also reduced the collapse surface tension of pure cholesterol from 27 to 23 mN/m. DPPC and cholesterol formed homogeneous mixed monolayers when both were dissolved in the spreading solvent prior to spreading, while separate cholesterol-rich domains appeared when DPPC and cholesterol were spread successively. Cholesterol resisted squeeze-out from either mixed monolayer through compression. Although SP-A could not promote the squeeze-out of cholesterol from homogeneous mixed monolayers, it facilitated that of cholesterol domains especially when SP-A had first interacted with DPPC.

These results indicate that pulmonary surfactant protein A facilitates the squeeze-out of cholesterol domains from mixed monolayers by condensing DPPC and limiting lateral interactions of DPPC with cholesterol domains.—Yu, S-H., and F. Possmayer. Interaction of pulmonary surfactant protein A with dipalmitoylphosphatidylcholine and cholesterol at the air/water interface. J. Lipid Res. 1998. 39: 555–568.

Supplementary key words: air/water interface, dipalmitoylphosphatidylcholine, monolayer, cholesterol, L-B film, pulmonary surfactant, surface tension, surfactant-associated protein A

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				R. Marttila, R. Haataja, S. Guttentag, and M. Hallman Surfactant Protein A and B Genetic Variants in Respiratory Distress Syndrome in Singletons and Twins Am. J. Respir. Crit. Care Med., November 15, 2003; 168(10): 1216 - 1222. [Abstract] [Full Text] [PDF]

				K. R. Capote, F. X. McCormack, and F. Possmayer Pulmonary Surfactant Protein-A (SP-A) Restores the Surface Properties of Surfactant after Oxidation by a Mechanism That Requires the Cys6 Interchain Disulfide Bond and the Phospholipid Binding Domain J. Biol. Chem., May 30, 2003; 278(23): 20461 - 20474. [Abstract] [Full Text] [PDF]

				S.-H. Yu and F. Possmayer Lipid compositional analysis of pulmonary surfactant monolayers and monolayer-associated reservoirs J. Lipid Res., March 1, 2003; 44(3): 621 - 629. [Abstract] [Full Text] [PDF]

				S.-H. Yu and F. Possmayer Dipalmitoylphosphatidylcholine and cholesterol in monolayers spread from adsorbed films of pulmonary surfactant J. Lipid Res., September 1, 2001; 42(9): 1421 - 1429. [Abstract] [Full Text] [PDF]

				O. V. Lopatko, S. Orgeig, D. Palmer, S. Schurch, and C. B. Daniels Alterations in pulmonary surfactant after rapid arousal from torpor in the marsupial Sminthopsis crassicaudata J Appl Physiol, June 1, 1999; 86(6): 1959 - 1970. [Abstract] [Full Text] [PDF]

				S.-H. Yu, F. X. McCormack, D. R. Voelker, and F. Possmayer Interactions of pulmonary surfactant protein SP-A with monolayers of dipalmitoylphosphatidylcholine and cholesterol: roles of SP-A domains J. Lipid Res., May 1, 1999; 40(5): 920 - 929. [Abstract] [Full Text]

				N. Palaniyar, R. A. Ridsdale, S. A. Hearn, Y. M. Heng, F. P. Ottensmeyer, F. Possmayer, and G. Harauz Filaments of surfactant protein A specifically interact with corrugated surfaces of phospholipid membranes Am J Physiol Lung Cell Mol Physiol, April 1, 1999; 276(4): L631 - L641. [Abstract] [Full Text] [PDF]

				N. Palaniyar, R. A. Ridsdale, S. A. Hearn, F. Possmayer, and G. Harauz Formation of membrane lattice structures and their specific interactions with surfactant protein A Am J Physiol Lung Cell Mol Physiol, April 1, 1999; 276(4): L642 - L649. [Abstract] [Full Text] [PDF]