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Originally published In Press as doi:10.1074/jbc.M204669200 on May 14, 2002

J. Biol. Chem., Vol. 277, Issue 30, 26966-26970, July 26, 2002
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Placental Alkaline Phosphatase Is Efficiently Targeted to Rafts in Supported Lipid Bilayers*

David E. SaslowskyDagger , Jared LawrenceDagger , Xiaoyan Ren§, Deborah A. Brown§, Robert M. HendersonDagger , and J. Michael EdwardsonDagger

From the Dagger  Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, United Kingdom and the § Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, New York 11794-5215

Evidence is growing that biological membranes contain lipid microdomains or "rafts" that may be involved in processes such as cellular signaling and protein trafficking. In this study, we have used atomic force microscopy to examine the behavior of rafts in supported lipid bilayers. We show that bilayers composed of equimolar dioleoylphosphatidylcholine and sphingomyelin spontaneously form rafts, which are detectable as raised features. A comparison of the extents of protrusion of the rafts in monolayers and bilayers indicates that the rafts in the two leaflets of the bilayer coincide. The rafts were observed both in the absence and presence of cholesterol (33 mol %). Cholesterol reduced raft protrusion presumably by increasing the thickness of the non-raft bilayer. PLAP (glycosylphosphatidylinositol-anchored protein placental alkaline phosphatase) was purified and shown to exist as a dimer. Following its incorporation into supported lipid bilayers, PLAP was found to be targeted efficiently to rafts, both in the absence and presence of cholesterol. We suggest that atomic force microscopy provides a powerful tool for the study of raft structure and properties.

* This work was supported by Grant B12816 from the Biotechnology and Biological Sciences Research Council (to R. M. H. and J. M. E.) and Grant GM47987 from the National Institutes of Health (to D. A. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 44-1223-334014; Fax: 44-1223-334040; E-mail: jme1000@cam.ac.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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