NDLI: Selective binding of perfringolysin O derivative to cholesterol-rich membrane microdomains (rafts).

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Selective binding of perfringolysin O derivative to cholesterol-rich membrane microdomains (rafts).

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Selective binding of perfringolysin O derivative to cholesterol-rich membrane microdomains (rafts).

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nakamura, M. Ohno-iwashita, Y. Iwashita, S. Waheed, A. A. Shimada, Y. Hayashi, M. Slot, J. W. Inomata, M. Heijnen, H. F.
Description	Author Affiliation: Waheed AA ( Department of Protein Biochemistry, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173-0015, Japan. awaheed@tmig.or.jp);
Abstract	There is increasing evidence that sphingolipid- and cholesterol-rich microdomains (rafts) exist in the plasma membrane. Specific proteins assemble in these membrane domains and play a role in signal transduction and many other cellular events. Cholesterol depletion causes disassembly of the raft-associated proteins, suggesting an essential role of cholesterol in the structural maintenance and function of rafts. However, no tool has been available for the detection and monitoring of raft cholesterol in living cells. Here we show that a protease-nicked and biotinylated derivative (BCtheta) of perfringolysin O (theta-toxin) binds selectively to cholesterol-rich microdomains of intact cells, the domains that fulfill the criteria of rafts. We fractionated the homogenates of nontreated and Triton X-100-treated platelets after incubation with BCtheta on a sucrose gradient. BCtheta was predominantly localized in the floating low-density fractions (FLDF) where cholesterol, sphingomyelin, and Src family kinases are enriched. Immunoelectron microscopy demonstrated that BCtheta binds to a subpopulation of vesicles in FLDF. Depletion of 35% cholesterol from platelets with cyclodextrin, which accompanied 76% reduction in cholesterol from FLDF, almost completely abolished BCtheta binding to FLDF. The staining patterns of BCtheta and filipin in human epidermoid carcinoma A431 cells with and without cholesterol depletion suggest that BCtheta binds to specific membrane domains on the cell surface, whereas filipin binding is indiscriminate to cell cholesterol. Furthermore, BCtheta binding does not cause any damage to cell membranes, indicating that BCtheta is a useful probe for the detection of membrane rafts in living cells.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	98
Language	English
Publisher	National Academy of Sciences
Publisher Date	2001-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Toxins Metabolism Cholesterol Membrane Microdomains Beta-Cyclodextrins Biotinylation Blood Platelets Cytology Drug Effects Cells, Cultured Centrifugation, Density Gradient Cyclodextrins Pharmacology Endopeptidases Erythrocytes Filipin Hemolysin Proteins Chemistry Microscopy, Immunoelectron Molecular Probes Octoxynol Sphingomyelins Substrate Specificity Tumor Cells, Cultured Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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