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Journal of Histochemistry and Cytochemistry, Vol. 51, 245-252, February 2003, Copyright © 2003, The Histochemical Society, Inc.

ARTICLE

Actin-rich Spherical Extrusion Induced in Okadaic Acid-treated K562 Cells by Crosslinking of Membrane Microdomains

Takeshi Babaa, Keiko Udakab, Nobuo Teradaa, Hideho Uedaa, Yasuhisa Fujiia, Shinichi Ohnoa, and Satoshi B. Satob
a Department of Anatomy, Faculty of Medicine, University of Yamanashi, Yamanashi, Japan
b Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto, Japan

Correspondence to: Takeshi Baba, Dept. of Anatomy, Faculty of Medicine, University of Yamanashi, 1110 Shimokato, Tamaho, Yamanashi 409-3898, Japan. E-mail: tbaba@res.yamanashi- med.ac.jp

Interconnection between surface microdomains and the actin cytoskeleton is vital to various cellular activities. We studied the responses of okadaic acid (OKA)-treated K562 leukemia cells to crosslinking of membrane microdomains. Although OKA alone induced clustering of surface-bound F-actin, addition of a biotinylated poly(ethylene glycol) derivative of cholesterol (bPEG-Chol) and subsequent binding of streptavidin (SA) further induced accumulation of the clusters, resulting in the formation of a spherical cell extrusion. This extrusion was also induced by direct crosslinking of a raft marker, CD59, and ganglioside GM1. In addition, we found that knockout of the gene encoding Fyn kinase inhibited formation of the spherical extrusion in murine T-cells. In bPEG-Chol/SA-treated cells, CD59, ganglioside GM1, and clathrin/AP-2 were all accumulated on the surface of the actin-rich extrusion, whereas dynamin and transferrin receptors were unaffected. Intermediate filaments, mitochondria, and other vesicles also accumulated. These results suggest that crosslinking of membrane domains exaggerates the linkage between actin and a defined set of membrane proteins in OKA-treated cells.

(J Histochem Cytochem 51:245–252, 2003)

Key Words: lipid rafts, clathrin-coated pits, actin, okadaic acid


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