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J. Biol. Chem., Vol. 279, Issue 44, 45379-45388, October 29, 2004

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Involvement of Cell Surface HSP90 in Cell Migration Reveals a Novel Role in the Developing Nervous System^*

Katerina Sidera, Martina Samiotaki¶, Eleni Yfanti, George Panayotou¶, and Evangelia Patsavoudi||**

From the Department of Biochemistry, Hellenic Pasteur Institute, Athens 11521, Greece, ^¶Protein Chemistry Laboratory, Biomedical Sciences Research Center, Alexander Fleming, Athens 16672, Greece, and the ^||Department of Biomedical Instrumentation Technology, Technological Educational, Institute of Athens, Athens 12210, Greece

Heat shock protein HSP90 plays important roles in cellular regulation, primarily as a chaperone for a number of key intracellular proteins. We report here that the two HSP90 isoforms, and , also localize on the surface of cells in the nervous system and are involved in their migration. A 94-kDa surface antigen, the 4C5 antigen, which was previously shown to be involved in migration processes during development of the nervous system, is shown to be identical to HSP90 using mass spectrometry analysis. This identity is further confirmed by immunoprecipitation experiments and by induction of 4C5 antigen expression in heat shock-treated embryonic rat brain cultures. Moreover, immunocytochemistry on live cerebellar rat cells reveals cell surface localization of both HSP90 and -. Cell migration from cerebellar and sciatic nerve explants is inhibited by anti-HSP90 and anti-HSP90 antibodies, similarly to the inhibition observed with monoclonal antibody 4C5. Moreover, immunostaining with rhodamine-phalloidin of migrating Schwann cells cultured in the presence of antibodies against both and isoforms of HSP90 reveals that HSP90 activity is associated with actin cytoskeletal organization, necessary for lamellipodia formation.

Received for publication, May 17, 2004 , and in revised form, July 9, 2004.

^* This work was supported by the Hellenic General Secretarial of Research and Technology. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a Hellenic Pasteur Institute scholarship.

^** To whom correspondence should be addressed: Dept. of Biochemistry Hellenic Pasteur Institute, 127 Vas. Sofias, Athens 11521, Greece. Tel.: 302106478838; Fax: 302106423498; E-mail: epatsavoudi{at}pasteur.gr.

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