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

J. Biol. Chem., Vol. 279, Issue 19, 19628-19633, May 7, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/19/19628    most recent M313864200v1 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Xi, J. Articles by Eckenhoff, R. G. Search for Related Content PubMed PubMed Citation Articles by Xi, J. Articles by Eckenhoff, R. G. Social Bookmarking                      What's this?

Inhalational Anesthetic-binding Proteins in Rat Neuronal Membranes^*

Jin Xi, Renyu Liu, G. Reid Asbury, Maryellen F. Eckenhoff, and Roderic G. Eckenhoff¶

From the Department of Anesthesia, University of Pennsylvania Health System, Philadelphia, Pennsylvania 19104 and Amersham Biosciences, Piscataway, New Jersey 08855-1327

Molecular targets of inhaled anesthetics must be represented in the group that specifically bind these drugs, but the paucity of direct binding data has limited the number of candidates for further evaluation. To find candidate targets, we used a combination of photolabeling, two-dimensional gel electrophoresis, and mass spectrometry to identify halothane-binding targets in rat neuronal membranes. Of the 265 spots detected on the two-dimensional gels, 90 were labeled by [¹⁴C]halothane, and 34 were identified. Mitochondrial proteins, especially respiratory complex and voltage-dependent anion channels, dominated the labeled group, and there were several examples of subunit- and state-dependent binding. A significant correlation was found between internal protein cavities and binding in a group of proteins with high resolution structures. Therefore, in addition to identifying novel neuronal targets, these data suggest a general molecular feature, the buried cavity, as a dominant attribute of volatile anesthetic-binding sites found in a limited number of neuronal membrane proteins.

Received for publication, December 18, 2003 , and in revised form, February 20, 2004.

^* Supported by National Institute of General Medical Sciences Grants 51595 and 55876, National Institutes of Health, and by the Austin Lamont Endowment (to the Department of Anesthesia). 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.

^¶ To whom correspondence should be addressed: Dept. of Anesthesia, University of Pennsylvania Health System, 305 John Morgan, 3620 Hamilton Walk, Philadelphia, PA 19104. Tel.: 215-662-3705; Fax: 215-349-5078; E-mail: roderic.eckenhoff{at}uphs.upenn.edu.

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

This article has been cited by other articles:

				J. H. Streiff, T. W. Allen, E. Atanasova, N. Juranic, S. Macura, A. R. Penheiter, and K. A. Jones Prediction of Volatile Anesthetic Binding Sites in Proteins Biophys. J., November 1, 2006; 91(9): 3405 - 3414. [Abstract] [Full Text] [PDF]

				J. H. Atkins and J. S. Johansson Technologies to shape the future: proteomics applications in anesthesiology and critical care medicine. Anesth. Analg., April 1, 2006; 102(4): 1207 - 1216. [Abstract] [Full Text] [PDF]

				R. Liu, P. J. Loll, and R. G. Eckenhoff Structural basis for high-affinity volatile anesthetic binding in a natural 4-helix bundle protein FASEB J, April 1, 2005; 19(6): 567 - 576. [Abstract] [Full Text] [PDF]

				J. H. Streiff, N. O. Juranic, S. I. Macura, D. O. Warner, K. A. Jones, and W. J. Perkins Saturation Transfer Difference Nuclear Magnetic Resonance Spectroscopy As a Method for Screening Proteins for Anesthetic Binding Mol. Pharmacol., October 1, 2004; 66(4): 929 - 935. [Abstract] [Full Text] [PDF]