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J. Biol. Chem., Vol. 279, Issue 50, 52033-52041, December 10, 2004

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Proteomic Analysis of the Drosophila Larval Hemolymph Clot^*

Christine Karlsson, Ahmed M. Korayem¶, Christoph Scherfer||, Olga Loseva**, Mitchell S. Dushay, and Ulrich Theopold

From the Department of Molecular Biology and Functional Genomics, University of Stockholm, 10691 Stockholm, Sweden, the Department of Zoology, Faculty of Science, Assiut University, 71516 Assiut, Egypt, and the Department of Natural Sciences, Södertörns Högskola, 14189 Huddinge, Sweden

Components of the insect clot, an extremely rapid forming and critical part of insect immunity, are just beginning to be identified (1). Here we present a proteomic comparison of larval hemolymph before and after clotting to learn more about this process. This approach was supplemented by the identification of substrates for the enzyme transglutaminase, which plays a role in both vertebrate blood clotting (as factor XIIIa) and hemolymph coagulation in arthropods. Hemolymph proteins present in lower amounts after clotting include CG8502 (a protein with a mucin-type domain and a domain with similarity to cuticular components), CG11313 (a protein with similarity to prophenoloxidase-activating proteases), and two phenoloxidases, lipophorin, a secreted gelsolin, and CG15825, which had previously been isolated from clots (2). Proteins whose levels increase after clotting include a ferritin-subunit and two members of the immunoglobulin family with a high similarity to the small immunoglobulin-like molecules involved in mammalian innate immunity. Our results correlate with findings from another study of coagulation (2) that involved a different experimental approach. Proteomics allows the isolation of novel candidate clotting factors, leading to a more complete picture of clotting. In addition, our two-dimensional protein map of cell-free Drosophila hemolymph includes many additional proteins that were not found in studies performed on whole hemolymph.

Received for publication, July 20, 2004 , and in revised form, October 1, 2004.

^* This work was supported in part by research grants (to U. T.) from the Swedish Research Council (including a grant from the Middle East and North African (MENA) partnership program to U. T. and A. M. K.), the Carl-Tryggers Foundation, and a setup grant from Stockholm University. 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 postdoctoral fellowship from the Wenner-Gren foundation.

^|| Supported by a fellowship from the German Academic Exchange Service (DAAD).

^** Supported by a postdoctoral fellowship from the Swedish Research Council.

To whom correspondence should be addressed. Tel.: 46-8-164181; Fax: 46-8-152350; E-mail: uli{at}molbio.su.se.

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