Global proteomic analysis of zebrafish plasma

TOXI 71

I. Ramesh Babu, rbabu@mit.edu1, Wolfram Goessling, Wolfram_Goessling@dfci.harvard.edu2, Leonard I. Zon, zon@enders.tch.harvard.edu3, John S. Wishnok1, and Steven R. Tannenbaum4. (1) Biological Engineering Division, Massachusetts Institute of Tehnology, 77 Massachusetts Avenue, cambridge, MA 02139, (2) Children's Hospital, Harvard Medical School, Longwood Avenue, Boston, MA 02115, (3) Karp Family Research Laboratories, Rm 7211, HHMI/Children's Hospital, 300 Longwood Ave., Boston, MA 02115, (4) Biological Engineering Division and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139
The zebrafish (Danio rerio) is an important vertebrate model for mechanisms of early development, organogenesis, vertebrate blood development and chemical/drug toxicity. These characteristics have driven the need to sequence its genome, which is on-going at several laboratories. Despite a substantial understanding of zebrafish developmental biology and genetics, its proteome remains largely unknown. Here we present the proteomic analysis of zebrafish serum. We have generated a partial 2D-gel map of the zebrafish plasma proteome and have also obtained a more comprehensive protein coverage by using 2D-LC MS/MS. From combined 2D-gel LC-MS/MS, MudPIT analyses we have identified 215 high confidence-proteins using Agilent Spectrum Mill software. Several of these, including apolipoprotein, alpha-2-macroglobulin, transferrin, fibrinogen, alpha-1-anti trypsin, ceruloplasmin, plasminogen and hemopexin, are also present in human serum. Our current objective is to investigate changes in the zebrafish proteome in response to toxic challenges.
 

Poster Session and Awards
6:00 PM-10:00 PM, Tuesday, August 21, 2007 BCEC -- 204 A/B, Poster

Division of Chemical Toxicology

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007