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Identification of Estrogen-responsive Vitelline Envelope Protein Fragments from Rainbow Trout (Oncorhynchus mykiss) Plasma Using Mass Spectrometry
Citation:
SALINAS, K., M. J. HEMMER, J. A. SERRANO, L. HIGGINS, L. B. ANDERSON, A. D. BENNINGHOFF, D. E. WILLIAMS, AND C. WALKER. Identification of Estrogen-responsive Vitelline Envelope Protein Fragments from Rainbow Trout (Oncorhynchus mykiss) Plasma Using Mass Spectrometry. MOLECULAR REPRODUCTION AND DEVELOPMENT. John Wiley & Sons, Ltd., Indianapolis, IN, 77(11):963-970, (2010).
Impact/Purpose:
Mass spectrometric detection and identification of estrogen-responsive plasma protein biomarkers in rainbow trout (Oncorhynchus mykiss). Differential regulation of VEP and vitellogenin proteins provides valuable complementary information regarding temporal and mechanistic aspects of estrogenic exposure in aquatic fish species, and could aid in the developement of proteomic methods for use in risk assessment and monitoring efforts.
Description:
Plasma protein biomarkers associated with exposure of rainbow trout (Oncorhynchus mykiss) to 17β-estradiol were isolated and identified using novel sample preparation techniques and state-of-the-art mass spectrometry and bioinformatics approaches. Juvenile male and female trout were administered 17β-estradiol through dietary exposure. Plasma samples from exposed and control trout were screened for biomarkers by high throughput, low resolution MALDI TOF MS, and peptides of interest were selected for identification via MALDI QqTOF MS/MS and MALDI TOFTOF MS/MS analysis. To isolate and analyze proteins of interest from high abundance plasma components, two fractionation methods were applied: solid-phase ligand library spin columns and strong anion exchange spin columns. Two masses were identified as significant matches for the C-terminal propeptide from vitelline envelope protein (VEP)α and VEPγ isoforms of rainbow trout. Our findings support previous suggestions of VEPs as alternative biomarkers of estrogenic exposure in teleost fish. Differential regulation of VEP and vitellogenin proteins provides valuable complementary information regarding temporal and mechanistic aspects of estrogenic exposure in aquatic fish species, and could aid in the development of proteomic methods for use in risk assessment and monitoring efforts.