|A proteomic analysis of green and white sturgeon larvae exposed to heat stress and selenium|Silvestre, F.; Linares-Casenave, J.; Doroshov, S.I.; Kültz, D. (2010). A proteomic analysis of green and white sturgeon larvae exposed to heat stress and selenium. Sci. Total Environ. 408(16): 3176-3188. hdl.handle.net/10.1016/j.scitotenv.2010.04.005
In: Science of the Total Environment. Elsevier: Amsterdam. ISSN 0048-9697, more
Acipenseridae Bonaparte, 1831 [WoRMS]; Marine; Brackish water; Fresh water
Sturgeon; Selenium; Temperature; Proteomics; Valosin-containing protein; Biomarker
|Authors|| || Top |
- Silvestre, F., more
- Linares-Casenave, J.
- Doroshov, S.I.
- Kültz, D.
Temperature and selenium are two environmental parameters that potentially affect reproduction and stock recruitment of sturgeon in the San Francisco Bay/Delta Estuary. To identify proteins whose expression is modified by these environmental stressors, we performed a proteomic analysis on larval green and white sturgeons exposed to 18 or 26 °C and micro-injected with Seleno-L-Methionine to reach 8 µg g-1 selenium body burden, with L-Methionine as a control. Selenium and high temperature induced mortalities and abnormal morphologies in both species, with a higher mortality in green sturgeon. Larval proteins were separated by two-dimensional gel electrophoresis and differential abundances were detected following spot quantitation and hierarchical cluster analysis. In green sturgeon, 34 of 551 protein spots detected on gels showed a variation in abundance whereas in white sturgeon only 9 of 580 protein spots were differentially expressed (P < 0.01). Gel replicates were first grouped according to heat treatment. Fifteen of these spots were identified using MALDI TOF/TOF mass spectrometry. Proteins involved in protein folding, protein synthesis, protein degradation, ATP supply and structural proteins changed in abundance in response to heat and/or selenium. 40S ribosomal protein SA, FK506-binding protein 10, 65 kDa regulatory subunit A of protein phosphatase 2, protein disulfide isomerase, stress-induced-phosphoprotein 1, suppression of tumorigenicity 13 and collagen type II alpha 1, were differentially expressed in high temperature treatment only. Serine/arginine repetitive matrix protein 1, creatine kinase, serine peptidase inhibitor Kazal type 5 and HSP90 were sensitive to combined temperature and selenium exposure. Valosin-containing protein, a protein involved in aggresome formation and in protein quality control decreased more than 50% in response to selenium treatment. Potential use of such proteins as biomarkers of environmental stressors in larval sturgeons could indicate early warning signals preceding population decline.