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Vitellogenin as a potential biomarker for environmental contaminants

Conference ·
OSTI ID:40094
 [1];  [2];  [3]
  1. Univ. of Florida, Gainesville, FL (United States). Dept. of Biochemical Molecular Biology
  2. Environmental Protection Agency, Gulf Breeze, FL (United States)
  3. North Carolina State Univ., Raleigh, NC (United States). Dept. of Zoology
The authors have recently obtained N-terminal amino acid sequences for the egg protein vitellogenin (Vtg) from phylogenetically diverse teleost fish ranging from rainbow trout to the striped bass. Using the striped bass sequence as a template, the other teleost fish showed at least an 87% identity through the region of amino acids 7--20. The amino acid sequence was not as well conserved for other fishes; white sturgeon (60%) and brook lamprey (47%), the clawed frog Xenopus (47--60%) or the domestic chicken (40%). The authors synthesized a consensus peptide to this highly conserved region and have raised a polygonal antibody from rabbit. This antibody shows wide cross-reactivity to Vtg from many species of teleost fish. The authors have found that serum Vtg levels are elevated in both male and female brown bullheads with liver tumors from an area contaminated with polycyclic aromatic hydrocarbons. Serum levels of Vtg were also elevated in rainbow trout with liver tumors induced with aflatoxin B-1. The authors also describe an in-vitro system of plated hepatocytes to screen for estrogenic and antiestrogenic xenobiotic chemicals in the environment and using Vtg as a screening tool to establish structure-activity relationships for reproductive failure in female fish.
OSTI ID:
40094
Report Number(s):
CONF-9410273--
Country of Publication:
United States
Language:
English