Apo-AII is an elevated biomaker of chronic non-human primate ethanol self-administration

Willard M. Freeman, Randy S. Gooch, Melinda E. Lull, Travis J. Worst, Stephen J. Walker, Arron S.L. Xu, Heather Green, Peter J. Pierre, Kathleen A. Grant, Kent E. Vrana

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Aims: Serum protein profiles were examined in näve, ethanol self-administering and ethanol abstinent cynomolgus monkeys (Macaca fasicularis) to search for differences in protein expression which could possibly serve as biomarkers of heavy ethanol consumption. Methods: Surface-enhanced laser desorption ionization time-of-flight (SELDI-ToF) mass spectrometry was used for proteomic profiling of serum. Results: Two proteins were identified by SELDI-ToF to be increased in ethanol self-administering compared with abstinent animals. These proteins were identified to be apolipoprotein AI (Apo-AI) and apolipoprotein AII (Apo-AII) by peptide mass fingerprinting and comparison with spectra of purified human Apo-AI and AII proteins. Immunoblot analysis of Apo-AI and Apo-AII was performed on a separate group of animals (within-animal ethanol-näve and self-administering) and confirmed a statistically significant increase in Apo-AII, while Apo-AI was unchanged. Conclusions: An open proteomic screen of serum and confirmation in a separate set of animals found Apo-AII to be increased in the serum of ethanol self-administering monkeys. These results are consistent with previous clinical studies of human ethanol consumption and serum apolipoprotein expression. Moreover, these results validate the use of non-human primates as a model organism for proteomic analysis of ethanol self-administration biomarkers.

Original languageEnglish (US)
Pages (from-to)300-305
Number of pages6
JournalAlcohol and Alcoholism
Volume41
Issue number3
DOIs
StatePublished - May 1 2006

Fingerprint

Apolipoprotein A-II
Self Administration
Primates
Ethanol
Apolipoprotein A-I
Animals
Proteomics
Biomarkers
Serum
Ionization
Desorption
Proteins
Lasers
Peptide Mapping
Macaca fascicularis
Apolipoproteins
Macaca
Haplorhini
Mass spectrometry
Blood Proteins

All Science Journal Classification (ASJC) codes

  • Medicine (miscellaneous)
  • Toxicology
  • Psychiatry and Mental health

Cite this

Freeman, W. M., Gooch, R. S., Lull, M. E., Worst, T. J., Walker, S. J., Xu, A. S. L., ... Vrana, K. E. (2006). Apo-AII is an elevated biomaker of chronic non-human primate ethanol self-administration. Alcohol and Alcoholism, 41(3), 300-305. https://doi.org/10.1093/alcalc/agl021
Freeman, Willard M. ; Gooch, Randy S. ; Lull, Melinda E. ; Worst, Travis J. ; Walker, Stephen J. ; Xu, Arron S.L. ; Green, Heather ; Pierre, Peter J. ; Grant, Kathleen A. ; Vrana, Kent E. / Apo-AII is an elevated biomaker of chronic non-human primate ethanol self-administration. In: Alcohol and Alcoholism. 2006 ; Vol. 41, No. 3. pp. 300-305.
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Freeman, WM, Gooch, RS, Lull, ME, Worst, TJ, Walker, SJ, Xu, ASL, Green, H, Pierre, PJ, Grant, KA & Vrana, KE 2006, 'Apo-AII is an elevated biomaker of chronic non-human primate ethanol self-administration', Alcohol and Alcoholism, vol. 41, no. 3, pp. 300-305. https://doi.org/10.1093/alcalc/agl021

Apo-AII is an elevated biomaker of chronic non-human primate ethanol self-administration. / Freeman, Willard M.; Gooch, Randy S.; Lull, Melinda E.; Worst, Travis J.; Walker, Stephen J.; Xu, Arron S.L.; Green, Heather; Pierre, Peter J.; Grant, Kathleen A.; Vrana, Kent E.

In: Alcohol and Alcoholism, Vol. 41, No. 3, 01.05.2006, p. 300-305.

Research output: Contribution to journalArticle

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T1 - Apo-AII is an elevated biomaker of chronic non-human primate ethanol self-administration

AU - Freeman, Willard M.

AU - Gooch, Randy S.

AU - Lull, Melinda E.

AU - Worst, Travis J.

AU - Walker, Stephen J.

AU - Xu, Arron S.L.

AU - Green, Heather

AU - Pierre, Peter J.

AU - Grant, Kathleen A.

AU - Vrana, Kent E.

PY - 2006/5/1

Y1 - 2006/5/1

N2 - Aims: Serum protein profiles were examined in näve, ethanol self-administering and ethanol abstinent cynomolgus monkeys (Macaca fasicularis) to search for differences in protein expression which could possibly serve as biomarkers of heavy ethanol consumption. Methods: Surface-enhanced laser desorption ionization time-of-flight (SELDI-ToF) mass spectrometry was used for proteomic profiling of serum. Results: Two proteins were identified by SELDI-ToF to be increased in ethanol self-administering compared with abstinent animals. These proteins were identified to be apolipoprotein AI (Apo-AI) and apolipoprotein AII (Apo-AII) by peptide mass fingerprinting and comparison with spectra of purified human Apo-AI and AII proteins. Immunoblot analysis of Apo-AI and Apo-AII was performed on a separate group of animals (within-animal ethanol-näve and self-administering) and confirmed a statistically significant increase in Apo-AII, while Apo-AI was unchanged. Conclusions: An open proteomic screen of serum and confirmation in a separate set of animals found Apo-AII to be increased in the serum of ethanol self-administering monkeys. These results are consistent with previous clinical studies of human ethanol consumption and serum apolipoprotein expression. Moreover, these results validate the use of non-human primates as a model organism for proteomic analysis of ethanol self-administration biomarkers.

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