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A proteomic approach combining MS and bioinformatic analysis for the detection and identification of biomarkers of administration of exogenous human growth hormone in humans

journal contribution
posted on 18.09.2014 by Joshua Boateng, Richard G. Kay, Lee Lancashire, Pamela Brown, Cristiana Velloso, Pierre Bouloux, Phil Teale, Jane Roberts, Robert Rees, Graham Ball, Stephen Harridge, Geoffrey Goldspink, Colin Creaser
An integrated MS-based proteomic approach is described that combines MALDI-MS and LC-MS with artificial neural networks for the identification of protein and peptide biomarkers associated with recombinant human growth hormone (rhGH) administration. Serum from exercised males administered with rhGH or placebo was analysed using ELISA to determine insulin-like growth factor-I concentrations. Diluted serum from rhGH- and placebo-treated subjects was analysed for protein biomarkers by MALDI-MS, whereas LC-MS was used to analyse tryptically digested ACN-depleted serum extracts for peptide biomarkers. Ion intensities and m/z values were used as inputs to artificial neural networks to classify samples into rhGH- and placebo-treated groups. Six protein ions (MALDI-MS) correctly classified 96% of samples into their respective groups, with a sensitivity of 91% (20 of 22 rhGH treated) and specificity of 100% (24 of 24 controls). Six peptide ions (LC-MS) were also identified and correctly classified 93% of samples with a sensitivity of 90% (19 of 21 rhGH treated) and a specificity of 95% (20 of 21 controls). The peptide biomarker ion with the highest significance was sequenced using LC-MS/MS and database searching and found to be associated with leucine-rich α-2-glycoprotein.

History

School

  • Science

Department

  • Chemistry

Published in

PROTEOMICS CLINICAL APPLICATIONS

Volume

3

Issue

8

Pages

912 - 922 (11)

Citation

BOATENG, J. ... et al, 2009. A proteomic approach combining MS and bioinformatic analysis for the detection and identification of biomarkers of administration of exogenous human growth hormone in humans. PROTEOMICS - Clinical Applications, 3 (8), pp. 912 - 922.

Publisher

© Wiley VCH Verlag GmbH & Co.

Version

VoR (Version of Record)

Publisher statement

This work is made available according to the conditions of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) licence. Full details of this licence are available at: https://creativecommons.org/licenses/by-nc-nd/4.0/

Publication date

2009

Notes

This article is closed access.

ISSN

1862-8346

Language

en

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