Literature DB >> 17384011

Simultaneous quantification of ghrelin and desacyl-ghrelin by liquid chromatography-tandem mass spectrometry in plasma, serum, and cell supernatants.

Manfred Rauh1, Michael Gröschl, Wolfgang Rascher.   

Abstract

BACKGROUND: A sensitive method specific for ghrelins is needed for investigations of this gastrointestinal peptide. Our aim was to develop and validate a quantitative mass spectrometry (MS) method to measure ghrelin and desacyl-ghrelin simultaneously.
METHODS: After deproteinization by precipitation, we performed reversed-phase separation with a rapid 2-column online extraction design coupled to a quadrupole mass spectrometer for electrospray ionization MS detection. Chromatography was performed on a C(18) monolithic column, with ammonium acetate buffer/methanol as the mobile phase and a chromatographic run time of 6 min/sample. The 4-fold-charged ions were used for multiple reaction monitoring experiments.
RESULTS: The method was linear with injections of 0.01-10 ng. Limits of detection and quantification were 0.02 and 0.07 microg/L for ghrelin, respectively, and 0.03 and 0.35 microg/L for desacyl-ghrelin. Intra- and interday imprecision (CVs) were 9%-4% and 12%-6% at concentrations of 0.33-5.93 microg/L for ghrelin, respectively, and 16%-6% and 15%-8% at concentrations of 1.12-10.02 microg/L for desacyl-ghrelin. The mean (SD) recoveries in plasma of added ghrelin and desacyl-ghrelin were 95.8% (12%) and 101% (1.2%), respectively. Using kinetic modeling, we determined the mean (SD) periods of half-change (t(1/2)) of ghrelin to be 156 (16) min in EDTA plasma and 49 (1) min in Li-heparin plasma. Bland-Altman analysis showed that the median differences between EIA and liquid chromatography-tandem mass spectrometry (MS/MS) for desacyl-ghrelin were -40% for plasma/serum samples and 85% for cell supernatants and for ghrelin were 6% for enriched plasma samples and 44% for cell supernatants.
CONCLUSION: Our HPLC-MS/MS procedure has excellent selectivity and sufficient limit of quantification to allow the monitoring of concentration-time profiles in biological matrices.

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Year:  2007        PMID: 17384011     DOI: 10.1373/clinchem.2006.078956

Source DB:  PubMed          Journal:  Clin Chem        ISSN: 0009-9147            Impact factor:   8.327


  9 in total

1.  Radiometric assay of ghrelin hydrolase activity and 3H-ghrelin distribution into mouse tissues.

Authors:  Vicky Ping Chen; Yang Gao; Liyi Geng; Stephen Brimijoin
Journal:  Biochem Pharmacol       Date:  2015-10-26       Impact factor: 5.858

Review 2.  The ghrelin axis in disease: potential therapeutic indications.

Authors:  Ralf Nass; Bruce D Gaylinn; Michael O Thorner
Journal:  Mol Cell Endocrinol       Date:  2011-02-25       Impact factor: 4.102

3.  The antimicrobial activity of the appetite peptide hormone ghrelin.

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4.  Comparison of competitive radioimmunoassays and two-site sandwich assays for the measurement and interpretation of plasma ghrelin levels.

Authors:  Catherine Prudom; Jianhua Liu; James Patrie; Bruce D Gaylinn; Karen E Foster-Schubert; David E Cummings; Michael O Thorner; H Mario Geysen
Journal:  J Clin Endocrinol Metab       Date:  2010-03-01       Impact factor: 5.958

5.  A liquid chromatography-mass spectrometry assay for quantification of Exendin[9-39] in human plasma.

Authors:  Maria Lasaosa; Puja Patel; Stephanie Givler; Diva D De León; Steven H Seeholzer
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6.  Ghrelin promotes oral tumor cell proliferation by modifying GLUT1 expression.

Authors:  Dominik Kraus; Jan Reckenbeil; Matthias Wenghoefer; Helmut Stark; Matthias Frentzen; Jean-Pierre Allam; Natalija Novak; Stilla Frede; Werner Götz; Rainer Probstmeier; Rainer Meyer; Jochen Winter
Journal:  Cell Mol Life Sci       Date:  2015-09-25       Impact factor: 9.261

Review 7.  The role of ghrelin, salivary secretions, and dental care in eating disorders.

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Review 8.  Ghrelin-Mediated Regeneration and Plasticity After Nervous System Injury.

Authors:  Irina Stoyanova; David Lutz
Journal:  Front Cell Dev Biol       Date:  2021-03-25

Review 9.  Expression of the growth hormone secretagogue receptor 1a (GHS-R1a) in the brain.

Authors:  Marat I Airapetov; Sergei O Eresko; Andrei A Lebedev; Evgenii R Bychkov; Petr D Shabanov
Journal:  Physiol Rep       Date:  2021-11
  9 in total

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