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Affinity proteomics discovers decreased levels of AMFR in plasma from Osteoporosis patients

PURPOSE: Affinity proteomic approaches by antibody bead arrays enable multiplexed analysis of proteins in body fluids. In the presented study, we investigated blood plasma within osteoporosis to discovery differential protein profiles and to propose novel biomarkers candidates for subsequent studies...

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Autores principales: Qundos, Ulrika, Drobin, Kimi, Mattsson, Cecilia, Hong, Mun‐Gwan, Sjöberg, Ronald, Forsström, Björn, Solomon, David, Uhlén, Mathias, Nilsson, Peter, Michaëlsson, Karl, Schwenk, Jochen M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5029581/
https://www.ncbi.nlm.nih.gov/pubmed/25689831
http://dx.doi.org/10.1002/prca.201400167
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author Qundos, Ulrika
Drobin, Kimi
Mattsson, Cecilia
Hong, Mun‐Gwan
Sjöberg, Ronald
Forsström, Björn
Solomon, David
Uhlén, Mathias
Nilsson, Peter
Michaëlsson, Karl
Schwenk, Jochen M.
author_facet Qundos, Ulrika
Drobin, Kimi
Mattsson, Cecilia
Hong, Mun‐Gwan
Sjöberg, Ronald
Forsström, Björn
Solomon, David
Uhlén, Mathias
Nilsson, Peter
Michaëlsson, Karl
Schwenk, Jochen M.
author_sort Qundos, Ulrika
collection PubMed
description PURPOSE: Affinity proteomic approaches by antibody bead arrays enable multiplexed analysis of proteins in body fluids. In the presented study, we investigated blood plasma within osteoporosis to discovery differential protein profiles and to propose novel biomarkers candidates for subsequent studies. EXPERIMENTAL DESIGN: Starting with 4608 antibodies and plasma samples from 22 women for an untargeted screening, a set of 72 proteins were suggested for further analysis. Complementing these with targets from literature and other studies, a targeted bead array of 180 antibodies was built to profile for 92 proteins in plasma samples of 180 women from two independent population‐based studies. RESULTS: Differential profiles between osteoporosis patients and matched controls were discovered for 12 proteins in at least one of the two study sets. Among these targets, the levels of autocrine motility factor receptor (AMFR) were concordantly lower in plasma of female osteoporosis patients. Subsequently, verification of anti‐AMFR antibody selectivity was conducted using high‐density peptide and protein arrays, and Western blotting. CONCLUSIONS AND CLINICAL RELEVANCE: Further validation in additional study sets will be needed to determine the clinical value of the observed decrease in AMFR plasma levels in osteoporosis patients, but AMFR may aid our understanding of disease mechanisms and could support existing tools for diagnosis and monitoring of patient mobility within osteoporosis.
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spelling pubmed-50295812016-10-03 Affinity proteomics discovers decreased levels of AMFR in plasma from Osteoporosis patients Qundos, Ulrika Drobin, Kimi Mattsson, Cecilia Hong, Mun‐Gwan Sjöberg, Ronald Forsström, Björn Solomon, David Uhlén, Mathias Nilsson, Peter Michaëlsson, Karl Schwenk, Jochen M. Proteomics Clin Appl Research Articles PURPOSE: Affinity proteomic approaches by antibody bead arrays enable multiplexed analysis of proteins in body fluids. In the presented study, we investigated blood plasma within osteoporosis to discovery differential protein profiles and to propose novel biomarkers candidates for subsequent studies. EXPERIMENTAL DESIGN: Starting with 4608 antibodies and plasma samples from 22 women for an untargeted screening, a set of 72 proteins were suggested for further analysis. Complementing these with targets from literature and other studies, a targeted bead array of 180 antibodies was built to profile for 92 proteins in plasma samples of 180 women from two independent population‐based studies. RESULTS: Differential profiles between osteoporosis patients and matched controls were discovered for 12 proteins in at least one of the two study sets. Among these targets, the levels of autocrine motility factor receptor (AMFR) were concordantly lower in plasma of female osteoporosis patients. Subsequently, verification of anti‐AMFR antibody selectivity was conducted using high‐density peptide and protein arrays, and Western blotting. CONCLUSIONS AND CLINICAL RELEVANCE: Further validation in additional study sets will be needed to determine the clinical value of the observed decrease in AMFR plasma levels in osteoporosis patients, but AMFR may aid our understanding of disease mechanisms and could support existing tools for diagnosis and monitoring of patient mobility within osteoporosis. John Wiley and Sons Inc. 2015-04-21 2016-06 /pmc/articles/PMC5029581/ /pubmed/25689831 http://dx.doi.org/10.1002/prca.201400167 Text en © 2015 The Authors. PROTEOMICS ‐ Clinical Applications Published by WILEY‐VCH Verlag GmbH & Co. KGaA This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial (http://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Research Articles
Qundos, Ulrika
Drobin, Kimi
Mattsson, Cecilia
Hong, Mun‐Gwan
Sjöberg, Ronald
Forsström, Björn
Solomon, David
Uhlén, Mathias
Nilsson, Peter
Michaëlsson, Karl
Schwenk, Jochen M.
Affinity proteomics discovers decreased levels of AMFR in plasma from Osteoporosis patients
title Affinity proteomics discovers decreased levels of AMFR in plasma from Osteoporosis patients
title_full Affinity proteomics discovers decreased levels of AMFR in plasma from Osteoporosis patients
title_fullStr Affinity proteomics discovers decreased levels of AMFR in plasma from Osteoporosis patients
title_full_unstemmed Affinity proteomics discovers decreased levels of AMFR in plasma from Osteoporosis patients
title_short Affinity proteomics discovers decreased levels of AMFR in plasma from Osteoporosis patients
title_sort affinity proteomics discovers decreased levels of amfr in plasma from osteoporosis patients
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5029581/
https://www.ncbi.nlm.nih.gov/pubmed/25689831
http://dx.doi.org/10.1002/prca.201400167
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