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Functional Proteomic Profiling of Phosphodiesterases Using SeraFILE Separations Platform

Functional proteomic profiling can help identify targets for disease diagnosis and therapy. Available methods are limited by the inability to profile many functional properties measured by enzymes kinetics. The functional proteomic profiling approach proposed here seeks to overcome such limitations....

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Detalles Bibliográficos
Autores principales: Oka, Amita R., Kuruc, Matthew P., Gujarathi, Ketan M., Roy, Swapan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3512300/
https://www.ncbi.nlm.nih.gov/pubmed/23227336
http://dx.doi.org/10.1155/2012/515372
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author Oka, Amita R.
Kuruc, Matthew P.
Gujarathi, Ketan M.
Roy, Swapan
author_facet Oka, Amita R.
Kuruc, Matthew P.
Gujarathi, Ketan M.
Roy, Swapan
author_sort Oka, Amita R.
collection PubMed
description Functional proteomic profiling can help identify targets for disease diagnosis and therapy. Available methods are limited by the inability to profile many functional properties measured by enzymes kinetics. The functional proteomic profiling approach proposed here seeks to overcome such limitations. It begins with surface-based proteome separations of tissue/cell-line extracts, using SeraFILE, a proprietary protein separations platform. Enzyme kinetic properties of resulting subproteomes are then characterized, and the data integrated into proteomic profiles. As a model, SeraFILE-derived subproteomes of cyclic nucleotide-hydrolyzing phosphodiesterases (PDEs) from bovine brain homogenate (BBH) and rat brain homogenate (RBH) were characterized for cAMP hydrolysis activity in the presence (challenge condition) and absence of cGMP. Functional profiles of RBH and BBH were compiled from the enzyme activity response to the challenge condition in each of the respective subproteomes. Intersample analysis showed that comparable profiles differed in only a few data points, and that distinctive subproteomes can be generated from comparable tissue samples from different animals. These results demonstrate that the proposed methods provide a means to simplify intersample differences, and to localize proteins attributable to sample-specific responses. It can be potentially applied for disease and nondisease sample comparison in biomarker discovery and drug discovery profiling.
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spelling pubmed-35123002012-12-07 Functional Proteomic Profiling of Phosphodiesterases Using SeraFILE Separations Platform Oka, Amita R. Kuruc, Matthew P. Gujarathi, Ketan M. Roy, Swapan Int J Proteomics Research Article Functional proteomic profiling can help identify targets for disease diagnosis and therapy. Available methods are limited by the inability to profile many functional properties measured by enzymes kinetics. The functional proteomic profiling approach proposed here seeks to overcome such limitations. It begins with surface-based proteome separations of tissue/cell-line extracts, using SeraFILE, a proprietary protein separations platform. Enzyme kinetic properties of resulting subproteomes are then characterized, and the data integrated into proteomic profiles. As a model, SeraFILE-derived subproteomes of cyclic nucleotide-hydrolyzing phosphodiesterases (PDEs) from bovine brain homogenate (BBH) and rat brain homogenate (RBH) were characterized for cAMP hydrolysis activity in the presence (challenge condition) and absence of cGMP. Functional profiles of RBH and BBH were compiled from the enzyme activity response to the challenge condition in each of the respective subproteomes. Intersample analysis showed that comparable profiles differed in only a few data points, and that distinctive subproteomes can be generated from comparable tissue samples from different animals. These results demonstrate that the proposed methods provide a means to simplify intersample differences, and to localize proteins attributable to sample-specific responses. It can be potentially applied for disease and nondisease sample comparison in biomarker discovery and drug discovery profiling. Hindawi Publishing Corporation 2012 2012-11-25 /pmc/articles/PMC3512300/ /pubmed/23227336 http://dx.doi.org/10.1155/2012/515372 Text en Copyright © 2012 Amita R. Oka et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Oka, Amita R.
Kuruc, Matthew P.
Gujarathi, Ketan M.
Roy, Swapan
Functional Proteomic Profiling of Phosphodiesterases Using SeraFILE Separations Platform
title Functional Proteomic Profiling of Phosphodiesterases Using SeraFILE Separations Platform
title_full Functional Proteomic Profiling of Phosphodiesterases Using SeraFILE Separations Platform
title_fullStr Functional Proteomic Profiling of Phosphodiesterases Using SeraFILE Separations Platform
title_full_unstemmed Functional Proteomic Profiling of Phosphodiesterases Using SeraFILE Separations Platform
title_short Functional Proteomic Profiling of Phosphodiesterases Using SeraFILE Separations Platform
title_sort functional proteomic profiling of phosphodiesterases using serafile separations platform
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3512300/
https://www.ncbi.nlm.nih.gov/pubmed/23227336
http://dx.doi.org/10.1155/2012/515372
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