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Antibody Array Analysis for Protein Detection in Porcine Non-Cystic Fibrosis and Cystic Fibrosis Airway Epithelia
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A3679 - Antibody Array Analysis for Protein Detection in Porcine Non-Cystic Fibrosis and Cystic Fibrosis Airway Epithelia
Author Block: M. I. Aguilar Pescozo, N. D. Gansemer, M. R. Stroik, L. S. Powers, P. H. Karp, J. Zabner, A. A. Pezzulo, D. A. Stoltz; Internal Medicine, University of Iowa, Iowa City, IA, United States.
Introduction: Cystic fibrosis (CF) is an autosomal recessive disease caused by mutations in the gene encoding the cystic fibrosis transmembrane conductance regulator (CFTR). How loss of CFTR mediated chloride and bicarbonate transport leads to chronic airway infection and inflammation has remained uncertain. While there are very few differences between CF and non-CF pig airway epithelial cells at birth at the transcriptional level, functional protein differences could be present. The goal of this study was to determine if CFTR loss causes differential regulation of protein phosphorylation in CF, prior to the onset of airway infection and inflammation.
Methods: To determine previously uncharacterized functional changes caused by CFTR loss, we performed protein phosphorylation array analysis in airway epithelial cell cultures from newborn non-CF and CF pigs. The array contains approximately 1,318 antibodies against individual proteins and their phosphorylation sites encompassing over 38 different regulatory pathways.
Results: We found that 38 proteins were differentially phosphorylated between CF and non-CF pig airway cultures in the antibody array analysis. The top three highest differentially phosphorylated proteins in CF compared to non-CF were Activating Transcription Factor 1 (ATF1), Spleen Associated Tyrosine Kinase (SYK), and Jun Proto-Oncogene (c-Jun), whereas the lowest three differentially phosphorylated proteins were Myocyte Enhancer Factor 2A (MEF2A), Cyclin E2 (CCNE2), and PKC delta (PRKCD). Ingenuity Pathway Analysis revealed that multiple pathways including the p38 Mitogen Activated Protein Kinases (p38 MAPK) signaling pathway were significantly dysregulated by CFTR loss.
Conclusion: We used phosphorylated and un-phosphorylated protein antibody array analysis to identify multiple proteins dysregulated by lack of CFTR. Whether these proteins are important in disease pathogenesis remains to be determined. These studies may provide additional insight into CF disease mechanisms.
Author Block: M. I. Aguilar Pescozo, N. D. Gansemer, M. R. Stroik, L. S. Powers, P. H. Karp, J. Zabner, A. A. Pezzulo, D. A. Stoltz; Internal Medicine, University of Iowa, Iowa City, IA, United States.
Introduction: Cystic fibrosis (CF) is an autosomal recessive disease caused by mutations in the gene encoding the cystic fibrosis transmembrane conductance regulator (CFTR). How loss of CFTR mediated chloride and bicarbonate transport leads to chronic airway infection and inflammation has remained uncertain. While there are very few differences between CF and non-CF pig airway epithelial cells at birth at the transcriptional level, functional protein differences could be present. The goal of this study was to determine if CFTR loss causes differential regulation of protein phosphorylation in CF, prior to the onset of airway infection and inflammation.
Methods: To determine previously uncharacterized functional changes caused by CFTR loss, we performed protein phosphorylation array analysis in airway epithelial cell cultures from newborn non-CF and CF pigs. The array contains approximately 1,318 antibodies against individual proteins and their phosphorylation sites encompassing over 38 different regulatory pathways.
Results: We found that 38 proteins were differentially phosphorylated between CF and non-CF pig airway cultures in the antibody array analysis. The top three highest differentially phosphorylated proteins in CF compared to non-CF were Activating Transcription Factor 1 (ATF1), Spleen Associated Tyrosine Kinase (SYK), and Jun Proto-Oncogene (c-Jun), whereas the lowest three differentially phosphorylated proteins were Myocyte Enhancer Factor 2A (MEF2A), Cyclin E2 (CCNE2), and PKC delta (PRKCD). Ingenuity Pathway Analysis revealed that multiple pathways including the p38 Mitogen Activated Protein Kinases (p38 MAPK) signaling pathway were significantly dysregulated by CFTR loss.
Conclusion: We used phosphorylated and un-phosphorylated protein antibody array analysis to identify multiple proteins dysregulated by lack of CFTR. Whether these proteins are important in disease pathogenesis remains to be determined. These studies may provide additional insight into CF disease mechanisms.
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