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Proteomic Profiling of Protein-Protein Interactions of Alpha-1 Antitrypsin in Plasma
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A4751 - Proteomic Profiling of Protein-Protein Interactions of Alpha-1 Antitrypsin in Plasma
Author Block: A. Dabo1, E. Eden2, R. F. Foronjy1, P. Geraghty1; 1SUNY Downstate Medical Center, Brooklyn, NY, United States, 2St Lukes-Roosevelt Hosp Ctr, New York, NY, United States.
Introduction/rationale to the study: Proteomics technology is utilized to characterization protein structure, function and protein-protein interactions. Alpha1-antitrypsin (AAT) is known to complex with several proteins in the plasma, including trypsin, alpha-chymotrypsin and neutrophil elastase. Here, we characterize protein interactions with AAT protein, isolated from PiMM and PiZZ subjects, by mass spectrometry (MS) analysis to identify unique AAT-dependent pathways. Methods used: In this study, plasma AAT was purified from 4 healthy AAT deficient subjects (PiZZ) not receiving AAT augmentation therapy and 4 aged-match PiMM controls by affinity chromatography. Global proteomic profiling was performed on equal concentrations of PiMM and PiZZ AAT protein and bound unknown protein utilizing an ultra-high-pressure liquid chromatography approach coupled to a high resolution, high mass accuracy quadrupole-Orbitrap MS (www.Bioproximity.com). Proteins corresponding to detected peptides were characterized using several protein sequence libraries. Identified proteins were grouped by biological function and predicted processes. Results of the study: AAT was observed to bind to over 3,000 peptide sequences unique to 206 proteins in the plasma. The AAT protein isolated from the PiMM genotype subjects bound to peptides associated with 201 proteins and the PiZZ form bound to peptides identified as 127 proteins. Interestingly, 79 proteins interacted with the PiMM AAT but not the PiZZ AAT protein. Equally, 5 proteins bound to the PiZZ AAT protein and not the PiZZ form of AAT. AAT interacting proteins are involved in multiple different biological processes, such as adhesion, regulation, growth, immune responses, locomotion, metabolism, stimuli responses, reproduction, localization and developmental. Conclusions of the study: AAT is interacting with numerous proteins, which suggests that AAT may have many functional roles in addition to its anti-protease definition. Equally, the mutated forms of AAT requires further protein-protein interaction analysis to determine the functional role of its unique protein-protein interactions.
Author Block: A. Dabo1, E. Eden2, R. F. Foronjy1, P. Geraghty1; 1SUNY Downstate Medical Center, Brooklyn, NY, United States, 2St Lukes-Roosevelt Hosp Ctr, New York, NY, United States.
Introduction/rationale to the study: Proteomics technology is utilized to characterization protein structure, function and protein-protein interactions. Alpha1-antitrypsin (AAT) is known to complex with several proteins in the plasma, including trypsin, alpha-chymotrypsin and neutrophil elastase. Here, we characterize protein interactions with AAT protein, isolated from PiMM and PiZZ subjects, by mass spectrometry (MS) analysis to identify unique AAT-dependent pathways. Methods used: In this study, plasma AAT was purified from 4 healthy AAT deficient subjects (PiZZ) not receiving AAT augmentation therapy and 4 aged-match PiMM controls by affinity chromatography. Global proteomic profiling was performed on equal concentrations of PiMM and PiZZ AAT protein and bound unknown protein utilizing an ultra-high-pressure liquid chromatography approach coupled to a high resolution, high mass accuracy quadrupole-Orbitrap MS (www.Bioproximity.com). Proteins corresponding to detected peptides were characterized using several protein sequence libraries. Identified proteins were grouped by biological function and predicted processes. Results of the study: AAT was observed to bind to over 3,000 peptide sequences unique to 206 proteins in the plasma. The AAT protein isolated from the PiMM genotype subjects bound to peptides associated with 201 proteins and the PiZZ form bound to peptides identified as 127 proteins. Interestingly, 79 proteins interacted with the PiMM AAT but not the PiZZ AAT protein. Equally, 5 proteins bound to the PiZZ AAT protein and not the PiZZ form of AAT. AAT interacting proteins are involved in multiple different biological processes, such as adhesion, regulation, growth, immune responses, locomotion, metabolism, stimuli responses, reproduction, localization and developmental. Conclusions of the study: AAT is interacting with numerous proteins, which suggests that AAT may have many functional roles in addition to its anti-protease definition. Equally, the mutated forms of AAT requires further protein-protein interaction analysis to determine the functional role of its unique protein-protein interactions.
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