Journal
JOURNAL OF PROTEOME RESEARCH
Volume 13, Issue 12, Pages 5869-5878Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr5007685
Keywords
Bioinformatics; chamber specificity; fetal tissue; mass spectrometry; ventricle; Q-exactive
Categories
Funding
- Canadian Institutes of Health Research [MOP-106538, GPG-102166]
- Heart and Stroke Foundation of Ontario [T-6281, NS-6636]
- Ontario Research Fund Global Leadership Round in Genomics and Life Sciences [GL2-01012]
- Canada Research Chair in Cardiovascular Proteomics and Molecular Therapeutic
- Ontario Graduate Scholarship in Science and Technology
- Department of Medical Biophysics Excellence Award
- Kristi Piia CALLUM Memorial Fellowship
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In this study we carried out a mass spectrometry-based proteome analysis of human fetal atria and ventricles. Heart protein lysates were analyzed on the Q-Exactive mass spectrometer in biological triplicates. Protein identification using MaxQuant yielded a total of 2754 atrial protein groups (91%) and 2825 ventricular protein groups (83%) in at least 2 of the 3 runs with >= 2 unique peptides. Statistical analyses using fold-enrichment (>2) and p-values (<= 0.05) selected chamber-enriched atrial (134) and ventricular (81) protein groups. Several previously characterized cardiac chamber-enriched proteins were identified in this study including atrial isoform of myosin light chain 2 (MYL7), atrial natriuretic peptide (NPPA), connexin 40 (GJA5), and peptidylglycine alpha-amidating monooxygenase (PAM) for atria, and ventricular isoforms of myosin light chains (MYL2 and MYL3), myosin heavy chain 7 (MYH7), and connexin 43 (GJA1) for ventricle. Our data was compared to in-house generated and publicly available human microarrays, several human cardiac proteomes, and phenotype ontology databases.
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