Detecting Cardiovascular Protein-Protein Interactions by Proximity Proteomics.
Rapidly changing and transient protein-protein interactions regulate dynamic cellular processes in the cardiovascular system. Traditional methods, including affinity purification and mass spectrometry, have revealed many macromolecular complexes in cardiomyocytes and the vasculature. Yet these methods often fail to identify in vivo or transient protein-protein interactions. To capture these interactions in living cells and animals with subsequent mass spectrometry identification, enzyme-catalyzed proximity labeling techniques have been developed in the past decade. Although the application of this methodology to cardiovascular research is still in its infancy, the field is developing rapidly, and the promise is substantial. In this review, we outline important concepts and discuss how proximity proteomics has been applied to study physiological and pathophysiological processes relevant to the cardiovascular system.
Duke Scholars
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Related Subject Headings
- Proteomics
- Proteome
- Protein Interaction Maps
- Protein Interaction Mapping
- Myocardium
- Humans
- Cardiovascular System & Hematology
- Animals
- 3202 Clinical sciences
- 3201 Cardiovascular medicine and haematology
Citation
Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Proteomics
- Proteome
- Protein Interaction Maps
- Protein Interaction Mapping
- Myocardium
- Humans
- Cardiovascular System & Hematology
- Animals
- 3202 Clinical sciences
- 3201 Cardiovascular medicine and haematology