Precision Profiling of the Cardiovascular Post-Translationally Modified Proteome: Where There Is a Will, There Is a Way

Circ Res. 2018 Apr 27;122(9):1221-1237. doi: 10.1161/CIRCRESAHA.118.310966.


There is an exponential increase in biological complexity as initial gene transcripts are spliced, translated into amino acid sequence, and post-translationally modified. Each protein can exist as multiple chemical or sequence-specific proteoforms, and each has the potential to be a critical mediator of a physiological or pathophysiological signaling cascade. Here, we provide an overview of how different proteoforms come about in biological systems and how they are most commonly measured using mass spectrometry-based proteomics and bioinformatics. Our goal is to present this information at a level accessible to every scientist interested in mass spectrometry and its application to proteome profiling. We will specifically discuss recent data linking various protein post-translational modifications to cardiovascular disease and conclude with a discussion for enablement and democratization of proteomics across the cardiovascular and scientific community. The aim is to inform and inspire the readership to explore a larger breadth of proteoform, particularity post-translational modifications, related to their particular areas of expertise in cardiovascular physiology.

Keywords: cardiovascular diseases; mass spectrometry; post-translational protein modifications; proteome; proteomics.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Cardiovascular Diseases / genetics
  • Cardiovascular Physiological Phenomena
  • Cardiovascular System / metabolism
  • Chromatography, Liquid
  • Humans
  • Protein Processing, Post-Translational*
  • Proteins / analysis
  • Proteome / genetics*
  • Proteomics / methods*
  • Tandem Mass Spectrometry


  • Proteins
  • Proteome