Unbiased and targeted mass spectrometry for the HDL proteome. Issue 1 (February 2017)

• Record Type: Journal Article
• Authors: Singh, Sasha A.; Aikawa, Masanori
• Is Part Of: Current opinion in lipidology. Volume 28:Issue 1(2017:Feb.)
• Publication Date: 2017-02
• Subjects: apolipoprotein -- label-free -- multiple reaction monitoring -- parallel reaction monitoring -- spectral counting -- stable isotopes; Lipids -- Periodicals; 572.574
• DOI: 10.1097/MOL.0000000000000374
• Languages: English
• ISSNs: 1473-6535

Abstract

Abstract : Purpose of review: Mass spectrometry is an ever evolving technology that is equipped with a variety of tools for protein research. Some lipoprotein studies, especially those pertaining to HDL biology, have been exploiting the versatility of mass spectrometry to understand HDL function through its proteome. Despite the role of mass spectrometry in advancing research as a whole, however, the technology remains obscure to those without hands on experience, but still wishing to understand it. In this review, we walk the reader through the coevolution of common mass spectrometry workflows and HDL research, starting from the basic unbiased mass spectrometry methods used to profile the HDL proteome to the most recent targeted methods that have enabled an unprecedented view of HDL metabolism. Recent findings: Unbiased global proteomics have demonstrated that the HDL proteome is organized into subgroups across the HDL size fractions providing further evidence that HDL functional heterogeneity is in part governed by its varying protein constituents. Parallel reaction monitoring, a novel targeted mass spectrometry method, was used to monitor the metabolism of HDL apolipoproteins in humans and revealed that apolipoproteins contained within the same HDL size fraction exhibit diverse metabolic properties. Summary: Mass spectrometry provides a variety of tools and strategies to facilitate understanding, through its proteins, the complex biology of HDL.