The History of Modern Quantitative Proteomics
In the past 18 years, proteomics research in the life sciences and medicine has flourished since Australian scientists Marc Wilkins (geneticist) and Keith L. Williams put forward the concept of proteomics in 1994. Especially, it gives a huge contribution to cardiac cerebral vascular disease, cancer, diabetes and other major diseases. The pathway of conventional 2DE-MS analysis has inherent limitations that the resolution is not high, poor reproducibility, and serious bias factor that restricting the further development of proteomics. So quantitative proteomics is gradually put forward.
In 1999, there were two important papers published that played a crucial role in the development of modern quantitative proteomics:
One was from Ruedi Aebersold’s group. The paper introduced the technology of Isotope-coded affinity tag (ICAT), which using a reagent with heavy or light isotopes and a biotin affinity tag can modify cysteine containing peptides. Aebersold’s group applied this technology to Saccharomyces cerevisiae cells successfully, then inspired many scientists to focus on quantification by labeling peptides and proteins. The other paper was form Brian Chait’s group. They used whole cell stable isotope to label Saccharomyces cerevisiae cells. Both technologies are stable in labeling proteins and peptides that allow scientists to detect the quantitative changes in proteins, which laid foundation for quantitative proteomics.
Both label-free or labeled quantitative proteomics, they get the data from the mass spectrometer.
Quantitative proteomics is a subject of precise quantification and identification of total protein expression in a genome or a complex hybrid system. The proposing of the concept marks of proteomic technology continues to improve and perfect. Proteomics research from simple qualitative development of protein to precise quantitative direction.
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