September 2016
Volume 57, Issue 12
Open Access
ARVO Annual Meeting Abstract  |   September 2016
Exploiting proteomics for understanding disease mechanisms
Author Affiliations & Notes
  • Jennifer Van Eyk
    Medicien, Cedars-Sinai Medical Center, Los Angeles, California, United States
  • Footnotes
    Commercial Relationships   Jennifer Van Eyk, Abbott (F), ImmunArray (P), Merck (F)
  • Footnotes
    Support  NIH grants, industry grants from Abbott on traumatic brain injury and Merck for drug development of protein kinase G (neither have impact this talk)
Investigative Ophthalmology & Visual Science September 2016, Vol.57, No Pagination Specified. doi:
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      Jennifer Van Eyk; Exploiting proteomics for understanding disease mechanisms. Invest. Ophthalmol. Vis. Sci. 2016;57(12):No Pagination Specified.

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      © ARVO (1962-2015); The Authors (2016-present)

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Presentation Description : Proteomics involves the quantification of proteins and their proteoforms: isoforms, single nucleotide polymorphorisms and co- and post-translational modifications. Proteoforms exponentially increases the biological diversity of the proteome over that of gene and mRNA. Technical and computational tools to monitor, quantify and access the proteome have continued to develop over time and now have matured to a state where proteomics can and should be applicable to the broader scientific community. There are currently two mass spectrometry-based approaches for discovering differences between experimental groups that can be applied to full proteomes, cellular subcompartments or protein complexes. These methods focus on protein quantification or specific post-translational modifications, the most common being phosphorylation. However, there are many modifications including citrullination, acetylation and SNOylation for which tools have been developed (with more on the way). Each modification can alter secondary messenager signaling pathways and cellular functions but there is growing acknowledge that it is the interplay between these modifications that provides individual variability with respectd to disease severity and differences in a patient's response to a perturbation or therapy. Targeted proteomics methods like multiple reaction monitoring allow for precise quantification of specific proteins or selected modified amino acid residue(s) and are as accurate as ELISA based method but are more easily multiplexed. Targeted based methods can be used in research (replacing western blots) and clinical laboratory to precisely measure up to 100 proteins or their proteotype in samples. Introduction of sample preparation automation allows the analysis of 100s of samples in both discovery and targeted approaches opening up our ablity to address epidemiological scale questions. In summary, proteomics technologies and approaches can and have been used to address key biological and clinical questions and are at point where broad application of these approaches within the scientific community would be transformative.

This is an abstract that was submitted for the 2016 ARVO Annual Meeting, held in Seattle, Wash., May 1-5, 2016.


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