Using mass spectrometry to analyze the aging population

The complex physiological process of aging represents many problems among rapidly aging populations. One well recognized consequence of aging is degradation of immune function, which is referred to as immunosenescence.

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Although elderly people are by no means immunodeficient, their response to new or previously encountered antigens is often inefficient. Immunosenescence is partially accountable for the increased susceptibility the elderly have to infection, as well as their poor response to vaccination. Both the adaptive and innate branches of the immune system are affected, but the molecular mechanisms involved are still not clear.

At this year’s Pittcon, the leading conference and exposition for laboratory science, more than 2,000 presentations will be held, providing an unmissable opportunity to hear about the latest findings in laboratory science. The topic of aging populations will be discussed, with an emphasis on how mass spectrometry is used to study age-related changes in response to infection.

Proteomic analysis of aging

Proteomics is the large-scale study of thousands of proteins within one experiment. It involves the qualitative, quantitative and functional characterization of all proteins within a given cell, tissue and/or organism. The simultaneous study of many proteins enables a more “systems biology” approach to mapping protein content, crosstalk and activation to a particular time point, for a particular condition.

For example, it is possible to screen for proteins that are differentially expressed between healthy and diseased tissue, which can help to improve diagnosis, monitoring of therapy and drug design. Native proteins may be profiled, as well as their isoforms, splice variants, and post-translationally modified species. Interactions between proteins may also be determined.

Mass-spectrometry based proteomics

The past two decades have seen remarkable advances in the field of proteomics. Mass spectrometry has emerged as the method of choice for characterizing protein components found in biological systems. The technique has led to important insights into the make-up, regulation and function of molecular complexes and pathways.

Mass spectrometry-based proteomics has become a powerful tool that can be combined with molecular, cellular and pharmacological techniques to translate large sets of data and elucidate complex biological processes.

At Pittcon 2017, major suppliers of mass spectrometry equipment will be showcasing their world-leading products. Among the exhibitors will be Bruker, Thermo Fisher Scientific, Waters, Shimazdu and PerkinElmer, making Pittcon an invaluable opportunity to learn about the latest technical advances in the field of mass spectrometry. This year’s Pittcon conference is being held in Chicago, Illinois between the 5th and 9th March.

Mass spectrometry in aging research

In a 2012 proteomics study by Lisa Staunton and colleagues, tissue specimens derived from middle-aged (47 to 62 years) and aged (76-82 years) individuals were compared for potential changes in protein expression profiles. The study revealed age-dependent changes in the concentration of 19 protein spots. Mass spectrometry showed that these components were involved in muscle fiber contraction, muscle metabolism, ion handling and the cellular stress response, indicating a disrupted pattern of protein expression in senescent human muscle.

A 2014 study by Paczek et al examined urine proteomes derived from 37 healthy individuals, aged 19 to 90 years, to explore which metabolic processes were weakened or enhanced as people age. Protein expression analysis by liquid chromatography–tandem mass spectrometry showed the differential expression of 19 proteins between young (19 to 26 years), intermediate (45 to 54 years) and old (72 to 90) age groups. Importantly, protein changes in the oldest group were reflective of altered extracellular matrix turnover and deteriorating immune function, changes that were in keeping with reported alterations in cardiovascular tissue remodeling and immune conditions among the elderly.

Caenorhabditis elegans (C. elegans) as a model for regulation of aging and innate immunity

C. elegans is a nematode that lives in the soil of temperate regions, where it feeds on bacteria. It is a major model in the study of a number of fields including developmental biology, apoptosis and aging. The worm has been shown to possess an inducible innate system and has become an important model for elucidating the mechanisms involved in innate immunity. Interestingly, it has also been shown that the regulation of aging and innate immunity in C. elegans seem to overlap.

Characterization of this nematode’s innate immune system suggests that certain immune system components are conserved in metazoans. The study of immunosenescence in C. elegans is likely to provide important insights into how immunity is affected as the nematode ages. This could help researchers to understand, at the cellular and molecular level, the reciprocal effects of aging and immunity on each other and how these may be relevant to humans.

At Pittcon 2017, we will hear from mass spectrometry and proteomics expert Renã Robinson about C. elegans as a model for following age-related, proteome-wide changes that occur in response to opportunistic pathogenic infection. An overview of mass spectrometry applications to aging will be given, including a demonstration of how there is a significant influence on host response due to aging in C. elegans.

For all this and more, do not miss out on the Pittcon conference in Chicago this March!

Mass Spectrometry in Proteomics from AZoNetwork on Vimeo.

References

  • Dorshkind K, et al. Causes, consequences, and reversal of immune system aging. J Clin Invest. 2013;123(3):958–965
  • Paczek L, et al. Urine proteomes of healthy aging humans reveal extracellular matrix (ECM) alterations and immune system dysfunction. Age (Dordr)2014;36(1): 299–311
  • Staunton L, et al. Mass spectrometry-based proteomic analysis of middle-aged vs. aged vastus lateralis reveals increased levels of carbonic anhydrase isoform 3 in senescent human skeletal muscle. Int J Mol Med 2012;30(4): 723–733
  • Ermolaeva M and Schumacher B. Insights from the worm: The C. elegans model for innate immunity. Semin Immunol 2014;26(4):303–309
  • Dansen TB, et al. Proteome-wide Changes in Protein Turnover Rates in C. elegans Models of Longevity and Age-Related Disease. Cell Rep 2016;16(11):3041–51
  • Weiskopf D, et al. The aging of the immune system. Transplant International 2009;22:1041–1050

Last updated: Feb 8, 2017 at 10:54 AM

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