Mass spectrometry based proteomics analyses in kallikrein-related peptidase research: implications for cancer research and therapy.

Expert Rev Proteomics 2017 12 17;14(12):1119-1130. Epub 2017 Oct 17.

b School of Biomedical Sciences , Institute of Health and Biomedical Innovation (IHBI), Queensland University of Technology (QUT), Translational Research Institute , Woolloongabba , Australia.

Introduction: Kallikrein-related peptidases (KLKs) are a family of serine peptidases that are deregulated in numerous pathological conditions, with a multitude of KLK-mediated functional roles implicated in the progression of cancer. Advances in multidimensional mass spectrometry (MS)-based proteomics have facilitated the quantitative measurement of deregulated KLK expression in cancer, identifying certain KLKs, as well as their substrates, as potential cancer biomarkers. Areas covered: In this review, we discuss how these approaches have been utilized for KLK biomarker discovery and unbiased substrate determination in complex protein pools that mimic the in vivo extracellular microenvironment. Expert commentary: Although a limited number of studies have been performed, the quantity of information generated has greatly improved our understanding of the functional roles of KLKs in cancer progression. In addition, these data suggest additional means through which deregulated KLK expression may be targeted in cancer treatment, highlighting the potential therapeutic value of these state-of-the-art MS-based studies.

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http://dx.doi.org/10.1080/14789450.2017.1389637DOI Listing
December 2017
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