Proteomic and other analyses to determine the functional consequences of deregulated kallikrein-related peptidase (KLK) expression in prostate and ovarian cancer

Rapidly developing proteomic tools are improving detection of deregulated kallikrein‐related peptidase (KLK) expression, at the protein level, in prostate and ovarian cancer, as well as facilitating the determination of functional consequences downstream. MS‐driven proteomics uniquely allows for the...

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Bibliographic Details
Published in:Proteomics. Clinical applications 2014-06, Vol.8 (5-6), p.403-415
Main Authors: Fuhrman-Luck, Ruth Anna, Silva, Munasinghage Lakmali, Dong, Ying, Irving-Rodgers, Helen, Stoll, Thomas, Hastie, Marcus Lachlan, Loessner, Daniela, Gorman, Jeffrey John, Clements, Judith Ann
Format: Article
Language:English
Subjects:
Cancer
Degradomics
Female
Gene Expression Regulation, Neoplastic
Humans
Kallikrein
Kallikreins - biosynthesis
Kallikreins - metabolism
Male
Medical research
Ovarian cancer
Ovarian Neoplasms - drug therapy
Ovarian Neoplasms - enzymology
Ovarian Neoplasms - genetics
Prostatic Neoplasms - drug therapy
Prostatic Neoplasms - enzymology
Prostatic Neoplasms - genetics
Protease
Proteins
Proteomics - methods
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Summary:Rapidly developing proteomic tools are improving detection of deregulated kallikrein‐related peptidase (KLK) expression, at the protein level, in prostate and ovarian cancer, as well as facilitating the determination of functional consequences downstream. MS‐driven proteomics uniquely allows for the detection, identification, and quantification of thousands of proteins in a complex protein pool, and this has served to identify certain KLKs as biomarkers for these diseases. In this review, we describe applications of this technology in KLK biomarker discovery and elucidate MS‐based techniques that have been used for unbiased, global screening of KLK substrates within complex protein pools. Although MS‐based KLK degradomic studies are limited to date, they helped to discover an array of novel KLK substrates. Substrates identified by MS‐based degradomics are reported with improved confidence over those determined by incubating a purified or recombinant substrate and protease of interest, in vitro. We propose that these novel proteomic approaches represent the way forward for KLK research, in order to correlate proteolysis of biological substrates with tissue‐related consequences, toward clinical targeting of KLK expression and function for cancer diagnosis, prognosis, and therapies.
ISSN:1862-8346
1862-8354
DOI:10.1002/prca.201300098