Global proteomic assessment of the classical protein-tyrosine phosphatome and “Redoxome”
Open accessAbstract
Protein-tyrosine phosphatases (PTPs), along with protein-tyrosine kinases, play key roles in cellular signaling. All Class I PTPs contain an essential active site cysteinyl residue, which executes a nucleophilic attack on substrate phosphotyrosyl residues. The high reactivity of the catalytic cysteine also predisposes PTPs to oxidation by reactive oxygen species, such as H(2)O(2). Reversible PTP oxidation is emerging as an important cellular regulatory mechanism and might contribute to diseases such as cancer. We exploited these unique features of PTP enzymology to develop proteomic methods, broadly applicable to cell and tissue samples, that enable the comprehensive identification and quantification of expressed classical PTPs (PTPome) and the oxidized subset of the PTPome (oxPTPome). We find that mouse and human cells and tissues, including cancer cells, display distinctive PTPomes and oxPTPomes, revealing additional levels of complexity in the regulation of protein-tyrosine phosphorylation in normal and malignant cells.
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The PTP-oxidation pattern can be revealed by a monoclonal antibody that recognizes oxidized cysteine.
“The PTPoxidation pattern can be revealed by a monoclonal antibody that recognizes oxidized cysteine (Karisch et al., 2011).”
From Cellular Senescence: Defining a Path Forward (2019) · cites this paper as Karisch et al., 2011
At high levels, reactive metabolites become toxic and kill cells through damage to the proteome and genome.
“While elevation of reactive metabolites can support oncogenesis in some contexts (Arnold et al., 2001; Irani et al., 1997; Suh et al., 1999; Weinberg et al., 2010), at high levels reactive metabolites become toxic and kill cells due to the resulting damage to the proteome and genome (Karisch et al., 2011; Rabbani and Thornalley, 2014).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Karisch et al., 2011
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References 76 · Cited by 179
- Authors
- Karisch, R., Fernandez, M., Taylor, P., Virtanen, C., St-Germain, J. R., Jin, L. L., Harris, I. S., Mori, J., Mak, T. W., Senis, Y. A., Östman, A., Moran, M. F., & Neel, B. G.
- Affiliations
- University Health Network (CA)
- University of Toronto (CA)
- University of Birmingham (GB)
- Karolinska Institutet (SE)
- Corresponding author
- Karisch, Robert
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2011-09
- Volume
- 146
- Issue
- 5
- Pages
- 826-840
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3176638
- OpenAlex
- W1969277972
- Cited by
- 179
- References
- 76
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 5 · 2023: 8 · 2022: 10 · 2021: 11 · 2020: 7 · 2019: 14 · 2018: 10 · 2017: 17 · 2016: 12 · 2015: 13 · 2014: 18 · 2013: 30 · 2012: 16
- FWCI
- 8.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 685 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
- Funders
- British Heart Foundation (PG/07/034/22 775, FS/08/034/25085)
- Canadian Institutes of Health Research
- National Cancer Institute (R37CA49152, R37CA049152)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- protein tyrosine phosphatase, tyrosine phosphorylation, reactive oxygen species, hydrogen peroxide, protein oxidation, cancer cells
- MeSH terms
- Animals, Cell Line, Humans, Mice, Inbred C57BL, Neoplasms, Oxidation-Reduction, Protein Tyrosine Phosphatases, Proteomics, Mice, Rats
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