| Literature DB >> 28625132 |
Mihwa Kim1, Minwoo Baek1, Dae Joon Kim1.
Abstract
Protein tyrosine phosphorylation is a crucial signaling mechanism that plays a role in epithelial carcinogenesis. Protein tyrosine kinases (PTKs) control various cellular processes including growth, differentiation, metabolism, and motility by activating major signaling pathways including STAT3, AKT, and MAPK. Genetic mutation of PTKs and/or prolonged activation of PTKs and their downstream pathways can lead to the development of epithelial cancer. Therefore, PTKs became an attractive target for cancer prevention. PTK inhibitors are continuously being developed, and they are currently used for the treatment of cancers that show a high expression of PTKs. Protein tyrosine phosphatases (PTPs), the homeostatic counterpart of PTKs, negatively regulate the rate and duration of phosphotyrosine signaling. PTPs initially were considered to be only housekeeping enzymes with low specificity. However, recent studies have demonstrated that PTPs can function as either tumor suppressors or tumor promoters, depending on their target substrates. Together, both PTK and PTP signal transduction pathways are potential therapeutic targets for cancer prevention and treatment. Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.org.Entities:
Keywords: AKT; Carcinogenesis; EGFR; IGF-1R; PTK; PTP; STAT3; tyrosine phosphorylation
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Year: 2017 PMID: 28625132 PMCID: PMC6745708 DOI: 10.2174/1381612823666170616082125
Source DB: PubMed Journal: Curr Pharm Des ISSN: 1381-6128 Impact factor: 3.116