期刊
CANCER AND METASTASIS REVIEWS
卷 27, 期 2, 页码 263-272出版社
SPRINGER
DOI: 10.1007/s10555-008-9113-3
关键词
protein tyrosine phosphatase (PTP); PTP1B; SHP2; Cdc25; PRL phosphatases; small molecule inhibitor design; PTP inhibitor
类别
资金
- NCI NIH HHS [R01 CA069202, CA 69202, R01 CA069202-13] Funding Source: Medline
- NIDDK NIH HHS [R01 DK068447, R01 DK068447-03, DK 68447] Funding Source: Medline
Protein tyrosine phosphorylation plays a major role in cellular signaling. The level of tyrosine phosphorylation is controlled by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). Disturbance of the normal balance between PTK and PTP activity results in aberrant tyrosine phosphorylation, which has been linked to the etiology of several human diseases, including cancer. A number of PTPs have been implicated in oncogenesis and tumor progression and therefore are potential drug targets for cancer chemotherapy. These include PTP1B, which may augment signaling downstream of HER2/Neu; SHP2, which is the first oncogene in the PTP superfamily and is essential for growth factor-mediated signaling; the Cdc25 phosphatases, which are positive regulators of cell cycle progression; and the phosphatase of regenerating liver (PRL) phosphatases, which promote tumor metastases. As PTPs have emerged as drug targets for cancer, a number of strategies are currently been explored for the identification of various classes of PTP inhibitors. These efforts have resulted many potent, and in some cases selective, inhibitors for PTP1B, SHP2, Cdc25 and PRL phosphatases. Structural information derived from these compounds serves as a solid foundation upon which novel anti-cancer agents targeted to these PTPs can be developed.
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