Protein tyrosine kinases (TKs) are enzymes that catalyze thetransfer of phosphate from ATP to tyrosine residues in polypeptides.The human genome contains about 90 TK and 43 TK-like genes,the products of which regulate cellular proliferation, survival,differentiation, function, and motility. More than 25 yearsago, TKs were implicated as oncogenes in animal tumors inducedby retroviruses. However, they were largely ignored in drugdevelopment because of a paucity of evidence for a causativerole in human cancer and concerns about drug specificity andtoxicity. The landscape was changed radically by the successof imatinib mesylate, an inhibitor of . . . [Full Text of this Article]
TK Regulation, Dysregulation, and Therapeutic Targeting
Regulation of Normal TK Activity
Mechanisms of TK Dysregulation in Cancer
Strategies to Target TKs in Cancer Therapy
TKs as Targets in the Treatment of Malignant Hematologic Disorders
Imatinib Mesylate: The First Successful Small-Molecule TK Inhibitor
FLT3: A Major TK Target in AML
Other TK Targets in Malignant Hematologic Disorders
The Dramatic Response of CML to Kinase Inhibition: The Rule or an Exception?
TKs as Targets for Therapy of Solid Tumors
Imatinib Targets in Solid Tumors: GIST and Beyond
Small-Molecule Inhibitors of EGFR
Targeting Receptor TKs and Their Ligands with Monoclonal Antibodies
Other TK Targets in Solid Tumors
Current Challenges and Future Directions
Limitations of TK-Targeted Therapies: Toxicity and Resistance
Strategies to Identify New TK Targets in Cancer
Are Changes in the Drug-Development Process Needed for TK-Targeted Therapies?
Source Information
From the Molecular Oncology Research Institute (D.S.K., R.A.V.) and the Division of Hematology–Oncology, Department of Medicine (R.A.V.), Tufts–New England Medical Center, Boston.
Address reprint requests to Dr. Van Etten at Tufts–New England Medical Center, 750 Washington St., Box 5609, Boston, MA 02111, or at rvanetten@tufts-nemc.org.
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