The C-Kit Receptor-Mediated Signal Transduction and Tumor-Related Diseases
Open Access
- 1 January 2013
- journal article
- review article
- Published by Ivyspring International Publisher in International Journal of Biological Sciences
- Vol. 9 (5) , 435-443
- https://doi.org/10.7150/ijbs.6087
Abstract
As an important member of tyrosine kinase family, c-kit receptor causes specific expression of certain genes, regulates cell differentiation and proliferation, resists cell apoptosis, and plays a key role in tumor occurrence, development, migration and recurrence through activating the downstream signaling molecules following interaction with stem cell factor (SCF). The abnormality of SCF/c-kit signaling pathway is closely related to some certain tumors. The discovery of c-kit receptor-targeted drugs has promoted clinical-related cancer's diagnosis and treatment. In this paper, we review recent research progress on c-kit receptor-mediated signal transduction and its potential therapeutic application as a target in tumor-related diseases.Keywords
This publication has 46 references indexed in Scilit:
- Targeting G-Quadruplex Structure in the Human c-Kit Promoter with Short PNA SequencesBioconjugate Chemistry, 2011
- Regulation of lymphocyte fate by Ras/ERK signalsCell Cycle, 2008
- Structural Basis for Activation of the Receptor Tyrosine Kinase KIT by Stem Cell FactorCell, 2007
- Gastrointestinal Stromal Tumors of the Jejunum and IleumThe American Journal of Surgical Pathology, 2006
- Treatment for Advanced Tumors: Src Reclaims Center StageClinical Cancer Research, 2006
- Soft tissue sarcomas of adults: state of the translational science.2003
- Structure, binding, and antagonists in the IL-4/IL-13 receptor systemBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2002
- The c-KIT mutation causing human mastocytosis is resistant to STI571 and other KIT kinase inhibitors; kinases with enzymatic site mutations show different inhibitor sensitivity profiles than wild-type kinases and those with regulatory-type mutationsBlood, 2002
- Human Stem Cell Factor Dimer Forms a Complex with Two Molecules of the Extracellular Domain of Its Receptor, KitJournal of Biological Chemistry, 1996
- Molecular Basis of Human Piebaldism.Journal of Investigative Dermatology, 1994