Platelet-derived growth factor (PDGF) receptor activation in cell transformation and human malignancy
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Cited by (18)
Tenascin-C-derived peptide TNIIIA2 highly enhances cell survival and Platelet-derived Growth Factor (PDGF)-dependent cell proliferation through potentiated and sustained activation of integrin α5β1
2014, Journal of Biological ChemistryCitation Excerpt :The present study showed an attenuation of contact inhibition in cell proliferation by TNIIIA2 in both a PDGF- and integrin α5β1-dependent manner. Of note, previous studies demonstrated that, on forced expression of PDGF, NIH3T3 cells undergo a loss of contact-inhibited growth and acquire the ability to grow in soft agar and form tumors in nude mice as a result of autocrine signaling (52, 53). Because coordinated input from RTKs and integrins is necessary for cell cycle progression and proliferation and because both types of receptors activate common members of the Ras/MAP kinase signaling pathway, it is not surprising that sustained activation of integrin α5β1 by TNIIIA2, in the presence of added PDGF, leads to the same result as that induced by stable expression of PDGF.
Protein tyrosine kinases and cancer
1997, Biochimica et Biophysica Acta - Reviews on CancerDiscovery of High-Affinity PDGF-VEGFR Interactions: Redefining RTK Dynamics
2017, Scientific ReportsOlaratumab for soft tissue sarcoma
2017, Expert Opinion on Biological Therapy