Blocking of EGF-dependent cell proliferation by EGF receptor kinase inhibitors.

Science (New York, N.Y.) (1988-11-11)
P Yaish, A Gazit, C Gilon, A Levitzki
RESUMEN

A systematic series of low molecular weight protein tyrosine kinase inhibitors were synthesized; they had progressively increasing affinity over a 2500-fold range toward the substrate site of epidermal growth factor (EGF) receptor kinase domain. These compounds inhibited EGF receptor kinase activity up to three orders of magnitude more than they inhibited insulin receptor kinase, and they also effectively inhibited the EGF-dependent autophosphorylation of the receptor. The most potent compounds effectively inhibited the EGF-dependent proliferation of A431/clone 15 cells with little or no effect on the EGF-independent proliferation of these cells. The potential use of tyrosine protein kinase inhibitors as antiproliferative agents is demonstrated.

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Sigma-Aldrich
Tyrphostin 23, ≥98%
Sigma-Aldrich
Tyrphostin 1, ≥98%
Sigma-Aldrich
Tyrphostin 51, ≥98%

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