Bcr-Abl presented a new challenge to treating cancer because of its newly conformed shaped. After some time, Gleevec was invented that acted as a superior treatment compared to previous attempts, earning it the moniker of “wonder drug”. Gleevec was able to competitively bind to the kinase domain on Bcr-Abl that normally bound with a different substrate that allowed it to be phosphorylated and thereby activated. Once Gleevec was introduced, the substrate was no longer able to bind and could no longer be phosphorylated. This rendered the tumor cell unable to proliferate. Because Gleevec acts as an inhibitor does not mean that Bcr-Abl is incapable of binding to the substrate that causes proliferation. It just means that this occurs less frequently. That leads to the possibility of a mutation in Bcr-Abl that increase the activity and allows for an increase in binding to the non-Gleevec substrate. This is one of the potential factors that could lead to resistance of the drug.
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