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The 3A mutation in GAP-F5 protein effectively blocks the increase in G2019S LRRK2-mediated phosphorylation in response to increasing amounts of GAP-F5 protein substrate, compared to the concentration-dependent increase in WT GAP-F5 phosphorylation, by in vitro radioactive kinase assay (Figure 2E)

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Hence, heterogeneity in islet size and cellular composition should be taken into consideration

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These two drugs are multi-kinase inhibitors, however, so it is difficult to draw conclusions about whether the positive results were associated with their MET activity