The protein tyrosine kinase inhibitors imatinib and nilotinib strongly inhibit several mammalian alpha-carbonic anhydrase isoforms.

Article Details

Citation

Parkkila S, Innocenti A, Kallio H, Hilvo M, Scozzafava A, Supuran CT

The protein tyrosine kinase inhibitors imatinib and nilotinib strongly inhibit several mammalian alpha-carbonic anhydrase isoforms.

Bioorg Med Chem Lett. 2009 Aug 1;19(15):4102-6. doi: 10.1016/j.bmcl.2009.06.002. Epub 2009 Jun 6.

PubMed ID
19527930 [ View in PubMed
]
Abstract

The protein tyrosine kinases (PTKs) are essential enzymes in cellular signaling processes that regulate cell growth, differentiation, migration and metabolism. Their inhibition was recently shown to constitute a new modality for treating cancers. Two clinically used PTK inhibitors (PTKIs), imatinib (Glivec/Gleevec) and nilotinib (Tasigna) were investigated for their effects on the zinc enzymes carbonic anhydrases (CAs, EC 4.2.1.1). The two PTKIs inhibited all 13 catalytically active mammalian isoforms CA I-XV with K(I)s in the range of 4.1nM-20.2microM. CA I and CA II were the most potently inhibited isoforms (K(I)s of 4-32nM), whereas CA VA and VB showed the lowest affinity for these drugs (K(I)s of 5.4-20.2microM). In cancer cells, these inhibitors may interact with CAs in addition to the targets for which they were designed, the PTKs.

DrugBank Data that Cites this Article

Binding Properties
DrugTargetPropertyMeasurementpHTemperature (°C)
AcetazolamideCarbonic anhydrase 1Ki (nM)250N/AN/ADetails
AcetazolamideCarbonic anhydrase 12Ki (nM)5.7N/AN/ADetails
AcetazolamideCarbonic anhydrase 14Ki (nM)41N/AN/ADetails
AcetazolamideCarbonic anhydrase 2Ki (nM)12N/AN/ADetails
AcetazolamideCarbonic anhydrase 3Ki (nM)200000N/AN/ADetails
AcetazolamideCarbonic anhydrase 4Ki (nM)74N/AN/ADetails
AcetazolamideCarbonic anhydrase 7Ki (nM)2.5N/AN/ADetails