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Influence of Tyrosine Kinase Inhibition on Organic Anion Transporting Polypeptide 1B3-Mediated Uptake
Vusumuzi N Hove1, Kenneth Anderson1, Elizabeth R Hayden1
1Department of Pharmaceutical Sciences, School of Pharmacy and Pharmaceutical Sciences (V.N.H., K.A., E.R.H., K.Z.P., S.S., J.Q., J.A.S.) and Department of Biostatistics (J.C.M.), University at Buffalo, State University of New York, Buffalo, New York and Division of Pharmaceutics and Pharmacology, College of Pharmacy and Comprehensive Cancer Center, The Ohio State University, Columbus, Ohio (A.A.G., Y.J., S.H.).
Abstract:
The organic anion transporting polypeptide family member (OATP) 1B3 is a hepatic uptake transporter that has a broad substrate recognition and plays a significant role in regulating elimination of endogenous biomolecules or xenobiotics. OATP1B3 works in tandem with OATP1B1, with which it shares approximately 80% sequence homology and a high degree of substrate overlap. Despite some substrates being recognized solely by OATP1B3, its ability to compensate for loss of OATP1B1-mediated elimination and recognition by regulatory agencies, little is known about OATP1B3 regulatory factors and how they are involved with drug-drug interaction. It was recently discovered that OATP1B1 function is mediated by the activity of a particular tyrosine kinase that is sensitive to a variety of tyrosine kinase inhibitors (TKIs). This study reports that OATP1B3 is similarly regulated, as at least 50% of its activity is reduced by 20 US Food and Drug Administration -approved TKIs. Nilotinib was assessed as the most potent OATP1B3 inhibitor among the investigated TKIs, which can occur at clinically relevant concentrations and acted predominantly through noncompetitive inhibition without impacting membrane expression. Finally, OATP1B3 function was determined to be sensitive to the knockdown of the Lck/Yes novel tyrosine kinase that is sensitive to nilotinib and has been previously implicated in mediating OATP1B1 activity. Collectively, our findings identify tyrosine kinase activity as a major regulator of OATP1B3 function which is sensitive to kinase inhibition. Given that OATP1B1 is similarly regulated, simultaneous disruption of these transporters can have drastic effects on systemic drug concentrations, which would promote adverse events. SIGNIFICANCE STATEMENT: The organic anion transporting polypeptide family member (OATP) 1B3 is a facilitator of hepatic drug elimination, although much is unknown of how OATP1B3 activity is mediated, or how such regulators contribute to drug-drug interactions. This study reports that OATP1B3 activity is dependent on the Lck/Yes novel tyrosine kinase, which is sensitive to numerous tyrosine kinase inhibitors. These findings provide insight into the occurrence of many clinical drug-drug interactions, and a rationale for future study of tyrosine kinases regulating drug disposition.
Insights
Organic anion transporting polypeptide 1B3 (OATP1B3) activity is regulated by tyrosine kinases, similar to OATP1B1. This discovery explains drug-drug interactions and highlights the impact of tyrosine kinase inhibitors on drug elimination.
Area of Science:
- Pharmacology
- Biochemistry
- Drug Metabolism
Background:
- Organic anion transporting polypeptide 1B3 (OATP1B3) is a key hepatic uptake transporter involved in eliminating endogenous compounds and xenobiotics.
- OATP1B3 shares functional similarities and substrate overlap with OATP1B1, but its regulatory factors and role in drug-drug interactions remain less understood.
- Recent findings indicate OATP1B1 function is modulated by tyrosine kinase activity, suggesting a potential similar mechanism for OATP1B3.
Purpose of the Study:
- To investigate the regulatory role of tyrosine kinases in OATP1B3 function.
- To identify specific tyrosine kinase inhibitors (TKIs) that affect OATP1B3 activity.
- To elucidate the mechanism by which TKIs impact OATP1B3-mediated transport.
Main Methods:
- Screening of 20 US Food and Drug Administration-approved TKIs for their effect on OATP1B3 activity.
- Assessing the inhibitory potency and mechanism of action of the most effective TKI, nilotinib.
- Investigating the role of Lck/Yes novel tyrosine kinase through knockdown experiments.
Main Results:
- At least 50% of OATP1B3 activity was reduced by 20 tested TKIs.
- Nilotinib demonstrated potent, noncompetitive inhibition of OATP1B3 at clinically relevant concentrations, without affecting membrane expression.
- OATP1B3 function was sensitive to the knockdown of Lck/Yes novel tyrosine kinase, which is also targeted by nilotinib.
Conclusions:
- Tyrosine kinase activity is a significant regulator of OATP1B3 function, susceptible to inhibition by TKIs.
- The similar regulation of OATP1B1 and OATP1B3 by tyrosine kinases suggests that combined inhibition could drastically alter systemic drug concentrations.
- These findings provide crucial insights into drug-drug interactions and the role of tyrosine kinases in drug disposition.
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