Inhibition of P-glycoprotein and multidrug resistance-associated proteins modulates the intracellular concentration of lopinavir in cultured CD4 T cells and primary human lymphocytes
Author(s) -
Omar Janneh,
E. Jones,
Becky Chandler,
Andrew Owen,
Saye Khoo
Publication year - 2007
Publication title -
journal of antimicrobial chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.124
H-Index - 194
eISSN - 1460-2091
pISSN - 0305-7453
DOI - 10.1093/jac/dkm353
Subject(s) - lopinavir , ritonavir , atazanavir , multidrug resistance associated protein 2 , amprenavir , efflux , pharmacology , p glycoprotein , probenecid , biology , chemistry , atp binding cassette transporter , multiple drug resistance , biochemistry , drug resistance , virology , transporter , protease , microbiology and biotechnology , enzyme , viral load , hiv 1 protease , human immunodeficiency virus (hiv) , antiretroviral therapy , gene
HIV protease inhibitors (HPIs) are an important component of highly active antiretroviral therapy. However, the activity of drug efflux transporters, such as P-glycoprotein (P-gp) and multidrug resistance-associated proteins (MRP1/MRP2), may limit intracellular drug accumulation. Drugs that inhibit the activity of drug efflux proteins may, in combination with HPIs, enhance the clinical efficacy of the drugs.
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