Organic anion transporting polypeptide 1b2 (Oatp1b2 (also SLCO1B2))

Organic anion transporting polypeptide 1b2 (Oatp1b2, encoded by SLCO1B2) is a sodium-independent transporter selectively and abundantly expressed on the basolateral (sinusoidal) membrane of rat hepatocytes, serving a role analogous to the human liver transporters OATP1B1 and OATP1B3[2][4]. It is a member of the solute carrier (SLC) family, mediating the hepatic uptake of a diverse range of endogenous substrates (bile acids, steroid and thyroid hormone conjugates, peptides, prostaglandins) and numerous drugs (statins, olmesartan, paclitaxel, rifampicin, etc.)[2][4][9]. Oatp1b2 participates in hepatic clearance and regulates systemic exposure to substrates, impacting both pharmacokinetics and toxicity. Oatp1b2 knockout models have established its critical role in drug disposition, drug-drug interaction potential, and susceptibility to hepatotoxicity by environmental and fungal toxins (phalloidin, microcystin-LR)[4][5][9]. In rodents, Oatp1b2 uniquely impacts the pharmacokinetics and toxicity profile of paclitaxel, and species differences must be considered when extrapolating to human OATP1B1/1B3 data[2][8]. Note: Oatp1b2 is the rat ortholog; the closest human equivalents are OATP1B1 (SLCO1B1) and OATP1B3 (SLCO1B3).

Other names

Oatp4rlst-1Slc21a10Lst-1Slco1b2

Substrate uptake through sodium-independent facilitated transport across basolateral membrane of hepatocytes[2][4] Drug-drug interactions via inhibition or competition at the transporter level (notably with statins, paclitaxel, sorafenib, and anti-cancer drugs)[9]