alanyl-alanyl-alanyl-alanine has been researched along with estrone-sulfate* in 1 studies
1 other study(ies) available for alanyl-alanyl-alanyl-alanine and estrone-sulfate
| Article | Year |
|---|---|
Contribution of organic anion transporting polypeptide OATP-C to hepatic elimination of the opioid pentapeptide analogue [D-Ala2, D-Leu5]-enkephalin.
The objective of this study was to examine the transport activity of the human organic anion transporter OATP-C (SLC21A6) for oligopeptides that are eliminated rapidly from the systemic circulation. We focused on an opioid peptide analogue, [D-Ala(2), D-Leu(5)]-enkephalin (DADLE), a linear pentapeptide modified to be stable. [(3)H]DADLE was taken up by rat isolated hepatocytes in a saturable manner and highly accumulated in the liver after intravenous administration to rats. The uptake of [(3)H]DADLE by the isolated hepatocytes was inhibited by several organic anions and pentapeptides, but not by tetra- or tripeptides. When OATP-C was expressed in Xenopus laevis oocytes, a significant increase in uptake of [(3)H]DADLE was observed. Moreover, the inhibitory effects of various compounds, including some peptides, on [(3)H]estrone-3-sulfate uptake by OATP-C were similar to those observed in [(3)H]DADLE uptake by rat isolated hepatocytes. In conclusion, it was demonstrated that OATP-C contributes to the rapid hepatic excretion of peptides and peptide-mimetic drugs. Topics: Animals; Anions; Bile; Biological Transport; Enkephalin, D-Penicillamine (2,5)-; Enkephalin, Leucine-2-Alanine; Estrone; Hepatocytes; In Vitro Techniques; Injections, Intravenous; Liver-Specific Organic Anion Transporter 1; Oocytes; Peptides; Rats; Rats, Sprague-Dawley; Structure-Activity Relationship; Xenopus laevis | 2003 |