Rat liver cells express the multispecific organic anion trans-tition with other substrates at the sites of glucuronidation and transport via cmoat. (HEPATOLOGY 1997;26:1467-1476.) porter (cmoat, cmrp, mrp2) and P-glycoprotein (Pgp) in their canalicular membranes, proteins that are homologous to the
Modulation of liver canalicular transport processes by the tyrosine-kinase inhibitor genistein: Implications of genistein metabolism in the rat
โ Scribed by W Jager; O Winter; B Halper; A Salamon; M Sartori; L Gajdzik; G Hamilton; G Theyer; J Graf; T Thalhammer
- Book ID
- 118686757
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 313 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0270-9139
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In conclusion, the report by Casey and colleagues is based on the use of two pharmacological inhibitors that have nonspecific effects and no attempt was made to verify their specificity. This lead the authors to ambitious conclusions on the involvement of tyrosine kinases on LTP in perforant path-gr
## Abstract A great deal of recent evidence points to a role for tyrosine kinase in expression of LTP. Data have been presented that are consistent with the idea that tyrosine phosphorylation of proteins occurs in both the presynaptic and postsynaptic areas. In this study, we set out to investigate