Suppression of Lymphocyte Activation by a Protein Released from Isolated Perfused Rat Liver
β Scribed by Christopher Pizzo; Donald Lee; Francis V. Chisari
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 1023 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0270-9139
No coin nor oath required. For personal study only.
β¦ Synopsis
Isolated rat liver perfusates contain a substance which inhibits 3H-thymidine uptake by phytohemagglutinin-stimulated human peripheral blood lymphocytes in a dose-dependent, noncytotoxic fashion. Suppression is not due to interference of lymphocyte-phytohemagglutinin interaction or dilution of the thymidine pool. Complete inhibition of thymidine uptake is achieved with less than 1.0 pg of material per ml (which is a potentially achievable concentration in vivo). The release of this material is directly and quantitatively associated with hepatocellular injury as measured by release of glutamic pyruvate transaminase. The material is a highly basic protein with a molecular weight of approximately 66,000 to 80,000 daltons. It is a product of the hepatocyte rather than of nonparenchymal liver cells. Liver-derived materials, such as the presently described molecule, may play a role in in situ regulation of lymphocyte function during immunologically mediated liver disease.
π SIMILAR VOLUMES
Bilirubin and other organic anions are transported in serum avidly bound to albumin from which they are extracted and transferred into the hepatocyte where they bind to cytosolic proteins. Two abundant organic anion binding proteins, ligandin and Z-protein, were previously purified from liver cytoso
Although the adverse effect of hypoxia on drug metabolism is well documented in subcellular systems, its effect on drug clearance by the intact liver has not been defined. This study was undertaken in the isolated perfused rat liver to examine the effects of acute hypoxia on the hepatic elimination
The highly efficient hepatic extraction of propranolol by the isolated perfused rat liver does not diminish when albumin binding is increased from 30 to 75%. One possible explanation of this insensitivity of propranolol uptake to changes in albumin binding is the mediation of uptake of bound ligand