@entity6970 influences amyloid-beta clearance from the XXXX periphery.

@entity15370 @entity6970 @entity19 @entity195
The relationship between amyloid-beta protein ( @entity15370 ) metabolism and @entity195 is currently poorly understood. While it is well known that the generation of @entity15370 results from enzymatic cleavage of its parent molecule, the amyloid beta protein precursor (AbetaPP), there is little information available regarding its in vivo clearance. The E4 isoform of @entity6970 ( @entity6970 ) has been associated with poor clearance of @entity15370 under in vitro conditions. This is thought to be due to its poor ability to bind @entity15370 compared with the other common isoforms, apoE2 and apoE3. Although cell culture studies support the notion that @entity15370 clearance depends upon @entity6970 isoform, validation of these findings requires @entity15370 clearance studies in vivo. In this study, we examined the clearance of @entity15370 in vivo from the periphery in @entity19 that expressed @entity6970 (C57BL/6J) or lacked @entity6970 ( @entity6970 knockout). We measured the clearance of peripherally injected @entity15370 over time and additionally, the quantities sequestered by peripheral organs. Western blot analysis of the @entity19 plasma indicated that the half-life of @entity15370 in the periphery was approximately 15 minutes. The livers of the C57BL/6J @entity19 were found to have sequestered approximately 40% of the total injected @entity15370 at 90 minutes post-injection, whilst their kidneys contained 5% of the total injected @entity15370 . In contrast, the livers and kidneys of the @entity6970 knockout animals were found to contain no detectable @entity15370 . These findings indicate that @entity15370 is rapidly removed from the plasma by @entity19 peripheral tissues and the rate of its clearance is affected by @entity6970 .
