Blood-brain barrier uptake of the 40 and 42 amino acid sequences of circulating Alzheimer's amyloid beta in guinea pigs
Blood-brain barrier uptake of the 40 and 42 amino acid sequences of circulating Alzheimer's amyloid beta in guinea pigs
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DOI：
10.1016/s0304-3940(96)12462-9
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发表时间：
1996-03-15
影响因子：
2.5
通讯作者：
Zlokovic, BV
中科院分区：
文献类型：
--
作者：
Martel, CL;Mackic, JB;Zlokovic, BV
在豚鼠中使用颈动脉内脑灌注/毛细血管耗竭技术来检查脑毛细血管隔离和sA β（1-40）和sA β（1-42）向脑实质中的转运，sA β（1-40）和sA β（1-42）是与在阿尔茨海默病病变中发现的两种形式的淀粉样β肽相同的合成肽：主要在血管沉积物中发现的40残基形式和主要在老年斑中发现的42残基形式。这些肽通过特异性转运机制很好地进入脑实质，其中sA β（1-40））的亲和力比sA β（1-42）高约2倍。有显着的毛细血管隔离SA β（1-40，但保留SA β？（1-42）可以忽略不计。这些数据表明，脑血管系统中的40个残基的肽和实质中的42个残基的肽的水平可以通过血脑屏障隔离和运输它们各自的循环前体来调节。
An intracarotid brain infusion/capillary depletion technique was used in guinea pigs to examine cerebral capillary sequestration and transport into brain parenchyma of sA beta(1-40) and sA beta(1-42), synthetic peptides identical to two forms of the amyloid beta peptide found in Alzheimer's disease lesions: the 40 residue form, found primarily in vascular deposits, and the 42 residue form, found primarily in senile plaques. The peptides crossed well into the brain parenchyma via a specific transport mechanism for which sA beta(1-40)) had an approximately two-fold greater affinity than sA beta(1-42). There was significant capillary sequestration of SA beta(1-40, but retention by the microvasculature of SA beta?(1-42) was negligible. These data suggest that the level of the 40 residue peptide in cerebral vasculature and of the 42 residue peptide in parenchyma could be regulated by blood-brain barrier sequestration and transport of their respective circulating precursors.