Blood-brain barrier uptake of the 40 and 42 amino acid sequences of circulating Alzheimer's amyloid β in guinea pigs
1996; Elsevier BV; Volume: 206; Issue: 2-3 Linguagem: Inglês
10.1016/s0304-3940(96)12462-9
ISSN1872-7972
AutoresCynthia L. Martel, Jasmina B. Mačkić, J. Gordon McComb, Jorge Ghiso, Berislav V. Zloković,
Tópico(s)Dementia and Cognitive Impairment Research
ResumoAn intracarotid brain infusion/capillary depletion technique was used in guinea pigs to examine cerebral capillary sequestration and transport into brain parenchyma of sAβ1–40 and sAβ1–42, synthetic peptides identical to two forms of the amyloid β 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 sAβ1–40 had an approximately two-fold greater affinity than sAβl–42. There was significant capillary sequestration of sAβ1–40, but retention by the microvasculature of sAβ1–42 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.
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