Blood-brain barrier uptake of the 40 and 42 amino acid sequences of circulating Alzheimer's amyloid β in guinea pigs
| Autor: | J. B. Mackic, J G McComb, C. L. Martel, Jorge Ghiso, Berislav V. Zlokovic |
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| Rok vydání: | 1996 |
| Předmět: |
Male
chemistry.chemical_classification Amyloid beta-Peptides Amyloid beta General Neuroscience Peptide Biology Blood–brain barrier Molecular biology Amino acid medicine.anatomical_structure chemistry Biochemistry Alzheimer Disease Blood-Brain Barrier Cricetinae Parenchyma medicine biology.protein Animals Female Amino Acid Sequence Senile plaques Beta (finance) Peptide sequence |
| Zdroj: | Neuroscience Letters. 206:157-160 |
| ISSN: | 0304-3940 |
| DOI: | 10.1016/s0304-3940(96)12462-9 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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