Premium
Interactions of β‐Amyloids with the Blood–Brain Barrier
Author(s) -
BANKS WILLIAM A.,
KASTIN ABBA J.,
MANESS LAWRENCE M.,
BANKS MARIAN F.,
SHAYO MARCOS,
McLAY ROBERT N.
Publication year - 1997
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1997.tb48470.x
Subject(s) - blood–brain barrier , chemistry , intracellular , transporter , biophysics , in vivo , brain function , enzyme , function (biology) , in vitro , biochemistry , microbiology and biotechnology , central nervous system , biology , neuroscience , gene
Blood‐borne β‐amyloids (Aβs) could affect brain function by (1) crossing the BBB to directly interact with brain tissues or (2) altering BBB function by interacting with the brain capillaries that make up the BBB. Several radioactively labeled Aβe have been examined for such interactions. Blood‐borne Aβ 1‐28 is hindered from accumulating in brain by a slow rate of passage across the BBB and by robust enzymatic degradation. Aβ 1‐40 , but not Aβ 40‐1 or Aβ 1‐42 , is sequestered by brain capillaries, raising the possibility that it could affect BBB function. Small amounts of circulating Aβ 1‐40 are recovered intact from CSF and brain. Aβ 1‐40 is degraded by aluminum‐sensitive, calcium‐dependent intracellular enzymes. Apo‐J, which can bind Aβ, has been shown with an in situ method to be transported by a saturable system across the BBB. However, our recent work has shown that this system is not operable in vivo , probably because the transporter is saturated at physiological blood levels. In conclusion, Aβs have been shown to interact with and to cross the BBB.