Amyloid β‐proteins 1—40 and 1—42(43) in the soluble fraction of extra‐ and intracranial blood vessels

  title={Amyloid $\beta$‐proteins 1—40 and 1—42(43) in the soluble fraction of extra‐ and intracranial blood vessels},
  author={Yasuhisa Shinkai and Masahiro Yoshimura and Yuji Ito and Asano Odaka and Nobuhiro Suzuki and Katsuhiko Yanagisawa and Yasuo Ihara},
  journal={Annals of Neurology},
To investigate the process of amyloid β‐protein (Aβ) accumulation in cerebral amyloid angiopathy (CAA), the levels of Aβ were determined in the soluble fraction of extra‐ and intracranial blood vessels and leptomeninges obtained at autopsy. Two enzyme immunoassays were employed that are known to sensitively and specifically quantify two Aβ species, Aβ1–40 and 1–42(43). Aβ was detectable in the intracranial blood vessels and leptomeninges with the latter containing the highest levels, while it… 
Amyloid β‐protein deposition in the leptomeninges and cerebral cortex
The presence of plaque‐free cortical samples showing significant levels of insoluble Aβ42 suggests that biochemically detectable Aβ accumulation precedes immunocytochemically detected Aβ deposition in the cortex, respectively.
Heparan sulfate proteoglycan expression in cerebrovascular amyloid β deposits in Alzheimer's disease and hereditary cerebral hemorrhage with amyloidosis (Dutch) brains
It is concluded that specific HSPG species may be involved in the pathogenesis of CAA in both AD and HCHWA-D, and that the pathogenic of C AA and SPs may differ with regard to the involvement of HSPg species.
Receptor-Mediated Transport of Human Amyloid β-Protein 1–40 and 1–42 at the Blood–Brain Barrier
The high PS values observed for A beta 1-40 and 1-42 compare to insulin, whose uptake is decidedly by a receptor-mediated transport process, and suggest a similar mechanism for L-A beta entry into the brain, which implies a stereoisomer-specific, ligand-receptor interaction at the BBB for the L- A beta proteins.
In Vitro Evidence That β‐Amyloid Peptide 1–40 Diffuses Across the Blood–Brain Barrier and Affects Its Permeability
It is hypothesized that a saturable, outwardly directed flux of this peptide occurs at the blood–brain barrier (BBB) and tested whether supraphysiological (possibly pathological) concentrations of sAβ could alter the permeability of this barrier to a paracellular tracer, polyethylene glycol (PEG).
Apolipoprotein E, Smooth Muscle Cells and the Pathogenesis of Cerebral Amyloid Angiopathy: the Potential Role of Impaired Cerebrovascular Aβ Clearance
A pathogenetic model of CAA is proposed, in which the ApoE‐ and HSPG‐mediated clearance of CSF‐derived Aβ peptides by SMCs protects the vascular extracellular matrix against critical Aβ concentrations.
Amyloid β-Peptide Is Transported on Lipoproteins and Albumin in Human Plasma*
Aβ is normally bound to and transported by albumin and specific lipoproteins in human plasma under physiological conditions and is not significantly influenced by apolipoprotein E genotype.
The Evolution of Aβ Peptide Burden in the APP23 Transgenic Mice: Implications for Aβ Deposition in Alzheimer Disease
It is suggested that the APP23 Tg mouse may develop an earlier blockage in Aβ clearance than the Tg2576 mice, resulting in a more severe accumulation of Aβ in the perivascular drainage pathways and in the brain.
Immunohistochemical Analysis of Amyloid β-Protein Isoforms in CAA
Findings are consistent in normal aged people and in disorders having CAA; i.e.poradic AD, early-onset familial AD with both APP and presenilin mutations, Down syndrome and HCHWA-D.
Astrocytes Containing Amyloid ( 3-Protein ( Af 3 )-Positive Granules Are Associated with A 1340-Positive Diffuse Plaques in the Aged Human Brain
From the Department of Neuropathology, Faculty ofMedicine, University of Tokyo, the department ofNeuropathology is composed of students from the Medical Research Institute, Tokyo Medical and Dental University, and Toho University, Tokyo.


beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease.
  • A. Roher, J. Lowenson, M. Ball
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1993
Reinvestigation of the chemical structure of beta-amyloid peptide (A beta) deposits in the vascular tissue of Alzheimer disease brains revealed that the 42-residue form A beta-(1-42), rather than the
Amyloid β protein (Aβ) deposition: Aβ42(43) precedes Aβ40 in down Syndrome
The chronological relationship regarding deposition of amyloid β protein (Aβ) species, Aβ40 and Aβ42(43), was investigated in 16 brains from Down syndrome patients aged 31 to 64 years and results indicate that the Aβ species intially deposited in the brain as senile plaques is Aβ 42(43).
Non‐Fibrillar β‐Amyloid Protein is Associated with Smooth Muscle Cells of Vessel Walls in Alzheimer Disease
Data indicate that during formation of amyloid in AD vessel walls, nonfibrillar, monomeric, and oligomeric β-protein accumulate.
High tissue content of soluble beta 1-40 is linked to cerebral amyloid angiopathy.
The tissue level of soluble beta 1-40 should be useful for the quantification of cerebral amyloid angiopathy inged control and Alzheimer's diseased brains.
APP717 missense mutation affects the ratio of amyloid beta protein species (A beta 1-42/43 and a beta 1-40) in familial Alzheimer's disease brain.
The APP717 missense mutation does not create new A beta species but promotes the increased accumulation of A beta 1-42/43 in the brain, which results in the enhancement of amyloid fibril formation from soluble A beta.
Differences Between Vascular and Plaque Core Amyloid in Alzheimer's Disease
The differences between vascular and plaque β‐amyloid may reflect diverse processing of the β protein precursor in the vessel wall and brain parenchyma due to tissue‐specific endopeptidases.