Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2004-4-15
pubmed:abstractText
Although the amyloid beta protein (Abeta) E693Q mutation enhances Abeta fibrillization in vitro and cerebral amyloid angiopathy (CAA) in vivo, brain parenchymal Abeta deposition and tau pathology in hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D) are limited. To evaluate whether clearance of Abeta by glial cells may play a role in this regard, this immunohistochemical study of frontal cortex of 14 HCHWA-D autopsy brains was performed using double staining with glial markers and end-specific antibodies to Abetax-42 (Abeta42) and Abetax-40 (Abeta40). Tau pathology was also assessed. Numerous microglia and/or astrocytes carrying cytoplasmic Abeta42(+)40(-) granules were scattered among non-fibrillar (Congo red-negative) Abeta deposits, i.e., clouds, fine diffuse plaques, and Abeta42(+)40(-) dense diffuse plaques. On the other hand, activated microglia and reactive astrocytes associated with fibrillar (Congo red-positive) Abeta deposition, i.e., Abeta42(+)40(+) dense diffuse plaques and CAA invading the parenchyma, were virtually devoid of Abeta granules. Tau pathology was scant and most frequently associated with CAA. These results suggest that relatively non-fibrillar parenchymal Abeta deposits may be liable to glial clearance. Abeta sequestration by glial cells may be a factor limiting the levels of neurotoxic soluble Abeta oligomers in HCHWA-D brain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation..., http://linkedlifedata.com/resource/pubmed/chemical/CD68 antigen, human, http://linkedlifedata.com/resource/pubmed/chemical/Glial Fibrillary Acidic Protein, http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 5, http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/amyloid beta-protein (1-40), http://linkedlifedata.com/resource/pubmed/chemical/amyloid beta-protein (1-42), http://linkedlifedata.com/resource/pubmed/chemical/tau Proteins
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0001-6322
pubmed:author
pubmed:issnType
Print
pubmed:volume
107
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
389-98
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:15014955-Aged, pubmed-meshheading:15014955-Aged, 80 and over, pubmed-meshheading:15014955-Amyloid beta-Peptides, pubmed-meshheading:15014955-Antigens, CD, pubmed-meshheading:15014955-Antigens, Differentiation, Myelomonocytic, pubmed-meshheading:15014955-Cerebral Amyloid Angiopathy, pubmed-meshheading:15014955-Cerebral Amyloid Angiopathy, Familial, pubmed-meshheading:15014955-Cerebral Hemorrhage, pubmed-meshheading:15014955-Female, pubmed-meshheading:15014955-Frontal Lobe, pubmed-meshheading:15014955-Glial Fibrillary Acidic Protein, pubmed-meshheading:15014955-Glucose Transporter Type 5, pubmed-meshheading:15014955-Humans, pubmed-meshheading:15014955-Immunohistochemistry, pubmed-meshheading:15014955-Male, pubmed-meshheading:15014955-Middle Aged, pubmed-meshheading:15014955-Monosaccharide Transport Proteins, pubmed-meshheading:15014955-Neuroglia, pubmed-meshheading:15014955-Peptide Fragments, pubmed-meshheading:15014955-Plaque, Amyloid, pubmed-meshheading:15014955-Postmortem Changes, pubmed-meshheading:15014955-tau Proteins
pubmed:year
2004
pubmed:articleTitle
Glial reactions and the clearance of amyloid beta protein in the brains of patients with hereditary cerebral hemorrhage with amyloidosis-Dutch type.
pubmed:affiliation
Department of Neurology, K5Q 97, Leiden University Medical Center, PO Box 9600, 2300 RC Leiden, The Netherlands. M.L.C.Maat-Schieman@lumc.nl
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't