Linked Life Data

11761721

Source:http://linkedlifedata.com/resource/pubmed/id/11761721

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-12-13
pubmed:abstractText
Cerebrovascular deposition of amyloid beta protein (A beta) is a characteristic lesion of Alzheimer's disease (AD) and hereditary cerebral hemorrhage with amyloidosis of the Dutch type (HCHWA-D). Besides A beta, several other proteins and proteoglycans accumulate in cerebral amyloid angiopathy (CAA). We have now analyzed the expression of the heparan sulfate proteoglycan (HSPG) subtypes agrin, perlecan, glypican-1, syndecans 1-3 and HS glycosaminoglycan (GAG) side chains in CAA in brains of patients with AD and HCHWA-D. Hereto, specific well-characterized antibodies directed against the core protein of these HSPGs and against the GAG side chains were used for immunostaining. Glypican-1 was abundantly expressed in CAA both in AD and HCHWA-D brains, whereas perlecan and syndecans-1 and -3 were absent in both. Colocalization of agrin with vascular A beta was clearly observed in CAA in HCHWA-D brains, but only in a minority of the AD cases. Conversely, syndecan-2 was frequently associated with vascular A beta in AD, but did not colocalize with vascular A beta deposits in HCHWA-D. The three different syndecans, agrin, glypican-1 and HS GAG, but not perlecan, were associated with the majority of senile plaques (SPs) in all brains. Our results suggest a role for agrin in the formation of SPs and of CAA in HCHWA-D, but not in the pathogenesis of CAA in AD. Both syndecan-2 and glypican, but not perlecan, may be involved in the formation of CAA. We conclude that specific HSPG species may be involved in the pathogenesis of CAA in both AD and HCHWA-D, and that the pathogenesis of CAA and SPs may differ with regard to the involvement of HSPG species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0001-6322
pubmed:author
pubmed:issnType
Print
pubmed:volume
102
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
604-14
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:11761721-Agrin, pubmed-meshheading:11761721-Alzheimer Disease, pubmed-meshheading:11761721-Amyloid beta-Peptides, pubmed-meshheading:11761721-Brain, pubmed-meshheading:11761721-Cerebral Amyloid Angiopathy, Familial, pubmed-meshheading:11761721-Cerebral Arteries, pubmed-meshheading:11761721-Female, pubmed-meshheading:11761721-Glycosaminoglycans, pubmed-meshheading:11761721-Glypicans, pubmed-meshheading:11761721-Heparan Sulfate Proteoglycans, pubmed-meshheading:11761721-Humans, pubmed-meshheading:11761721-Immunohistochemistry, pubmed-meshheading:11761721-Male, pubmed-meshheading:11761721-Membrane Glycoproteins, pubmed-meshheading:11761721-Middle Aged, pubmed-meshheading:11761721-Plaque, Amyloid, pubmed-meshheading:11761721-Proteoglycans, pubmed-meshheading:11761721-Syndecans
pubmed:year
2001
pubmed:articleTitle
Heparan sulfate proteoglycan expression in cerebrovascular amyloid beta deposits in Alzheimer's disease and hereditary cerebral hemorrhage with amyloidosis (Dutch) brains.
pubmed:affiliation
Department of Pathology, University Medical Center, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands. j.vanhorssen@pathol.azn.nl
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't