| pubmed-article:11450095 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11450095 | lifeskim:mentions | umls-concept:C0005854 | lld:lifeskim |
| pubmed-article:11450095 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:11450095 | lifeskim:mentions | umls-concept:C1555029 | lld:lifeskim |
| pubmed-article:11450095 | lifeskim:mentions | umls-concept:C1743100 | lld:lifeskim |
| pubmed-article:11450095 | pubmed:dateCreated | 2001-7-13 | lld:pubmed |
| pubmed-article:11450095 | pubmed:abstractText | Our experiments were performed to test the hypothesis that human beta-amyloid peptide 42 (beta A) is able to enter and exit the brain parenchyma through the blood-brain barrier. In an effort to determine the effect of beta A in an animal model, we have injected beta A i.v. into rats following single and repeated brain ischemia. Rats were sacrificed at 3 and 12 months after injection and beta A was localized by monoclonal antibody (mAb) 4G8. The present observations revealed an abundant presence of beta A in the extracellular space of the brain, which appeared to be dilated, and a vigorous uptake of beta A into the cytoplasm of endothelial and ependymal cells, pericytes, astrocytes and neurons. Some of the beta A deposits were associated and/or had migrated to the vessels and to the ventricles, and by 3 months a significant amount of beta A was directly associated with the vessels and was observed inside the ventricular space. Virtually no soluble and aggregating beta A was found in brain tissue 1 year later. This suggests that phagocytic pericytes and astrocytes take up exogenous beta A in an attempt to clear the peptide from the brain extracellular space and deliver it to the circulation. Further, direct removal of beta A from the ventricles by the bloodstream is also possible. These observations suggest that a reverse transport of beta A across endothelial cells of microvessels represents one of the possible mechanisms responsible for removal of extravasated beta A. The findings of the present study indicate that in normal conditions beta A is rapidly cleared from the cerebrospinal fluid and brain parenchyma, suggesting that irreversible changes in the physico-chemical properties of the cerebrovascular endothelial cell surface are involved in beta A deposition in the brain in Alzheimer's disease (AD). | lld:pubmed |
| pubmed-article:11450095 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11450095 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11450095 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11450095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11450095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11450095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11450095 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11450095 | pubmed:issn | 0065-1419 | lld:pubmed |
| pubmed-article:11450095 | pubmed:author | pubmed-author:BarcikowskaMM | lld:pubmed |
| pubmed-article:11450095 | pubmed:author | pubmed-author:PlutaRR | lld:pubmed |
| pubmed-article:11450095 | pubmed:author | pubmed-author:LipkowskiA... | lld:pubmed |
| pubmed-article:11450095 | pubmed:author | pubmed-author:MisickaAA | lld:pubmed |
| pubmed-article:11450095 | pubmed:author | pubmed-author:JanuszewskiSS | lld:pubmed |
| pubmed-article:11450095 | pubmed:author | pubmed-author:SpisackaSS | lld:pubmed |
| pubmed-article:11450095 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11450095 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:11450095 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11450095 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11450095 | pubmed:pagination | 73-7 | lld:pubmed |
| pubmed-article:11450095 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:meshHeading | pubmed-meshheading:11450095... | lld:pubmed |
| pubmed-article:11450095 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11450095 | pubmed:articleTitle | Possible reverse transport of beta-amyloid peptide across the blood-brain barrier. | lld:pubmed |
| pubmed-article:11450095 | pubmed:affiliation | Department of Neuropathology, Medical Research Centre, Polish Academy of Sciences, Warsaw, Poland. | lld:pubmed |
| pubmed-article:11450095 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11450095 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11450095 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11450095 | lld:pubmed |
