pubmed-article:7859081 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7859081 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
pubmed-article:7859081 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
pubmed-article:7859081 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
pubmed-article:7859081 | lifeskim:mentions | umls-concept:C0078939 | lld:lifeskim |
pubmed-article:7859081 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
pubmed-article:7859081 | lifeskim:mentions | umls-concept:C0806140 | lld:lifeskim |
pubmed-article:7859081 | lifeskim:mentions | umls-concept:C1511636 | lld:lifeskim |
pubmed-article:7859081 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:7859081 | lifeskim:mentions | umls-concept:C1335533 | lld:lifeskim |
pubmed-article:7859081 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:7859081 | pubmed:dateCreated | 1995-3-22 | lld:pubmed |
pubmed-article:7859081 | pubmed:abstractText | Effects of amyloid beta protein fragment 25-35, A beta P(25-35), on membrane permeability and cell viability were examined in the brain neurons dissociated from the rats using a flow cytometer and two fluorescent dyes, fluo-3 to monitor intracellular Ca2+ concentration ([Ca2+]i) of neurons and ethidium which is impermeant to membranes of intact neurons to stain dead and dying neurons. A beta P(25-35) augmented fluo-3 fluorescence of some neurons at concentrations greater than 1 microM, indicating an increase in [Ca2+]i although other neurons (about 80% of total neurons) did not respond to A beta P(25-35) even at 10 microM. A beta P(25-35) at 1 microM or greater increased dose-dependently the number of ethidium-stained neurons, suggesting a dose-dependent increase in number of dead and dying neurons. Results suggest that A beta P(25-35) increases the membrane permeability of brain neurons, resulting in a destabilized intracellular homeostasis that leads to neuonal death. | lld:pubmed |
pubmed-article:7859081 | pubmed:language | eng | lld:pubmed |
pubmed-article:7859081 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7859081 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7859081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7859081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7859081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7859081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7859081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7859081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7859081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7859081 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7859081 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7859081 | pubmed:month | Oct | lld:pubmed |
pubmed-article:7859081 | pubmed:issn | 0006-8993 | lld:pubmed |
pubmed-article:7859081 | pubmed:author | pubmed-author:AkaikeNN | lld:pubmed |
pubmed-article:7859081 | pubmed:author | pubmed-author:FurukawaKK | lld:pubmed |
pubmed-article:7859081 | pubmed:author | pubmed-author:OyamaYY | lld:pubmed |
pubmed-article:7859081 | pubmed:author | pubmed-author:HatakeyamaYY | lld:pubmed |
pubmed-article:7859081 | pubmed:author | pubmed-author:ChikahisaLL | lld:pubmed |
pubmed-article:7859081 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7859081 | pubmed:day | 31 | lld:pubmed |
pubmed-article:7859081 | pubmed:volume | 662 | lld:pubmed |
pubmed-article:7859081 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7859081 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7859081 | pubmed:pagination | 259-62 | lld:pubmed |
pubmed-article:7859081 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:7859081 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7859081 | pubmed:articleTitle | Flow cytometric analysis on cytotoxic action of amyloid beta protein fragment 25-35 on brain neurons dissociated from the rats. | lld:pubmed |
pubmed-article:7859081 | pubmed:affiliation | Laboratory of Cell Signaling [Pharmacology], Faculty of Integrated Arts and Sciences, University of Tokushima, Japan. | lld:pubmed |
pubmed-article:7859081 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7859081 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |