| pubmed-article:12477666 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12477666 | lifeskim:mentions | umls-concept:C0225336 | lld:lifeskim |
| pubmed-article:12477666 | lifeskim:mentions | umls-concept:C0001898 | lld:lifeskim |
| pubmed-article:12477666 | lifeskim:mentions | umls-concept:C0017890 | lld:lifeskim |
| pubmed-article:12477666 | lifeskim:mentions | umls-concept:C0024348 | lld:lifeskim |
| pubmed-article:12477666 | lifeskim:mentions | umls-concept:C0332206 | lld:lifeskim |
| pubmed-article:12477666 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:12477666 | pubmed:dateCreated | 2003-3-6 | lld:pubmed |
| pubmed-article:12477666 | pubmed:abstractText | The maitotoxin (MTX)-induced cell death cascade in bovine aortic endothelial cells (BAECs) is a model for oncotic/necrotic cell death. The cascade is initiated by an increase in cytosolic free Ca(2+) concentration ([Ca(2+)](i)), which is followed by the biphasic uptake of vital dyes. The initial phase of dye entry reflects activation of large pores and correlates with surface membrane bleb formation; the second phase reflects cell lysis. In the present study, the effect of the cytoprotective amino acid glycine was examined. Glycine had no effect on MTX-induced change in [Ca(2+)](i) or on the first phase of vital dye uptake but produced a concentration-dependent (EC(50) approximately 1 mM) inhibition of the second phase of dye uptake. No cytoprotective effect was observed with l-valine, l-proline, or d-alanine, whereas l-alanine was equieffective to glycine. Furthermore, glycine had no effect on MTX-induced bleb formation. To test the hypothesis that glycine specifically blocks formation of a lytic "pore," the loss of fluorescence from BAECs transiently expressing GFP and concatemers of GFP ranging in size from 27 to 162 kDa was examined using time-lapse videomicroscopy. MTX-induced loss of GFP was rapid, correlated with the second phase of dye uptake, and was relatively independent of molecular size. The MTX-induced loss of GFP from BAECs was completely blocked by glycine. The data suggest that the second "lytic" phase of MTX-induced endothelial cell death reflects formation of a novel permeability pathway that allows macromolecules such as GFP or LDH to escape, yet can be prevented by the cytoprotective agents glycine and l-alanine. | lld:pubmed |
| pubmed-article:12477666 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12477666 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12477666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12477666 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12477666 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12477666 | pubmed:issn | 0363-6143 | lld:pubmed |
| pubmed-article:12477666 | pubmed:author | pubmed-author:SchillingWill... | lld:pubmed |
| pubmed-article:12477666 | pubmed:author | pubmed-author:EstacionMarkM | lld:pubmed |
| pubmed-article:12477666 | pubmed:author | pubmed-author:WeinbergJusti... | lld:pubmed |
| pubmed-article:12477666 | pubmed:author | pubmed-author:SinkinsWillia... | lld:pubmed |
| pubmed-article:12477666 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12477666 | pubmed:volume | 284 | lld:pubmed |
| pubmed-article:12477666 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12477666 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12477666 | pubmed:pagination | C1006-20 | lld:pubmed |
| pubmed-article:12477666 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
| pubmed-article:12477666 | pubmed:meshHeading | pubmed-meshheading:12477666... | lld:pubmed |
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| pubmed-article:12477666 | pubmed:meshHeading | pubmed-meshheading:12477666... | lld:pubmed |
| pubmed-article:12477666 | pubmed:meshHeading | pubmed-meshheading:12477666... | lld:pubmed |
| pubmed-article:12477666 | pubmed:meshHeading | pubmed-meshheading:12477666... | lld:pubmed |
| pubmed-article:12477666 | pubmed:meshHeading | pubmed-meshheading:12477666... | lld:pubmed |
| pubmed-article:12477666 | pubmed:meshHeading | pubmed-meshheading:12477666... | lld:pubmed |
| pubmed-article:12477666 | pubmed:meshHeading | pubmed-meshheading:12477666... | lld:pubmed |
| pubmed-article:12477666 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12477666 | pubmed:articleTitle | Blockade of maitotoxin-induced endothelial cell lysis by glycine and L-alanine. | lld:pubmed |
| pubmed-article:12477666 | pubmed:affiliation | Rammelkamp Center for Education and Research, MetroHealth Medical Center, Cleveland, Ohio 44109-1998, USA. | lld:pubmed |
| pubmed-article:12477666 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12477666 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12477666 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12477666 | lld:pubmed |
