Source:http://linkedlifedata.com/resource/pubmed/id/12477666
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2003-3-6
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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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Marine Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxocins,
http://linkedlifedata.com/resource/pubmed/chemical/maitotoxin
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0363-6143
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
C1006-20
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pubmed:dateRevised |
2010-12-3
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pubmed:meshHeading |
pubmed-meshheading:12477666-Alanine,
pubmed-meshheading:12477666-Animals,
pubmed-meshheading:12477666-Aorta,
pubmed-meshheading:12477666-Cattle,
pubmed-meshheading:12477666-Cell Death,
pubmed-meshheading:12477666-Cells, Cultured,
pubmed-meshheading:12477666-Cytoprotection,
pubmed-meshheading:12477666-Endothelium, Vascular,
pubmed-meshheading:12477666-Glycine,
pubmed-meshheading:12477666-Green Fluorescent Proteins,
pubmed-meshheading:12477666-Indicators and Reagents,
pubmed-meshheading:12477666-Luminescent Proteins,
pubmed-meshheading:12477666-Marine Toxins,
pubmed-meshheading:12477666-Oxocins,
pubmed-meshheading:12477666-Permeability,
pubmed-meshheading:12477666-Time Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Blockade of maitotoxin-induced endothelial cell lysis by glycine and L-alanine.
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pubmed:affiliation |
Rammelkamp Center for Education and Research, MetroHealth Medical Center, Cleveland, Ohio 44109-1998, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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