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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-3-15
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pubmed:abstractText |
The magnesium buffer coefficient (BMg) was calculated for BC3H-1 cells from the rise in cytosolic Mg2+ activity observed when magnesium was released from ATP after iodoacetate (IAA) and NaCN treatment. The basal cytosolic Mg2+ activity (0.54 +/- 0.1 mM) measured with mag-fura-2 doubled when 4.54 mM magnesium was liberated from ATP: BMg was 12.9 indicating that a 1 mM increase in Mg2+ activity requires an addition of about 13 mM magnesium. The accuracy of this value depends on these assumptions: (a) all of the magnesium released from ATP stayed in the cells; (b) the rise in Mg2+ was not secondary to pH-induced changes in BMg; (c) mag-fura-2 measured Mg2+ and not Ca2+; and (d) the accuracy of the mag-fura-2 calibration. Total magnesium did not change in response to IAA/CN treatment, thus the change in Mg2+ activity reflected a redistribution of cell magnesium. pH changes induced by NH4Cl pulse and removal had little effect on Mg2+ activity and the changes were slower than and opposite to pH-induced changes in Ca2+ activity measured by fura-2. Ca2+ responses were temporally uncoupled from Mg2+ responses when the cells were treated with IAA only and in no cases did Ca2+ levels rise above 1 microM, showing that the mag-fura-2 is responding to Mg2+. Additional studies demonstrated that approximately 90% of the mag-fura-2 signal was cytosolic in origin. The remaining non-diffusible mag-fura-2 either was bound to cytosolic membranes or sequestered in organelles with the fluorescence characteristics of the Mg2(+)-complexed form, even when cytosolic free Mg2+ activity was approximately 0.5 mM. This bound mag-fura-2 would appear to increase the Kd and thus clearly limits the accuracy of our estimmate for BMg. Despite this limitation, we demonstrate that Mg2+ is tightly regulated in face of large changes in extracellular Mg2+, and that interplay observed between pH, Ca2+ and Mg2+ activities strongly supports the hypothesis that these factors interact through a shared buffer capacity of the cell.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-(2-(5-carboxy)oxazole)-5-hydroxy-6...,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Ammonium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Buffers,
http://linkedlifedata.com/resource/pubmed/chemical/Digitonin,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Fura-2,
http://linkedlifedata.com/resource/pubmed/chemical/Iodoacetates,
http://linkedlifedata.com/resource/pubmed/chemical/Iodoacetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Phloretin,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Cyanide
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0300-8177
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
136
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-22
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7854327-Adenosine Triphosphate,
pubmed-meshheading:7854327-Ammonium Chloride,
pubmed-meshheading:7854327-Animals,
pubmed-meshheading:7854327-Buffers,
pubmed-meshheading:7854327-Cell Compartmentation,
pubmed-meshheading:7854327-Cells, Cultured,
pubmed-meshheading:7854327-Cytosol,
pubmed-meshheading:7854327-Digitonin,
pubmed-meshheading:7854327-Fluorescent Dyes,
pubmed-meshheading:7854327-Fura-2,
pubmed-meshheading:7854327-Hydrogen-Ion Concentration,
pubmed-meshheading:7854327-Iodoacetates,
pubmed-meshheading:7854327-Iodoacetic Acid,
pubmed-meshheading:7854327-Magnesium,
pubmed-meshheading:7854327-Muscles,
pubmed-meshheading:7854327-Phloretin,
pubmed-meshheading:7854327-Sodium Cyanide
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pubmed:year |
1994
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pubmed:articleTitle |
Determination of cytosolic Mg2+ activity and buffering in BC3H-1 cells with mag-fura-2.
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pubmed:affiliation |
Department of Pharmacology and Toxicology, School of Medicine, Wright State University, Dayton, Ohio 45435.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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