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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1976-3-1
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pubmed:abstractText |
Ethanol, in concentrations of 0.05-0.8 M, inhibited intact human and rabbit reticulocyte protein synthesis in the presence of iron-transferrin for endogenous haem synthesis. Associated with this effect there was a conversion of polyribosomes to monoribosomes and a decreased incorporation of radioactive leucine into nascent globin chains. When physiological levels of ethanol (0.05-0.1 M) were used, these effects were prevented by incubation with 50 muM haemin and reversed by removing the alcohol and reincubating with iron-transferrin or haemin. The polyribosomal disaggregation was also prevented by stopping ribosomal movement with 5 mM cycloheximide. Neither ATP nor GSH levels were altered in the presence of ethanol. When non-physiological levels of 0.8 M ethanol were used, haemin did not prevent the inhibition of protein synthesis. Likewise, in the rabbit reticulocyte cell-free lysate system containing haemin inhibition was noted at concentrations greater than 0.05 M ethanol. The polyribosomal disaggregation in reticulocytes incubated with 0.8 M ethanol was associated with decreased dissociation of monoribosomes into subunits. Similarly, when ribosomes were directly suspended cell-free in 0.1 or 0.8 M ethanol there was a decreased percentage of subunits. These results indicate that physiological concentrations of ethanol inhibit initiation of reticulocyte protein synthesis secondary to a block in haem synthesis. When intact cells are exposed to high non-physiological concentrations of ethanol the inhibition is secondary to decreased ribosomal dissociation. The cell-free lysate inhibition is also through this effect on ribosomal dissociation. This study supports the view that alcohol is a direct toxin to developing red cell precursors via its effect on mitochondrial haem synthesis. The physiological role of the decreased dissociation of monoribosomes into subunits is not yet clear.
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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/Acetaldehyde,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Ethanol,
http://linkedlifedata.com/resource/pubmed/chemical/Globins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Hemin,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0007-1048
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
351-63
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:1201218-Acetaldehyde,
pubmed-meshheading:1201218-Adenosine Triphosphate,
pubmed-meshheading:1201218-Animals,
pubmed-meshheading:1201218-Ethanol,
pubmed-meshheading:1201218-Globins,
pubmed-meshheading:1201218-Glutathione,
pubmed-meshheading:1201218-Hematopoiesis,
pubmed-meshheading:1201218-Heme,
pubmed-meshheading:1201218-Hemin,
pubmed-meshheading:1201218-Humans,
pubmed-meshheading:1201218-Polyribosomes,
pubmed-meshheading:1201218-Rabbits,
pubmed-meshheading:1201218-Reticulocytes,
pubmed-meshheading:1201218-Ribosomes,
pubmed-meshheading:1201218-Transferrin
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pubmed:year |
1975
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pubmed:articleTitle |
Ethanol inhibition of reticulocyte protein synthesis: the role of haem.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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