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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1978-12-27
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pubmed:abstractText |
Oxidized glutathione (GSSG) (0.02-0.5 mM) inhibits reticulocyte lysates by a mechanism similar to that observed in heme deficiency. Incubation of hemin-supplemented postribosomal supernates with GSSG results in the activation of a translational inhibitor [I(GSSG)]. The activation of I(GSSG) is enhanced by the presence of an energy-regenerating system. The simultaneous addition of 1 mM dithiothreitol blocks the activation of the GSSG-induced inhibitor; however, once inhibitor is formed, its activity is not affected by 1 mM dithiothreitol. GSSG-treated postribosomal supernates and partially purified preparations of I(GSSG) inhibit protein synthesis in hemin-supplemented lysates with biphasic kinetics. Inhibition by I(GSSG) is blocked by cyclic AMP (2-10 mM) and is potentiated by ATP (2 mM). The inhibition is also blocked or reversed by eukaryotic initiation factor eIF-2. The activation of I(GSSG) is accompanied by an increased cyclic AMP-independent protein kinase activity which phosphorylates the 38,000-dalton component (alpha subunit) of eIF-2; however, GSSG treatment of supernates does not alter the activity of the cyclic AMP-independent protein kinase activity that phosphorylates the 49,000-dalton polypeptide component (beta subunit) of eIF-2. These data indicate that GSSG treatment of reticulocyte lysates results in the activation of a protein kinase with inhibitory and phosphorylation properties similar to those of the heme-regulated cyclic AMP-independent protein kinase which is activated in heme deficiency.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-1008879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-1069987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-1201028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-173394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-177976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-184458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-184460,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-193100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-272639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-273238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-323054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-4363751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-4388022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-4512619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-4528029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-4528641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-4680051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-4762417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-4846277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-5037023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-5050922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-5128185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-5238986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-5266178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-5488930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-5546565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-559547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-5750729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-5803298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-618548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-782923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-788835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-805425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-836310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-907668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-921787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/279901-971309
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
75
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4110-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:279901-Cell-Free System,
pubmed-meshheading:279901-Depression, Chemical,
pubmed-meshheading:279901-Enzyme Activation,
pubmed-meshheading:279901-Glutathione,
pubmed-meshheading:279901-Kinetics,
pubmed-meshheading:279901-Macromolecular Substances,
pubmed-meshheading:279901-Peptide Chain Initiation, Translational,
pubmed-meshheading:279901-Peptide Initiation Factors,
pubmed-meshheading:279901-Phosphorylation,
pubmed-meshheading:279901-Protein Kinases,
pubmed-meshheading:279901-Reticulocytes
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pubmed:year |
1978
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pubmed:articleTitle |
Inhibition of protein synthesis initiation by oxidized glutathione: activation of a protein kinase that phosphorylates the alpha subunit of eukaryotic initiation factor 2.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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