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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
1983-9-9
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pubmed:abstractText |
ADP-ribosylation of proteins was analyzed by in vivo labeling of cells with [3H]adenosine, followed by separation of their protein components by two-dimensional isoelectric focusing/NaDodSO4 polyacrylamide gel electrophoresis. We show here that in several cell types of avian and mammalian origin the major [34H]adenosine acceptor in vivo is a polypeptide with a Mr of 83,000 and isoelectric point of approximately equal to 5.3. This polypeptide is identical to one of the stress-inducible and glucose-regulated proteins (here called SP83) previously described in avian and mammalian cells. Snake venom phosphodiesterase digestion of purified 3H-labeled SP83 releases 5'-AMP and a minor fraction of 2'-(5"-phosphoribosyl)-5-AMP. In vitro labeling with [32P]NAD+ of total cell lysates made in the presence of non-ionic detergents also results in incorporation of radioactivity into SP83. Both of these results strongly suggest that the modification is an ADP-ribosylation. Heat shock and glucose starvation of cells induce a rapid and extensive decrease in the incorporation of ADP-ribose into SP83, suggesting that ADP-ribosylation may be important for the regulation of the function of this protein.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-110462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-164015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-165508,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-172024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-208069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-210449,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-274702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-423788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-4297784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-4371081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-5543668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-5646604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-569556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-570568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-6125514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-6247348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-6286632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-6294115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-6298601,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-6765171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-6806295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-6943552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-6946438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-6990412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-7110134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-7151177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-7174676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-7204495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-7204505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-7237559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-7263772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-7309789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6576354-7328131
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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 |
Aug
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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 |
80
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4664-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6576354-Adenosine,
pubmed-meshheading:6576354-Adenosine Diphosphate Ribose,
pubmed-meshheading:6576354-Animals,
pubmed-meshheading:6576354-Cells, Cultured,
pubmed-meshheading:6576354-Chick Embryo,
pubmed-meshheading:6576354-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6576354-Fibroblasts,
pubmed-meshheading:6576354-Glucose,
pubmed-meshheading:6576354-HSP70 Heat-Shock Proteins,
pubmed-meshheading:6576354-Heat-Shock Proteins,
pubmed-meshheading:6576354-Hot Temperature,
pubmed-meshheading:6576354-Kinetics,
pubmed-meshheading:6576354-Membrane Proteins,
pubmed-meshheading:6576354-Nucleoside Diphosphate Sugars,
pubmed-meshheading:6576354-Protein Processing, Post-Translational,
pubmed-meshheading:6576354-Proteins,
pubmed-meshheading:6576354-Tritium
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pubmed:year |
1983
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pubmed:articleTitle |
ADP-ribosylation of the Mr 83,000 stress-inducible and glucose-regulated protein in avian and mammalian cells: modulation by heat shock and glucose starvation.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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