Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1983-9-9
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.
pubmed:grant
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
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
80
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4664-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1983
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.
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