Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1987-3-9
pubmed:databankReference
pubmed:abstractText
The 78-kDa glucose-regulated protein GRP78 is a stress-inducible protein ubiquitously expressed in animal cells. In this paper we show that the first exon of this endoplasmic reticulum-localized protein consists of an 18 amino acid leader sequence rich in hydrophobic residues, followed by a highly acidic mature N-terminus and an 11 amino acid domain that is shared by members of the 70-kDa heat shock protein family. The end of this shared domain also marks the beginning of the first intron of this gene. A DNA region upstream of the promoter element important for induction by calcium ionophore and by a temperature-sensitive mutation was identified by deletion analysis. Our results indicate that a region spanning from 85 to 480 nucleotides upstream of the major transcription initiation site is important for both induction conditions. With evidence suggesting that perturbations in protein glycosylation may be one of the common stimuli involved in transcription activation of the GRPs, we measured the rate of glycosylation during A23187, glucose starvation, and temperature-shift induced conditions. The inverse correlation observed between the rate of glycosylation and the steady-state level of the GRP78 transcripts lends support to this hypothesis.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-196769, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-198809, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-216013, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-217883, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-218220, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-2937542, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-2941719, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-3023878, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-3084497, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-3085957, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-3087629, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-3097027, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-3455894, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-3456160, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-3782307, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-3929069, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-4055909, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-4359531, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-557044, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-6037551, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-6246368, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-6294115, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-6301457, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-6406494, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-6484570, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-6583707, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-6707023, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-6946438, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-7143579, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-7204505, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-7328131, http://linkedlifedata.com/resource/pubmed/commentcorrection/3468506-7459679
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
680-4
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its regulatory sequences and the effect of protein glycosylation on its expression.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't