Source:http://linkedlifedata.com/resource/pubmed/id/12514190
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2003-3-17
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pubmed:abstractText |
The full-length cDNA clone of a novel GRP78-binding protein (GBP) was isolated from rat brain using PCR-selected cDNA subtraction. GBP was predominantly expressed in neuronal cells among various brain tissues. GBP mRNA was already detected in the E12 brain and then gradually increased to reach a peak within P0-2 weeks after birth. GBP expression in the brain decreased age-dependently to approximately 30% of the postnatal level at 12 months. GBP encoded 1021 amino acids and was predicted to have two transmembrane regions and glutamic acid- and proline-rich regions. Because the sequence of GBP offered few clues to the possible function, we performed a GST-tagged GBP pull-down assay in PC12 lysates and identified GRP78, one of the heat shock proteins, as a counterpart. Observation of COS7 cells expressing green fluorescent protein- or Myc-tagged GBP showed that GBP was localized in the endoplasmic reticulum-Golgi domain where BODIPY 558/568 (4,4-difluro-5-(2-thienyl)-4-bora-3alpha,4alpha-diaza-S-indacene)-labeled brefeldin A accumulated. To investigate a biological role for GBP, we established Neuro2a cells stably expressing Myc-tagged GBP. Overexpression of GBP did not affect cell growth or morphological features but attenuated the time-dependent decrease in cell viability caused by serum deprivation compared with control cells. After 48 h of serum starvation, Neuro2a cells overexpressing GBP were resistant to the cell death induced by serum withdrawal. These results suggest that GBP would have a relevant functional role in embryonic and postnatal development of the brain.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/molecular chaperone GRP78
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10531-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12514190-Amino Acid Sequence,
pubmed-meshheading:12514190-Animals,
pubmed-meshheading:12514190-Base Sequence,
pubmed-meshheading:12514190-Brain Chemistry,
pubmed-meshheading:12514190-COS Cells,
pubmed-meshheading:12514190-Carrier Proteins,
pubmed-meshheading:12514190-Cell Death,
pubmed-meshheading:12514190-Cloning, Molecular,
pubmed-meshheading:12514190-Heat-Shock Proteins,
pubmed-meshheading:12514190-Immunohistochemistry,
pubmed-meshheading:12514190-Molecular Chaperones,
pubmed-meshheading:12514190-Molecular Sequence Data,
pubmed-meshheading:12514190-RNA, Messenger,
pubmed-meshheading:12514190-Rats
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pubmed:year |
2003
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pubmed:articleTitle |
Cloning and characterization of a novel GRP78-binding protein in the rat brain.
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pubmed:affiliation |
Department of Anatomy and Neurobiology, Kyoto Prefectural University of Medicine, Kawaramachi-Hirokoji, Kamikyo-ku, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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