Source:http://linkedlifedata.com/resource/pubmed/id/15456855
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
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| pubmed:dateCreated |
2004-12-23
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| pubmed:abstractText |
Many genes are expressed in mammalian liver in a sexually dimorphic manner. DNA microarray analysis has shown that growth hormone (GH) and its sex-dependent pattern of pituitary secretion play a major role in establishing the sexually dimorphic patterns of liver gene expression. However, GH may exert effects on protein post-translational modification and nuclear localization that are not reflected at the mRNA level. To investigate these potential effects of GH, we used two-dimensional gel electrophoresis followed by LC-MS/MS to: 1) identify rat liver nuclear proteins whose abundance or state of post-translational modification displays sex-dependent differences; and 2) determine the role of the plasma GH profile in establishing these differences. Nuclear extracts prepared from livers of individual male (n=9) and female (n=5) adult rats, and from males given GH by continuous infusion for 7 days to feminize liver gene expression (n=5 rats), were resolved by two-dimensional electrophoresis. Image analysis of SYPRO Ruby-stained gels revealed 165 sexually dimorphic protein spots that differ in normalized volume between male and female groups by >1.5-fold at p<0.05. Sixty of these proteins exhibited female-like changes in spot abundance following continuous GH treatment. Comparison of male and GH-treated male groups revealed 130 proteins that displayed >1.5-fold differences in abundance, with 60 of these GH-responsive spots being sexually dimorphic. Thus, GH plays an important role in establishing the sex-dependent differences in liver nuclear protein content. Twenty-eight of the sexually dimorphic and/or GH-regulated protein spots were identified by LC-MS/MS. Proteins identified include regucalcin, nuclear factor 45, and heterogeneous nuclear ribonucleoproteins A3, D-like, and K, in addition to proteins such as GST, normally associated with cytosolic extracts but also reported to be localized in the nucleus.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
1535-9476
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
3
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1170-80
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:15456855-Animals,
pubmed-meshheading:15456855-Cell Nucleus,
pubmed-meshheading:15456855-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:15456855-Female,
pubmed-meshheading:15456855-Glutathione Transferase,
pubmed-meshheading:15456855-Growth Hormone,
pubmed-meshheading:15456855-Hydrogen-Ion Concentration,
pubmed-meshheading:15456855-Image Processing, Computer-Assisted,
pubmed-meshheading:15456855-Liver,
pubmed-meshheading:15456855-Male,
pubmed-meshheading:15456855-Oligonucleotide Array Sequence Analysis,
pubmed-meshheading:15456855-Peptides,
pubmed-meshheading:15456855-Protein Processing, Post-Translational,
pubmed-meshheading:15456855-RNA, Messenger,
pubmed-meshheading:15456855-Rats,
pubmed-meshheading:15456855-Rats, Inbred F344,
pubmed-meshheading:15456855-Sex Characteristics,
pubmed-meshheading:15456855-Sex Factors,
pubmed-meshheading:15456855-Time Factors
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| pubmed:year |
2004
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| pubmed:articleTitle |
Sexual dimorphism of rat liver nuclear proteins: regulatory role of growth hormone.
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| pubmed:affiliation |
Division of Cell and Molecular Biology, Department of Biology, Boston University, Boston, MA 02215, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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