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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2011-5-30
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pubmed:abstractText |
Pirh2 is an E3 ligase that negatively regulates p53 through both direct physical interaction and ubiquitin-mediated proteolysis. Here, we identified a novel Pirh2-interacting protein, AIG1, by yeast two-hybrid screening and confirmed its interaction with p53 both in vitro and in vivo. Quantitative real-time reverse transcription-PCR analysis showed that AIG1 expression levels were reduced in 50 out of 79 (63%) human hepatocellular carcinomas (HCCs) when compared to matched, non-cancerous liver tissue; levels were significantly different between HCCs with or without lymph node metastasis. Kaplan-Meier analysis indicated that the survival time of HCC patients down-regulated for AIG1 is much shorter than it is for patients up-regulated for AIG1 expression (p = 0.0313 as determined by the Log-rank test). Finally, AIG1 activated the nuclear factor of activated T cells (NFAT) signaling pathway in a dose-dependent manner when over-expressed in HEK293T cells. Our results suggest AIG1 could serve as a new biomarker for the diagnosis and prognostic evaluation of HCCs.
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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:issn |
1945-0508
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pubmed:author |
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pubmed:issnType |
Electronic
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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 |
834-42
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pubmed:meshHeading |
pubmed-meshheading:21622095-Amino Acid Sequence,
pubmed-meshheading:21622095-Animals,
pubmed-meshheading:21622095-Base Sequence,
pubmed-meshheading:21622095-Cell Line,
pubmed-meshheading:21622095-DNA Primers,
pubmed-meshheading:21622095-Female,
pubmed-meshheading:21622095-Humans,
pubmed-meshheading:21622095-Male,
pubmed-meshheading:21622095-Membrane Proteins,
pubmed-meshheading:21622095-Middle Aged,
pubmed-meshheading:21622095-Molecular Sequence Data,
pubmed-meshheading:21622095-NFATC Transcription Factors,
pubmed-meshheading:21622095-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:21622095-Sequence Homology, Amino Acid,
pubmed-meshheading:21622095-Signal Transduction,
pubmed-meshheading:21622095-Subcellular Fractions,
pubmed-meshheading:21622095-Two-Hybrid System Techniques,
pubmed-meshheading:21622095-Ubiquitin-Protein Ligases,
pubmed-meshheading:21622095-Ubiquitination
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pubmed:year |
2011
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pubmed:articleTitle |
AIG1 is a novel Pirh2-interacting protein that activates the NFAT signaling pathway.
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pubmed:affiliation |
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai, PR China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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