Binding of a 40-kDa Protein to the N-myc 3ʹ-Untranslated Region Correlates with Enhanced N-myc Expression in Human Neuroblastoma
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Subclones of neuronal (N) and non-neuronal (S) cells established from neuroblastoma tumors cultured in vitro differ in their growth characteristics and N-myc expression. N (W-N) cells derived from the NBL-W cell line express 5-fold higher levels of N-myc mRNA and 10-12-fold higher levels of protein than S cells (W-S), despite having the same N-myc copy number. This study demonstrates that the steady-state levels of N-myc are largely determined by differences in N-myc mRNA stability. The half-life of N-myc mRNA in the W-N cells is approximately 35 min compared with approximately 6 min in the W-S cells. Turnover of labile mRNAs is thought to be mediated in part by the interactions of trans-acting factors with elements within the 3'-untranslated region. RNA UV cross-linking assays using W-N cell lysate demonstrate abundant quantities of a protein complex that is 40 kDa in size (p40) that binds to the N-myc 3'-untranslated region. p40 is barely detectable in W-S cells. We have mapped two distinct regions within the 3'-UTR that specifically bind p40 (base pairs 5694-5715 and 6465-6482). Analysis of nine additional neuroblastoma cell lines shows that p40 activity correlates with enhanced expression of N-myc. p40 activity is also detected in 5 of 19 primary neuroblastomas, and activity is associated with clinically aggressive disease. In the accompanying study, we identify p40 as a member of the embryonic lethal abnormal vision (ELAV)-like family of RNA-binding proteins. Our studies…
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Aberrant expression or function of HuD has been detected in several cancers of the central and peripheral nervous system, most prominently neuroblastomas and small cell lung cancers.
“Aberrant expression or function of HuD has been detected in several cancers of the central and peripheral nervous system, most prominently NBs and SCLCs (Szabo et al. 1991; Dalmau et al. 1992; Chagnovich and Cohn 1996; Ball and King 1997; Schramm et al. 1999; Stawski et al. 2012).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Chagnovich and Cohn 1996
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References 48 · Cited by 37
- Authors
- Chagnovich, D., & Cohn, S. L.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Cohn, Susan L.
- ORCID
- Cohn, Susan L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-12
- Volume
- 271
- Issue
- 52
- Pages
- 33580-33586
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1988520219
- Cited by
- 37
- References
- 48
- Citations by year
- 2023: 1 · 2018: 1 · 2013: 1
- FWCI
- 3.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r29ca051061-02)
- National Cancer Institute (CA-51061, 5P30CA60553, P30CA060553)
- Topics
- Health Sciences › Medicine › Neurology › Neuroblastoma Research and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- MYCN, neuroblastoma, 3' untranslated region, mRNA stability, mRNA turnover, ELAV-like proteins, RNA-binding proteins, tumor cell phenotype, primary neuroblastoma
- MeSH terms
- ELAV-Like Protein 2, Binding Sites, Electrophoresis, Polyacrylamide Gel, Humans, Molecular Weight, Nerve Tissue Proteins, Neuroblastoma, Solubility, Transcription, Genetic, Proto-Oncogene Proteins c-myc, RNA-Binding Proteins, ELAV Proteins
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