HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Godbout, R. Articles by Bie, W. Search for Related Content PubMed PubMed Citation Articles by Godbout, R. Articles by Bie, W. Social Bookmarking                      What's this?

J Biol Chem, Vol. 273, Issue 33, 21161-21168, August 14, 1998

Overexpression of a DEAD Box Protein (DDX1) in Neuroblastoma and Retinoblastoma Cell Lines

From the Department of Oncology, Cross Cancer Institute and University of Alberta, 11560 University Ave., Edmonton, Alberta T6G1Z2, Canada

The DEAD box gene, DDX1, is a putative RNA helicase that is co-amplified with MYCN in a subset of retinoblastoma (RB) and neuroblastoma (NB) tumors and cell lines. Although gene amplification usually involves hundreds to thousands of kilobase pairs of DNA, a number of studies suggest that co-amplified genes are only overexpressed if they provide a selective advantage to the cells in which they are amplified. Here, we further characterize DDX1 by identifying its putative transcription and translation initiation sites. We analyze DDX1 protein levels in MYCN/DDX1-amplified NB and RB cell lines using polyclonal antibodies specific to DDX1 and show that there is a good correlation with DDX1 gene copy number, DDX1 transcript levels, and DDX1 protein levels in all cell lines studied. DDX1 protein is found in both the nucleus and cytoplasm of DDX1-amplified lines but is localized primarily to the nucleus of nonamplified cells. Our results indicate that DDX1 may be involved in either the formation or progression of a subset of NB and RB tumors and suggest that DDX1 normally plays a role in the metabolism of RNAs located in the nucleus of the cell.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				A. Pacheco, S. L. de Quinto, J. Ramajo, N. Fernandez, and E. Martinez-Salas A novel role for Gemin5 in mRNA translation Nucleic Acids Res., February 1, 2009; 37(2): 582 - 590. [Abstract] [Full Text] [PDF]

				F. V. Fuller-Pace DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation Nucleic Acids Res., September 10, 2006; 34(15): 4206 - 4215. [Abstract] [Full Text] [PDF]

				S. Sato, M. Fukasawa, Y. Yamakawa, T. Natsume, T. Suzuki, I. Shoji, H. Aizaki, T. Miyamura, and M. Nishijima Proteomic profiling of lipid droplet proteins in hepatoma cell lines expressing hepatitis C virus core protein. J. Biochem., May 1, 2006; 139(5): 921 - 930. [Abstract] [Full Text] [PDF]

				A. Weber, P. Imisch, E. Bergmann, and H. Christiansen Coamplification of DDX1 Correlates With an Improved Survival Probability in Children With MYCN-Amplified Human Neuroblastoma J. Clin. Oncol., July 1, 2004; 22(13): 2681 - 2690. [Abstract] [Full Text] [PDF]

				H.-C. Chen, W.-C. Lin, Y.-G. Tsay, S.-C. Lee, and C.-J. Chang An RNA Helicase, DDX1, Interacting with Poly(A) RNA and Heterogeneous Nuclear Ribonucleoprotein K J. Biol. Chem., October 18, 2002; 277(43): 40403 - 40409. [Abstract] [Full Text] [PDF]

				S. Bleoo, X. Sun, M. J. Hendzel, J. M. Rowe, M. Packer, and R. Godbout Association of Human DEAD Box Protein DDX1 with a Cleavage Stimulation Factor Involved in 3'-End Processing of Pre-mRNA Mol. Biol. Cell, October 1, 2001; 12(10): 3046 - 3059. [Abstract] [Full Text] [PDF]

				V. Drewett, H. Molina, A. Millar, S. Muller, F. v. Hesler, and P. E. Shaw DNA-bound transcription factor complexes analysed by mass-spectrometry: binding of novel proteins to the human c-fos SRE and related sequences Nucleic Acids Res., January 15, 2001; 29(2): 479 - 487. [Abstract] [Full Text] [PDF]

				J. Doorbar, R. C. Elston, S. Napthine, K. Raj, E. Medcalf, D. Jackson, N. Coleman, H. M. Griffin, P. Masterson, S. Stacey, et al. The E1and E4 Protein of Human Papillomavirus Type 16 Associates with a Putative RNA Helicase through Sequences in Its C Terminus J. Virol., November 1, 2000; 74(21): 10081 - 10095. [Abstract] [Full Text]

				P. Kannouche, P. Mauffrey, G. Pinon-Lataillade, M. G. Mattei, A. Sarasin, L. Daya-Grosjean, and J. F. Angulo Molecular cloning and characterization of the human KIN17 cDNA encoding a component of the UVC response that is conserved among metazoans Carcinogenesis, September 1, 2000; 21(9): 1701 - 1710. [Abstract] [Full Text] [PDF]

				V. Martelange, C. De Smet, E. De Plaen, C. Lurquin, and T. Boon Identification on a Human Sarcoma of Two New Genes with Tumor-specific Expression Cancer Res., July 1, 2000; 60(14): 3848 - 3855. [Abstract] [Full Text]

				A. T. Grundhoff, E. Kremmer, O. Tureci, A. Glieden, C. Gindorf, J. Atz, N. Mueller-Lantzsch, W. H. Schubach, and F. A. Grasser Characterization of DP103, a Novel DEAD Box Protein That Binds to the Epstein-Barr Virus Nuclear Proteins EBNA2 and EBNA3C J. Biol. Chem., July 2, 1999; 274(27): 19136 - 19144. [Abstract] [Full Text] [PDF]