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Blood, 1 June 2006, Vol. 107, No. 11, pp. 4391-4398. Prepublished online as a Blood First Edition Paper on February 2, 2006; DOI 10.1182/blood-2005-12-4822. This Article Full Text (PDF) All Versions of this Article: 2005-12-4822v1 107/11/4391    most recent Alert me when this article is cited Alert me if a correction is posted 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 Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Cheli, Y. Articles by Kunicki, T. J Search for Related Content PubMed PubMed Citation Articles by Cheli, Y. Articles by Kunicki, T. J Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted December 6, 2005 Accepted January 25, 2006 hnRNP L regulates differences in expression of mouse integrin 21 Yann Cheli and Thomas J Kunicki* The Division of Experimental Hemostasis and Thrombosis of the Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA, USA * Corresponding author; email: tomk{at}scripps.edu. There is a two-fold variation in platelet integrin 21 levels among inbred mouse strains. Decreased 21 in four strains carrying ITGA2 haplotype 2 results from decreased affinity of heterogeneous nuclear ribonucleoprotein L (hnRNP L) for a six CA repeat sequence (CA6) within intron 1. Seven strains bearing haplotype 1 and a twenty-one CA repeat sequence at this position (CA21) express twice the level of platelet 21 and exhibit an equivalent gain of platelet function in vitro. By UV cross-linking and immunoprecipitation, hnRNP L binds more avidly to CA21, relative to CA6. By cell-free, in vitro mRNA splicing, decreased binding of hnRNP L results in decreased splicing efficiency and an increased proportion of alternatively spliced product. The splicing enhancer activity of CA21 in vivo is abolished by prior treatment with hnRNP L-specific siRNA. Thus, decreased surface 21 results from decreased ITGA2 pre-mRNA splicing regulated by hnRNP L and dependent upon CA repeat length at a specific site in intron 1. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. Nurden GPVI: the inside story Blood, August 27, 2009; 114(9): 1723 - 1724. [Abstract] [Full Text] [PDF] J. Yu, Y. Hai, G. Liu, T. Fang, S. K. P. Kung, and J. Xie The Heterogeneous Nuclear Ribonucleoprotein L Is an Essential Component in the Ca2+/Calmodulin-dependent Protein Kinase IV-regulated Alternative Splicing through Cytidine-Adenosine Repeats J. Biol. Chem., January 16, 2009; 284(3): 1505 - 1513. [Abstract] [Full Text] [PDF] B. J. Hamilton, X.-W. Wang, J. Collins, D. Bloch, A. Bergeron, B. Henry, B. M. Terry, M. Zan, A. J. Mouland, and W. F. C. Rigby Separate cis-trans Pathways Post-transcriptionally Regulate Murine CD154 (CD40 Ligand) Expression: A NOVEL FUNCTION FOR CA REPEATS IN THE 3'-UNTRANSLATED REGION J. Biol. Chem., September 12, 2008; 283(37): 25606 - 25616. [Abstract] [Full Text] [PDF] L.-H. Hung, M. Heiner, J. Hui, S. Schreiner, V. Benes, and A. Bindereif Diverse roles of hnRNP L in mammalian mRNA processing: A combined microarray and RNAi analysis RNA, February 1, 2008; 14(2): 284 - 296. [Abstract] [Full Text] [PDF]

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