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Blood, 15 December 2005, Vol. 106, No. 13, pp. 4367-4369. Prepublished online as a Blood First Edition Paper on September 8, 2005; DOI 10.1182/blood-2005-05-1813. This Article Full Text Full Text (PDF) All Versions of this Article: 2005-05-1813v1 106/13/4367    most recent Alert me when this article is cited 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 Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Costa, D. B. Articles by Forget, B. G. Search for Related Content PubMed PubMed Citation Articles by Costa, D. B. Articles by Forget, B. G. Related Collections Red Cells Cytoskeleton Free Research Articles Brief Reports Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  RED CELLS Brief report A novel splicing mutation of the -spectrin gene in the original hereditary pyropoikilocytosis kindred Daniel B. Costa, Larisa Lozovatsky, Patrick G. Gallagher, and Bernard G. Forget From the Departments of Medicine and Pediatrics, Yale University School of Medicine, New Haven, CT. Hereditary pyropoikilocytosis (HPP) is a severe hemolytic anemia due to abnormalities of the red blood cell (RBC) membrane skeleton. In the original HPP kindred, there is compound heterozygosity for an allele encoding a structural variant of -spectrin (L207P) and an -spectrin allele associated with a defect in -spectrin production. To identify the molecular defect in the production-defective allele, reticulocyte -spectrin cDNA from one of the original HPP patients was analyzed. Transcripts from the production-defective, non-L207P allele demonstrated a pattern of abnormal splicing between exons 22 and 23, resulting in insertion of intronic fragments with an in-frame premature termination codon. A G to A substitution at position +5 of the donor consensus splice site of IVS 22 was identified in the inserts. Following gene transfer into tissue culture cells, there was complete absence of normally spliced -spectrin gene transcripts derived from a minigene containing the IVS 22 +5 mutation. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: A cell by any other name Narla Mohandas Blood 2005 106: 4017. [Full Text] [PDF] This article has been cited by other articles: W. Tolpinrud, Y. D. Maksimova, B. G. Forget, and P. G. Gallagher Nonsense mutations of the {alpha}-spectrin gene in hereditary pyropoikilocytosis Haematologica, November 1, 2008; 93(11): 1752 - 1754. [Full Text] [PDF] X. Pei, X. Guo, R. Coppel, S. Bhattacharjee, K. Haldar, W. Gratzer, N. Mohandas, and X. An The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion Blood, August 1, 2007; 110(3): 1036 - 1042. [Abstract] [Full Text] [PDF]

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