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Blood, 15 December 2005, Vol. 106, No. 13, pp. 4359-4366. Prepublished online as a Blood First Edition Paper on August 23, 2005August 25, 2005; DOI 10.1182/blood-2005-07-2806. This Article Full Text (PDF) All Versions of this Article: 2005-07-2806v1 2005-07-2806v2 106/13/4359    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 Perrotta, S. Articles by Della Ragione, F. Search for Related Content PubMed PubMed Citation Articles by Perrotta, S. Articles by Della Ragione, F. Related Collections Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted July 14, 2005 Accepted August 12, 2005 The N-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function Silverio Perrotta*, Adriana Borriello, Andrea Scaloni, Lucia De Franceschi, Anna Maria Brunati, Francesco Turrini, Vincenzo Nigro, Emanuele Miraglia del Giudice, Bruno Nobili, Maria Luisa Conte, Francesca Rossi, Achille Iolascon, Arianna Donella-Deana, Vincenzo Zappia, Vincenzo Poggi, William Anong, Philip Low, Narla Mohandas, and Fulvio Della Ragione Department of Pediatrics, Second University of Naples, Naples, Italy Department of Biochemistry and Biophysics "F. Cedrangolo", Second University of Naples, Naples, Italy Proteomics and Mass Spectrometry Laboratory, I.S.P.A.A.M., National Research Council, Naples, Italy Clinical and Experimental Medicine, University of Verona, Verona, Italy Department of Biochemistry, University of Padova, Padova, Italy Biology, Genetics and Medicinal Chemistry, University of Torino, Torino, Italy Dipartimento di Patologia Generale, Second University of Naples and TIGEM, Naples, Italy Medical Genetics, University Federico II, CEINGE, Naples, Italy Pediatric Hematology-Oncology, Pausillipon Hospital, Naples, Italy Department of Chemistry, Purdue University, West Lafayette, IN, USA New York Blood Center, New York, NY, USA * Corresponding author; email: silverio.perrotta{at}unina2.it. The 911 amino acid band 3 (SLC4A1) is the major intrinsic membrane protein of red cells and is the principal Cl-/HCO3- exchanger. The N-terminal cytoplasmic domain of band 3 anchors the spectrin-based membrane skeleton to the lipid bilayer through its interaction with ankyrin and also binds glycolytic enzymes and hemoglobin. We identified a son of consanguineous marriage with severe anemia in association with marked deficiency of band 3 (12±4% of normal). Direct nucleotide sequencing of SLC4A1 gene demonstrated a single base substitution (T->C) at position +2 in the donor splice site of intron 2 resulting in the generation of a novel mutant protein. Biochemical characterization of the mutant protein showed that it lacked the first 11 N-terminal amino acids (Band 3 "Neapolis"). The expression of the mutant protein resulted in the complete absence of membrane bound aldolase and the mutant band 3 could not be tyrosine phosphorylated. The ability of the malarial parasite, P. falciparum, to invade these red cells was significantly decreased. The identification of a novel band 3 mutant and its structural and functional characterization enabled us to identify pivotal roles for the 11 N-terminal amino acids in several protein functions and, in turn, in red cell physiology. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Band 3 "Neapolis": ciao ciao aldolase Carlo Brugnara Blood 2005 106: 4024-4025. [Full Text] [PDF] This article has been cited by other articles: A. M. Toye, R. C. Williamson, M. Khanfar, B. Bader-Meunier, T. Cynober, M. Thibault, G. Tchernia, M. Dechaux, J. Delaunay, and L. J. Bruce Band 3 Courcouronnes (Ser667Phe): a trafficking mutant differentially rescued by wild-type band 3 and glycophorin A Blood, June 1, 2008; 111(11): 5380 - 5389. [Abstract] [Full Text] [PDF]

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