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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 25, 2005; DOI 10.1182/blood-2005-07-2806.
RED CELLS The N-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 functionFrom the Department of Pediatrics and Department of Biochemistry and Biophysics "F. Cedrangolo," Second University of Naples; and Proteomics and Mass Spectrometry Laboratory, Istituto di Ricerche per il Sistema Produzione Animale in Ambiente Mediterraneo (ISPAAM), National Research Council, Naples; and Dipartimento di Patologia Generale, Second University of Naples, and Istituto Telethon di Genetica e Medicina (TIGEM); and Medical Genetics, University Federico II, Centro di Ingegneria Genetica (CEINGE); and Pediatric Hematology-Oncology, Pausillipon Hospital, 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; Department of Chemistry, Purdue University, West Lafayette, IN; and New York Blood Center, New York, NY.
The 911 amino acid band 3 (SLC4A1) is the major intrinsic membrane protein of red cells and is the principal
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| Copyright © 2005 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
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 a 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. 
