The n-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function (Articolo in rivista)

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  • The n-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1182/blood-2005-07-2806 (literal)
Alternative label
  • Perrotta S, Borriello A, Scaloni A, De Franceschi L, Brunati AM, Turrini F, Nigro V, Miraglia del Giudice E, Nobili B, Conte ML, Rossi F, Iolascon A, Donella-Deana A, Zappia V, Poggi V, Anong W, Low P, Mohandas N, Della Ragione F. (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
    in Blood
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Perrotta S, Borriello A, Scaloni A, De Franceschi L, Brunati AM, Turrini F, Nigro V, Miraglia del Giudice E, Nobili B, Conte ML, Rossi F, Iolascon A, Donella-Deana A, Zappia V, Poggi V, Anong W, Low P, Mohandas N, Della Ragione F. (literal)
Pagina inizio
  • 4359 (literal)
Pagina fine
  • 4366 (literal)
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  • 106 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Univ Naples 2, Dipartimento Pediat, I-80138 Naples, Italy Univ Naples 2, Dept Biochem & Biophys F Cedrangolo, I-80138 Naples, Italy CNR, Prote & Mass Spectrometry Lab, Ist Ric Sistema Prod Anim Ambiente Mediterraneo, Naples, Italy Univ Naples 2, Dipartimento Patol Gen, I-80138 Naples, Italy Ist Telethon Genet & Med TIGEM, Naples, Italy Univ Federico II, Ctr Ingn Genet CEINGE, Naples, Italy Pausillipon Hosp, Naples, Italy Univ Verona, I-37100 Verona, Italy Univ Padua, Dept Biochem, Padua, Italy Univ Turin, Turin, Italy Purdue Univ, Dept Chem, W Lafayette, IN 47907 USA New York Blood Ctr, New York, NY 10021 USA (literal)
Titolo
  • The n-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function (literal)
Abstract
  • 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 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. (literal)
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