http://www.cnr.it/ontology/cnr/individuo/prodotto/ID51408
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)
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- 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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