Source:http://linkedlifedata.com/resource/pubmed/id/16118313
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
13
|
| pubmed:dateCreated |
2005-12-5
|
| pubmed:abstractText |
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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0006-4971
|
| pubmed:author |
pubmed-author:AnongWilliamW,
pubmed-author:BorrielloAdrianaA,
pubmed-author:BrunatiAnna MariaAM,
pubmed-author:ConteMaria LuisaML,
pubmed-author:De FranceschiLuciaL,
pubmed-author:Della RagioneFulvioF,
pubmed-author:Donella-DeanaAriannaA,
pubmed-author:IolasconAchilleA,
pubmed-author:LowPhilipP,
pubmed-author:MohandasNarlaN,
pubmed-author:NigroVincenzoV,
pubmed-author:NobiliBrunoB,
pubmed-author:PerrottaSilverioS,
pubmed-author:PoggiVincenzoV,
pubmed-author:RossiFrancescaF,
pubmed-author:ScaloniAndreaA,
pubmed-author:TurriniFrancescoF,
pubmed-author:ZappiaVincenzoV,
pubmed-author:del GiudiceEmanuele MiragliaEM
|
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
106
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
4359-66
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:16118313-Amino Acid Sequence,
pubmed-meshheading:16118313-Animals,
pubmed-meshheading:16118313-Anion Exchange Protein 1, Erythrocyte,
pubmed-meshheading:16118313-Base Sequence,
pubmed-meshheading:16118313-Erythrocyte Membrane,
pubmed-meshheading:16118313-Erythrocytes,
pubmed-meshheading:16118313-Fructose-Bisphosphate Aldolase,
pubmed-meshheading:16118313-Glucose,
pubmed-meshheading:16118313-Homozygote,
pubmed-meshheading:16118313-Humans,
pubmed-meshheading:16118313-Molecular Sequence Data,
pubmed-meshheading:16118313-Mutation,
pubmed-meshheading:16118313-Phosphorylation,
pubmed-meshheading:16118313-Plasmodium falciparum,
pubmed-meshheading:16118313-Protein Binding,
pubmed-meshheading:16118313-RNA, Messenger,
pubmed-meshheading:16118313-RNA Splicing
|
| pubmed:year |
2005
|
| pubmed:articleTitle |
The N-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function.
|
| pubmed:affiliation |
Department of Pediatrics, Second University of Naples, Italy. silverio.perrotta@unina2.it
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|