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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1992-3-31
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pubmed:abstractText |
Hereditary ovalocytes from a Mauritian subject are extremely rigid, with a shear elastic modulus about three times that of normal cells, and have increased resistance to invasion by the malaria parasite Plasmodium falciparum in vitro. The genetic anomaly resides in band 3; the protein gives rise to chymotryptic fragments with reduced mobility in SDS/polyacrylamide gel electrophoresis, but this is a result of anomalous binding of SDS and not a higher molecular weight. Analysis of the band 3 gene reveals (1) a point mutation (Lys56----Glu), which also occurs in a common asymptomatic band 3 (Memphis) variant and governs the electrophoretic properties, and (2) a deletion of nine amino acid residues, including a proline residue, encompassing the interface between the membrane-associated and the N-terminal cytoplasmic domains. The interaction of the mutant band 3 with ankyrin appears unperturbed. The fraction of band 3 capable of undergoing translation diffusion in the membrane is greatly reduced in the ovalocytes. Cells containing the asymptomatic band 3 variant were normal with respect to all the properties that we have studied. Possible mechanisms by which a structural change in band 3 at the membrane interface could regulate rigidity are examined.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
223
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pubmed:owner |
NLM
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pubmed:authorsComplete |
N
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pubmed:pagination |
949-58
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:1538405-Adult,
pubmed-meshheading:1538405-Animals,
pubmed-meshheading:1538405-Anion Exchange Protein 1, Erythrocyte,
pubmed-meshheading:1538405-Base Sequence,
pubmed-meshheading:1538405-Elasticity,
pubmed-meshheading:1538405-Elliptocytosis, Hereditary,
pubmed-meshheading:1538405-Erythrocyte Deformability,
pubmed-meshheading:1538405-Erythrocyte Membrane,
pubmed-meshheading:1538405-Erythrocytes, Abnormal,
pubmed-meshheading:1538405-Humans,
pubmed-meshheading:1538405-Male,
pubmed-meshheading:1538405-Membrane Fluidity,
pubmed-meshheading:1538405-Molecular Sequence Data,
pubmed-meshheading:1538405-Plasmodium falciparum
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pubmed:year |
1992
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pubmed:articleTitle |
Basis of unique red cell membrane properties in hereditary ovalocytosis.
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pubmed:affiliation |
Department of Biochemistry, University of Bristol, U.K.
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pubmed:publicationType |
Journal Article,
Case Reports,
Research Support, Non-U.S. Gov't
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