Linked Life Data

1378323

Source:http://linkedlifedata.com/resource/pubmed/id/1378323

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-8-20
pubmed:abstractText
Protein 4.2 is a major red blood cell (RBC) protein that interacts with the band 3 protein and with ankyrin. Inherited deficiencies of this protein are associated with spherocytic hemolytic anemia, but the molecular basis of this defect is unknown. We have studied the underlying defect in a patient with spherocytic hemolytic anemia whose RBCs had a partial (29% +/- 5%) deficiency of protein 4.2. We have first studied the binding of normal ankyrin and protein 4.2 to patient inside-out vesicles (IOVs) stripped of peripheral proteins. While the binding of ankyrin was normal, the predicted maximal binding capacity of patient IOVs for band 4.2 was 20% to 33% lower than that of control IOVs, suggesting a defect in the cytoplasmic domain of band 3 (cdb3). An additional line of evidence pointing to a possible abnormality of band 3 was an abnormal proteolytic digest of cdb3. To elucidate the underlying molecular defect, we have cloned and sequenced the cDNA coding for cdb3 from the patient. One band 3 allele was found to be normal, while clones corresponding to the other allele contained two mutations: substitution A----G in nucleotide 166, changing codon 56 from AAG to GAG (Lys----Glu), and substitution C----G in nucleotide 980, changing codon 327 from CCC to CGC (Pro----Arg). Since the Lys56----Glu56 substitution is found in a common asymptomatic variant of the band 3 protein designated band 3 Memphis, we conclude that either the Pro327----Arg327 substitution itself, or in combination with the band 3 Memphis polymorphism, underlies the abnormal binding of protein 4.2 to cdb3 and results in the spherocytic phenotype.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
80
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
523-9
pubmed:dateRevised
2011-6-20
pubmed:meshHeading
pubmed-meshheading:1378323-Amino Acid Sequence, pubmed-meshheading:1378323-Anemia, Hemolytic, pubmed-meshheading:1378323-Animals, pubmed-meshheading:1378323-Anion Exchange Protein 1, Erythrocyte, pubmed-meshheading:1378323-Ankyrins, pubmed-meshheading:1378323-Arginine, pubmed-meshheading:1378323-Base Sequence, pubmed-meshheading:1378323-Blood Proteins, pubmed-meshheading:1378323-Cytoskeletal Proteins, pubmed-meshheading:1378323-DNA, pubmed-meshheading:1378323-Erythrocyte Membrane, pubmed-meshheading:1378323-Female, pubmed-meshheading:1378323-Humans, pubmed-meshheading:1378323-Kinetics, pubmed-meshheading:1378323-Male, pubmed-meshheading:1378323-Membrane Proteins, pubmed-meshheading:1378323-Molecular Sequence Data, pubmed-meshheading:1378323-Mutation, pubmed-meshheading:1378323-Oligodeoxyribonucleotides, pubmed-meshheading:1378323-Polymerase Chain Reaction, pubmed-meshheading:1378323-Proline, pubmed-meshheading:1378323-Protein Binding, pubmed-meshheading:1378323-RNA, pubmed-meshheading:1378323-Reticulocytes, pubmed-meshheading:1378323-Sequence Homology, Nucleic Acid
pubmed:year
1992
pubmed:articleTitle
Band 3 Tuscaloosa: Pro327----Arg327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2.
pubmed:affiliation
Department of Biomedical Research, St. Elizabeth's Hospital of Boston, Tufts University School of Medicine, MA 02135.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Case Reports