Linked Life Data

2085437

Source:http://linkedlifedata.com/resource/pubmed/id/2085437

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1991-5-23
pubmed:abstractText
Structural changes in human erythrocyte band 3 that affect anion transport are correlated with changes in glucose transport in situ. Breakdown of band 3, observed during normal erythrocyte aging in situ and in some diseases involving erythrocytes, is associated with an increase in Km and a decrease in Vmax of sulfate self-exchange, and with an increase in Km and Vmax of glucose efflux. Erythrocytes containing a high molecular weight form of band 3 exhibit an increase in Vmax of sulfate exchange and a decrease in Vmax of glucose efflux. Identical transport characteristics are observed in abnormal band-3-containing erythrocytes from individuals with familial amyotrophic chorea with acanthocytosis. A third band 3 alteration, fast-aging band 3, exhibits decreased Vmax of sulfate exchange and an increase in Km and decrease in Vmax of glucose efflux. Changes in band 3 structure that are the result of unstable hemoglobin or a deficiency in glucose-6-phosphate dehydrogenase and that do not affect anion transport have no effect on glucose transport characteristics. These data indicate the existence of a functional relationship between the membrane-spanning, anion-transport domain of band 3 and glucose transport in human erythrocytes. Antibodies to synthetic peptides reveal structural changes in membranes from the three inborn band 3 alterations and in band 3 itself in membranes from fast-aging band 3. Thus, immunological data suggests a structural relationship between anion and glucose transporters.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0829-8211
pubmed:author
pubmed:issnType
Print
pubmed:volume
68
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1419-27
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2085437-Amino Acid Sequence, pubmed-meshheading:2085437-Anion Exchange Protein 1, Erythrocyte, pubmed-meshheading:2085437-Anions, pubmed-meshheading:2085437-Antibodies, Monoclonal, pubmed-meshheading:2085437-Cytochalasin B, pubmed-meshheading:2085437-Erythrocyte Aging, pubmed-meshheading:2085437-Glucose, pubmed-meshheading:2085437-Glucosephosphate Dehydrogenase Deficiency, pubmed-meshheading:2085437-Hematologic Diseases, pubmed-meshheading:2085437-Humans, pubmed-meshheading:2085437-Kinetics, pubmed-meshheading:2085437-Molecular Sequence Data, pubmed-meshheading:2085437-Molecular Weight, pubmed-meshheading:2085437-Monosaccharide Transport Proteins, pubmed-meshheading:2085437-Peptide Fragments, pubmed-meshheading:2085437-Protein Conformation, pubmed-meshheading:2085437-Structure-Activity Relationship
pubmed:year
1990
pubmed:articleTitle
Alterations of band 3 transport protein by cellular aging and disease: erythrocyte band 3 and glucose transporter share a functional relationship.
pubmed:affiliation
Department of Medical Microbiology and Immunology, Texas A&M University, Temple 76504.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.