Linked Life Data

7798219

Source:http://linkedlifedata.com/resource/pubmed/id/7798219

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
1995-1-24
pubmed:abstractText
The AE1 (band 3) protein mediates the exchange of anions across the erythrocyte plasma membrane and, via association with the adapter molecule, ankyrin (Ank1), forms the major link between the membrane and the underlying spectrin cytoskeleton. The major kidney isoform of AE1 (kAE1), a protein that is otherwise identical to erythroid AE1 but lacks the NH2-terminal 79 amino acids, is localized to the basolateral plasma membrane of acid-secreting (alpha-type) intercalated cells of distal nephron. It has been proposed that this polarized distribution of kAE1 is due, at least in part, to its association with the ankyrin-spectrin cytoskeleton. In this study, we have used cell-free binding assays to investigate the interaction of anion exchangers with an Ank1 fragment, R13-H, that contains the AE1 binding site. Microsomes from cells expressing full-length erythroid AE1 bound 125I-labeled R13-H, revealing the presence of both high (Kd = 12.5 nM) and low (Kd = 166 nM) affinity sites. This binding was specific, as evidenced by the failure to observe high affinity binding of 125I-R13-H to microsomes from cells transfected with vector alone or with AE1m, a mutant lacking the approximately 400 amino acid NH2-terminal cytoplasmic ankyrin binding domain. Using this assay, we could detect no high affinity association between kAE1 and 125I-R13-H. We conclude that the NH2-terminal 79 amino acids play an essential role in high affinity and specific binding of AE1 to Ank1.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32201-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
The major kidney AE1 isoform does not bind ankyrin (Ank1) in vitro. An essential role for the 79 NH2-terminal amino acid residues of band 3.
pubmed:affiliation
Department of Biological Sciences, Stanford University, California 94305-5020.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't