Source:http://linkedlifedata.com/resource/pubmed/id/11756190
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
2001-12-28
|
| pubmed:abstractText |
Human band 3 Walton is an AE1 mutation that results in the deletion of the 11 COOH-terminal amino acids of the protein and is associated with dominant distal renal tubular acidosis. The properties of band 3 Walton expressed with normal band 3 in the heterozygous mutant erythrocytes and the kidney isoform expressed in Xenopus oocytes and in the Madin-Darby canine kidney cell line were examined. The mutant erythrocytes have normal hematology but have reduced band 3 Walton content. Transport studies showed that erythrocyte band 3 Walton has normal sulfate transport activity, and kidney band 3 Walton has normal chloride transport activity when expressed in Xenopus oocytes. The mutant protein is clearly able to reach the cell surface of erythrocytes and oocytes. In contrast, while normal kidney band 3 was expressed at the cell surface in the kidney cell line, the Walton mutant protein was retained intracellularly within the kidney cells. The results demonstrate that band 3 Walton is targeted differently in erythrocytes and kidney cells and indicate that the COOH-terminal tail of band 3 is required to allow movement to the cell surface in kidney cells. It is proposed here that the mutant band 3 gives rise to dominant distal renal tubular acidosis by inhibiting the movement of normal band 3 to the cell surface. It is suggested that this results from the association of the normal and mutant proteins in band 3 hetero-oligomers, which causes the intracellular retention of normal band 3 with the mutant protein.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anion Exchange Protein 1...,
http://linkedlifedata.com/resource/pubmed/chemical/Anions,
http://linkedlifedata.com/resource/pubmed/chemical/Carbonic Anhydrases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/band 3 protein Memphis
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0006-4971
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
99
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
342-7
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:11756190-Acidosis, Renal Tubular,
pubmed-meshheading:11756190-Adult,
pubmed-meshheading:11756190-Amino Acid Sequence,
pubmed-meshheading:11756190-Animals,
pubmed-meshheading:11756190-Anion Exchange Protein 1, Erythrocyte,
pubmed-meshheading:11756190-Anions,
pubmed-meshheading:11756190-Base Sequence,
pubmed-meshheading:11756190-Biological Transport,
pubmed-meshheading:11756190-Carbonic Anhydrases,
pubmed-meshheading:11756190-Cell Membrane,
pubmed-meshheading:11756190-Erythrocyte Membrane,
pubmed-meshheading:11756190-Female,
pubmed-meshheading:11756190-Fluorescent Antibody Technique,
pubmed-meshheading:11756190-Gene Expression,
pubmed-meshheading:11756190-Heterozygote,
pubmed-meshheading:11756190-Humans,
pubmed-meshheading:11756190-Kidney,
pubmed-meshheading:11756190-Male,
pubmed-meshheading:11756190-Molecular Sequence Data,
pubmed-meshheading:11756190-Oocytes,
pubmed-meshheading:11756190-Protein Isoforms,
pubmed-meshheading:11756190-Sequence Deletion,
pubmed-meshheading:11756190-Transfection,
pubmed-meshheading:11756190-Xenopus
|
| pubmed:year |
2002
|
| pubmed:articleTitle |
Band 3 Walton, a C-terminal deletion associated with distal renal tubular acidosis, is expressed in the red cell membrane but retained internally in kidney cells.
|
| pubmed:affiliation |
Department of Biochemistry, School of Medical Sciences, University of Bristol, United Kingdom.
|
| pubmed:publicationType |
Journal Article,
Case Reports,
Research Support, Non-U.S. Gov't
|