Linked Life Data

15528469

Source:http://linkedlifedata.com/resource/pubmed/id/15528469

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2004-11-26
pubmed:abstractText
Alpha-adducin polymorphism in humans is associated with abnormal renal sodium handling and high blood pressure. The mechanisms by which mutations in adducin affect the renal set point for sodium excretion are not known. Decreases in Na+,K+-ATPase activity attributable to endocytosis of active units in renal tubule cells by dopamine regulates sodium excretion during high-salt diet. Milan rats carrying the hypertensive adducin phenotype have a higher renal tubule Na+,K+-ATPase activity, and their Na+,K+-ATPase molecules do not undergo endocytosis in response to dopamine as do those of the normotensive strain. Dopamine fails to promote the interaction between adaptins and the Na+,K+-ATPase because of adaptin-mu2 subunit hyperphosphorylation. Expression of the hypertensive rat or human variant of adducin into normal renal epithelial cells recreates the hypertensive phenotype with higher Na+,K+-ATPase activity, mu2-subunit hyperphosphorylation, and impaired Na+,K+-ATPase endocytosis. Thus, increased renal Na+,K+-ATPase activity and altered sodium reabsorption in certain forms of hypertension could be attributed to a mutant form of adducin that impairs the dynamic regulation of renal Na+,K+-ATPase endocytosis in response to natriuretic signals.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1524-4571
pubmed:author
pubmed:issnType
Electronic
pubmed:day
26
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1100-8
pubmed:dateRevised
2011-7-12
pubmed:meshHeading
pubmed-meshheading:15528469-Adaptor Protein Complex 2, pubmed-meshheading:15528469-Adaptor Protein Complex mu Subunits, pubmed-meshheading:15528469-Amino Acid Substitution, pubmed-meshheading:15528469-Animals, pubmed-meshheading:15528469-Blood Pressure, pubmed-meshheading:15528469-Cell Line, pubmed-meshheading:15528469-Cytoskeletal Proteins, pubmed-meshheading:15528469-Dopamine, pubmed-meshheading:15528469-Endocytosis, pubmed-meshheading:15528469-Endosomes, pubmed-meshheading:15528469-Epithelium, pubmed-meshheading:15528469-Humans, pubmed-meshheading:15528469-Hypertension, pubmed-meshheading:15528469-Kidney Tubules, pubmed-meshheading:15528469-Microfilament Proteins, pubmed-meshheading:15528469-Mutagenesis, Site-Directed, pubmed-meshheading:15528469-Natriuresis, pubmed-meshheading:15528469-Opossums, pubmed-meshheading:15528469-Phosphoprotein Phosphatases, pubmed-meshheading:15528469-Protein Interaction Mapping, pubmed-meshheading:15528469-Protein Subunits, pubmed-meshheading:15528469-Rats, pubmed-meshheading:15528469-Rats, Mutant Strains, pubmed-meshheading:15528469-Recombinant Fusion Proteins, pubmed-meshheading:15528469-Sodium-Potassium-Exchanging ATPase, pubmed-meshheading:15528469-Structure-Activity Relationship, pubmed-meshheading:15528469-Transfection
pubmed:year
2004
pubmed:articleTitle
Hypertension-linked mutation in the adducin alpha-subunit leads to higher AP2-mu2 phosphorylation and impaired Na+,K+-ATPase trafficking in response to GPCR signals and intracellular sodium.
pubmed:affiliation
Department of Medicine, Atherosclerosis Research Unit, Membrane Signaling Networks, Karolinska Institutet, Karolinska University Hospital, S-171 76 Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural