Linked Life Data

12411747

Source:http://linkedlifedata.com/resource/pubmed/id/12411747

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-11-4
pubmed:abstractText
Mutations in the gene encoding nonmuscle alpha-actinin-4 (actinin-4), an actin cross-linking protein, lead to congenital nephrosis. This suggests that actinin-4 is an essential component of the glomerular filtration barrier. In the present study, we attempted to purify actinin-4 from the mammalian kidney. We also examined an interaction of the protein with puromycin aminonucleoside (PAN), which can induce nephrosis in animals. A 100-kD protein reactive with antibody against muscle alpha-actinin was purified from the Triton-insoluble cytoskeleton of porcine kidney, by MgCl2 treatment, ammonium sulfate fractionation, and subsequent DEAE-cellulose chromatography and hydroxyapatite chromatography. Its partial amino acid sequence was then determined. A filamentous actin (F-actin)-binding activity of the purified protein was examined by a cosedimentation assay. Interactions of the purified protein and its fragments with PAN were analyzed by an affinity assay using PAN-Sepharose. Determined 134 amino acid sequences of the purified porcine renal 100-kD protein were completely identical with those deduced from nucleotide sequence of the cDNA encoding human actinin-4. The purified protein possessed the known function of alpha-actinin, the F-actin-binding activity, and was tightly bound to PAN. The PAN-binding site was mapped within a central rod domain of the protein, which is a possible interaction site for various cytoskeletal and transmembrane proteins. We have established an efficient purification method for renal actinin-4. Moreover, our findings indicate that the central rod domain of actinin-4 has a high affinity to PAN. In the PAN nephrosis animal model, actinin-4 might be a target protein from PAN nephrotoxicity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1660-2129
pubmed:author
pubmed:copyrightInfo
Copyright 2003 S. Karger AG, Basel
pubmed:issnType
Electronic
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
e27-35
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12411747-Actinin, pubmed-meshheading:12411747-Actins, pubmed-meshheading:12411747-Amino Acid Sequence, pubmed-meshheading:12411747-Animals, pubmed-meshheading:12411747-Binding Sites, pubmed-meshheading:12411747-Blotting, Western, pubmed-meshheading:12411747-Cytoskeleton, pubmed-meshheading:12411747-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:12411747-Humans, pubmed-meshheading:12411747-Kidney Glomerulus, pubmed-meshheading:12411747-Microfilament Proteins, pubmed-meshheading:12411747-Molecular Sequence Data, pubmed-meshheading:12411747-Molecular Weight, pubmed-meshheading:12411747-Peptide Fragments, pubmed-meshheading:12411747-Peptide Mapping, pubmed-meshheading:12411747-Peptides, pubmed-meshheading:12411747-Protein Binding, pubmed-meshheading:12411747-Protein Structure, Tertiary, pubmed-meshheading:12411747-Puromycin Aminonucleoside, pubmed-meshheading:12411747-Sequence Analysis, Protein, pubmed-meshheading:12411747-Swine
pubmed:year
2003
pubmed:articleTitle
Renal alpha-actinin-4: purification and puromycin aminonucleoside-binding property.
pubmed:affiliation
Third Department of Internal Medicine, Akita University School of Medicine, Akita, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't