Renal @entity15168 : purification and XXXX -binding property.

@entity1 @entity535 @entity8723 @entity377 @entity3450 @entity7540 @entity15168 @entity8424 @entity1329 @entity8859
Mutations in the gene encoding nonmuscle @entity15168 ( @entity15168 ), an actin cross-linking protein, lead to congenital @entity3450 . This suggests that @entity15168 is an essential component of the glomerular filtration barrier. In the present study, we attempted to purify @entity15168 from the @entity1 kidney. We also examined an interaction of the protein with @entity8424 ( @entity7540 ), which can induce @entity3450 in animals. A 100-kD protein reactive with antibody against muscle @entity8859 was purified from the Triton-insoluble cytoskeleton of porcine kidney, by @entity8723 treatment, @entity1329 fractionation, and subsequent DEAE-cellulose chromatography and hydroxyapatite chromatography. Its partial @entity535 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 @entity7540 were analyzed by an affinity assay using @entity7540 -Sepharose. Determined 134 @entity535 sequences of the purified porcine renal 100-kD protein were completely identical with those deduced from @entity377 sequence of the cDNA encoding @entity1 @entity15168 . The purified protein possessed the known function of @entity8859 , the F-actin-binding activity, and was tightly bound to @entity7540 . The @entity7540 -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 @entity15168 . Moreover, our findings indicate that the central rod domain of @entity15168 has a high affinity to @entity7540 . In the @entity7540 @entity3450 animal model, @entity15168 might be a target protein from @entity7540 nephrotoxicity.
