| http://purl.uniprot.org/citations/17082197 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17082197 | http://www.w3.org/2000/01/rdf-schema#comment | "Mutations in the alpha-actinin-4 gene ACTN4 cause an autosomal dominant human kidney disease. Mice deficient in alpha-actinin-4 develop a recessive phenotype characterized by kidney failure, proteinuria, glomerulosclerosis, and retraction of glomerular podocyte foot processes. However, the mechanism by which alpha-actinin-4 deficiency leads to glomerular disease has not been defined. Here, we examined the effect of alpha-actinin-4 deficiency on the adhesive properties of podocytes in vivo and in a cell culture system. In alpha-actinin-4-deficient mice, we observed a decrease in the number of podocytes per glomerulus compared with wild-type mice as well as the presence of podocyte markers in the urine. Podocyte cell lines generated from alpha-actinin-4-deficient mice were less adherent than wild-type cells to glomerular basement membrane (GBM) components collagen IV and laminin 10 and 11. We also observed markedly reduced adhesion of alpha-actinin-4-deficient podocytes under increasing shear stresses. This adhesion deficit was restored by transfecting cells with alpha-actinin-4-GFP. We tested the strength of the integrin receptor-mediated linkages to the cytoskeleton by applying force to microbeads bound to integrin using magnetic pulling cytometry. Beads bound to alpha-actinin-4-deficient podocytes showed greater displacement in response to an applied force than those bound to wild-type cells. Consistent with integrin-dependent alpha-actinin-4-mediated adhesion, phosphorylation of beta1-integrins on alpha-actinin-4-deficient podocytes is reduced. We rescued the phosphorylation deficit by transfecting alpha-actinin-4 into alpha-actinin-4-deficient podocytes. These results suggest that alpha-actinin-4 interacts with integrins and strengthens the podocyte-GBM interaction thereby stabilizing glomerular architecture and preventing disease."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m605024200"xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/author | "Zhou J."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/author | "Sinha S."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/author | "Sugimoto H."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/author | "Pollak M.R."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/author | "Kalluri R."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/author | "Gerszten R.E."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/author | "Ingber D.E."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/author | "Dandapani S.V."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/author | "Matthews B.D."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/author | "Kolb R.J."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/pages | "467-477"xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/title | "Alpha-actinin-4 is required for normal podocyte adhesion."xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://purl.uniprot.org/core/volume | "282"xsd:string |
| http://purl.uniprot.org/citations/17082197 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17082197 |
| http://purl.uniprot.org/citations/17082197 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17082197 |
| http://purl.uniprot.org/uniprot/#_A0A1L1SV25-mappedCitation-17082197 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17082197 |
| http://purl.uniprot.org/uniprot/#_D3Z0L8-mappedCitation-17082197 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17082197 |
| http://purl.uniprot.org/uniprot/#_A0A1L1SVJ6-mappedCitation-17082197 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17082197 |
| http://purl.uniprot.org/uniprot/#_E9Q2W9-mappedCitation-17082197 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17082197 |
| http://purl.uniprot.org/uniprot/#_D3Z761-mappedCitation-17082197 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/17082197 |