title: Localization of intercellular adherens junction protein p120 catenin during podocyte differentiation.
abstract: To reveal the role of cadherin complex in podocyte differentiation, the present study describes the localization of the cadherin complex, including p120 catenin (p120ctn), in the developing and in the aminonucleoside nephrosis (PAN nephrosis) rat kidney, by immunofluorescence microscopy and immunogold electron microscopy. p120ctn and beta-catenin were co-localized at the apical part of lateral cell membranes in presumptive podocytes of the S-shaped body, and their localization shifted to the basal margin of lateral cell membranes in the capillary loop stage. There was no expression of the cadherin complex at the slit diaphragm, the intercellular junction of mature podocytes. After the regression of the podocyte junctional structure in PAN nephrosis, the cadherin complex was not re-expressed. The dynamic changes in the localization of the cadherin complex suggest that the it plays an important role during podocyte differentiation, including the rearrangement of the intercellular junction and the formation of the slit diaphragm.
authors.affiliation: Department of Pathology, Institute of Clinical Medicine, University of Tsukuba, 1-1-1 Ten-nodai, Tsukuba, 305-8575, Ibaraki, Japan.
authors.forename: Joichi
authors.initials: J
authors.lastname: Usui
authors.forename: Hidetake
authors.initials: H
authors.lastname: Kurihara
authors.forename: Yujing
authors.initials: Y
authors.lastname: Shu
authors.forename: Shinsuke
authors.initials: S
authors.lastname: Tomari
authors.forename: Katsuyoshi
authors.initials: K
authors.lastname: Kanemoto
authors.forename: Akio
authors.initials: A
authors.lastname: Koyama
authors.forename: Tatsuo
authors.initials: T
authors.lastname: Sakai
authors.forename: Takamune
authors.initials: T
authors.lastname: Takahashi
authors.forename: Michio
authors.initials: M
authors.lastname: Nagata
mesh_terms: D022005:Adherens Junctions / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D000831:Animals, Newborn; D015820:Cadherins / Q000378:metabolism; D051177:Catenins; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D002454:Cell Differentiation / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D003598:Cytoskeletal Proteins / Q000378:metabolism; D004847:Epithelial Cells / Q000378:metabolism* / Q000648:ultrastructure; D005333:Fetus; D007150:Immunohistochemistry; D007678:Kidney Glomerulus / Q000196:embryology* / Q000378:metabolism* / Q000648:ultrastructure; D007684:Kidney Tubules / Q000196:embryology* / Q000378:metabolism* / Q000648:ultrastructure; D008297:Male; D008648:Mesoderm / Q000378:metabolism / Q000648:ultrastructure; D008854:Microscopy, Electron; D009401:Nephrosis / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology; D010750:Phosphoproteins / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D017208:Rats, Wistar; D015534:Trans-Activators / Q000378:metabolism; D051176:beta Catenin; D000095002:Delta Catenin
chemical_list: D015820:Cadherins; D051177:Catenins; D015815:Cell Adhesion Molecules; C495268:Ctnnb1 protein, rat; D003598:Cytoskeletal Proteins; D010750:Phosphoproteins; D015534:Trans-Activators; D051176:beta Catenin; D000095002:Delta Catenin; C000722355:Ctnnd1 protein, rat