title: Distribution of cell membrane-associated proteins along the human nephron.
abstract: Cytoskeletal proteins associate with specific cell adhesion complexes and membrane proteins and influence the structural and functional organization of polarized epithelial cells in the kidney. Among such proteins that have been studied in cultured cell lines and in animals are the tight junction complex (ZO-1 and occludin), the adherens cell-cell adhesion complex (alpha-, beta-catenin and plakoglobin), and Na+,K+-ATPase, with its associated membrane skeleton proteins ankyrin and fodrin. Although abnormal distribution of these proteins has been implicated in the pathogenesis of various renal diseases, the relevance of these findings to corresponding disease of the human kidney remains to be established. As a first step towards elucidating a role for such proteins in human kidney disease, we undertook a histochemical analysis of the distribution of these proteins in biopsy specimens of human kidney taken from healthy kidney transplant donors. We found each protein to have a characteristic subcellular localization and an intensity of staining that varied among different segments of the nephron in a manner that is consistent with discrete, segmental nephron function.
authors.affiliation: Division of Nephrology, Stanford University School of Medicine, Stanford, California, USA.
authors.forename: O
authors.initials: O
authors.lastname: Kwon
authors.forename: B D
authors.initials: BD
authors.lastname: Myers
authors.forename: R
authors.initials: R
authors.lastname: Sibley
authors.forename: D
authors.initials: D
authors.lastname: Dafoe
authors.forename: E
authors.initials: E
authors.lastname: Alfrey
authors.forename: W J
authors.initials: WJ
authors.lastname: Nelson
mesh_terms: D000328:Adult; D017487:Ankyrins / Q000378:metabolism; D020346:Aquaporins / Q000378:metabolism; D002352:Carrier Proteins / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D051180:Desmoplakins; D003896:Desmosomes / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D008565:Membrane Proteins / Q000378:metabolism*; D008840:Microfilament Proteins / Q000378:metabolism; D008856:Microscopy, Fluorescence; D008875:Middle Aged; D009399:Nephrons / Q000378:metabolism*; D062793:Occludin; D010750:Phosphoproteins / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism; D019108:Tight Junctions / Q000378:metabolism; D015534:Trans-Activators; D062826:Zonula Occludens-1 Protein; D051178:alpha Catenin; D051176:beta Catenin; D051185:gamma Catenin; D013049:Spectrin
chemical_list: D017487:Ankyrins; D020346:Aquaporins; D002352:Carrier Proteins; D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; D051180:Desmoplakins; D008565:Membrane Proteins; D008840:Microfilament Proteins; D062793:Occludin; D010750:Phosphoproteins; D000254:Sodium-Potassium-Exchanging ATPase; D015534:Trans-Activators; D062826:Zonula Occludens-1 Protein; D051178:alpha Catenin; D051176:beta Catenin; D051185:gamma Catenin; D013049:Spectrin; C495273:CTNNA1 protein, human; C495270:CTNNB1 protein, human; C568985:OCLN protein, human; C569042:TJP1 protein, human