Differential expression of cell-cell and cell-substratum adhesion proteins along the kidney nephron

• Published in: The American journal of physiology Vol. 269; no. 6 Pt 1; pp. C1433 - C1449
• Main Authors: Piepenhagen, P A, Nelson, W J
• Format: Journal Article
• Language: English
• Published: United States 01-12-1995
• Subjects: Animals; Antigens, CD - metabolism; Cell Adhesion Molecules - metabolism; Cytoskeletal Proteins - metabolism; Female; Fluorescent Antibody Technique; Immunoblotting; Integrin alpha6; Intercellular Junctions - metabolism; Laminin - metabolism; Mice; Mice, Inbred C57BL; Nephrons - cytology; Nephrons - metabolism; Subcellular Fractions - metabolism; Tissue Distribution
• ISSN: 0002-9513
• DOI: 10.1152/ajpcell.1995.269.6.c1433

Structural and functional differences among epithelial cells of kidney nephrons may be regulated by variations in cell-to-cell (cell-cell) and cell-to-substratum (cell-substratum) junctions. Using immunofluorescence microscopy, we demonstrate that the cadherin-associated proteins alpha- and beta-catenin are localized to basolateral membranes of cells in all nephron segments, whereas plakoglobin, a protein associated with both classical and desmosomal cadherins, is localized to noninterdigitated lateral membranes in the distal half of the nephron where it colocalizes with desmoplakin and cytokeratin K8. Plakoglobin is also present in capillary endothelial cells where staining for the other catenins and desmosomal proteins is not observed. Immunofluorescence for laminin A and alpha 6-integrin, proteins that mediate cell-substratum contacts, reveal no correlations with the other staining patterns observed. These data indicate that plakoglobin and beta-catenin subserve distinct functions in cell-cell adhesion and suggest that E-cadherin-mediated contacts generate a basal level of cell-cell adhesion, whereas desmosomal junctions provide additional strength to cell-cell contacts in the distal nephron.