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First published online June 28, 2004
doi: 10.1242/10.1242/jcs.01163

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Enhanced podocalyxin expression alters the structure of podocyte basal surface

¹ Institute of Biology, National Center for Scientific Research `Demokritos', Agia Paraskevi, 15310 Athens, Greece
² Laboratory of Histology and Embryology, Medical School, University of Athens, 11527 Goudi, Athens, Greece
³ Department of Pediatrics, University of Michigan, 1500 E. Medical Center Drive, Ann Arbor, MI 48109, USA
⁴ Department of Clinical Pathology, University of Vienna, Währinger Gürtel 18-20, 1090 Vienna, Austria

^* Author for correspondence (e-mail: effie{at}bio.demokritos.gr)

Accepted 17 February 2004

Glomerular basement membrane (GBM) and podocalyxin are essential for podocyte morphology. We provide evidence of functional interconnections between basement membrane components (collagen IV and laminin), the expression of podocalyxin and the morphology of human glomerular epithelial cells (podocytes). We demonstrated that GBM and laminin, but not collagen IV, up-regulated the expression of podocalyxin. Scanning electron microscopy revealed that laminin induced a modified morphology of podocytes with process formation, which was more extensive in the presence of GBM. Under high magnification, podocytes appeared ruffled. Using transmission electron microscopy we observed that raised areas occurred in the basal cell surface. Furthermore, the presence of anti-podocalyxin antibody increased the extent of adhesion and spreading of podocytes to both collagen IV and laminin, thus podocalyxin apparently inhibits cell-matrix interactions. We also performed adhesion and spreading assays on podocytes grown under increased glucose concentration (25 mM). Under these conditions, the expression of podocalyxin was almost totally suppressed. The cells adhered and spread to basement membrane components but there was no increase in the extent of adhesion and spreading in the presence of anti-podocalyxin antibody, or ruffling of the cell edges. Additionally, in podocytes expressing podocalyxin, the presence of anti-podocalyxin antibody partially reversed the inhibition of adhesion to collagen IV provoked by anti-ß1 integrin antibody, thus podocalyxin should compete with ß1-related cell adhesion. We suggest that the observed podocalyxin-mediated inhibition of binding to the matrix could be in part responsible for the specialized conformation of the basal surface of podocytes.

Key words: Podocalyxin, Human glomerular epithelial cells, Collagen IV, Laminin, Glomerular basement membrane, Integrins

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