Ksp-cadherin is a functional cell–cell adhesion molecule related to LI-cadherin

• Published in: Experimental cell research Vol. 294; no. 2; pp. 345 - 355
• Main Authors: Wendeler, M.W, Praus, M, Jung, R, Hecking, M, Metzig, C, Geßner, R
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01-04-2004
• Subjects: 7D-cadherins; Animals; Antibodies - pharmacology; Beta-catenin; Cadherins - metabolism; Calcium Signaling - physiology; Carrier Proteins - metabolism; Cell adhesion; Cell Adhesion - physiology; Cell Aggregation - physiology; Cell aggregation assay; Cell clusters; Cell Communication - physiology; Cell morphology; Cell Size - physiology; Cell–cell adhesion; CHO Cells; Cricetinae; Cytoskeletal Proteins - metabolism; E-cadherin; Epithelial Cells - metabolism; Fluorescent Antibody Technique; Ksp-cadherin; LI-cadherin; Membrane Transport Proteins; Mice; Mice, Inbred C57BL; Protein Structure, Tertiary - physiology; Trans-Activators - metabolism; Cell aggregation assay; Beta-catenin; Ksp-cadherin; Cell adhesion; LI-cadherin; 7D-cadherins; Cell clusters; E-cadherin; Cell morphology; Cell–cell adhesion
• ISSN: 0014-4827; 1090-2422
• DOI: 10.1016/j.yexcr.2003.11.022

Ksp- and LI-cadherin are structurally homologous proteins coexpressed with E-cadherin in renal and intestinal epithelia, respectively. Whereas LI-cadherin has been shown to mediate Ca
2+-dependent homotypic cell–cell adhesion independent of stable interactions with the cytoskeleton, little is known about the physiological role of Ksp-cadherin. To analyze its potential adhesive and morphoregulatory functions, we expressed murine Ksp-cadherin in CHO cells. In this report, we show that Ksp-cadherin induces homotypic and Ca
2+-dependent cell–cell adhesion that can be specifically blocked with antibodies raised against the cadherin repeats EC1 and EC2. Ksp-cadherin mediates about the same quantitative adhesive effect (aggregation index) as LI- and E-cadherin. However, the cellular phenotype induced by Ksp-cadherin resembles more closely that of LI- than E-cadherin. This could reflect our observation, that Ksp-cadherin, as well as LI-cadherin, does not directly interact with β-catenin. In conclusion, both cadherins are thus not only structurally but also functionally related and may share other functions within their respective epithelia.