Tensin family members are cytoplasmic proteins that are localized to the integrin-mediated cell-basement membrane junctions and implicated in cytoskeletal organization, cell migration, and proliferation. The mammalian genome contains four paralogs, Tns1, Tns2, Tns3, and Tns4. Murine mutations in the Tns1 and Tns2 genes cause polycystic kidney disease and glomerular sclerosis, respectively, and Tns3-null mice exhibit an impaired intestinal epithelial development. However, the knowledge concerning the localization of each tensin is still fragmentary. In this study, the cellular and subcellular distributions of tensin members were defined and compared with each other. RT-PCR analysis indicated that Tns2 and Tns3 were more abundant in isolated glomeruli and that Tns1 was highly expressed in areas other than the glomeruli, but no Tns4 expression was observed in the kidney. All tensin members were detected in the small intestine. Immunohistochemical staining revealed that Tns1 was predominantly localized to the mesangium of glomeruli and renal tubules. In contrast, Tns2 and Tns3 were highly expressed in the podocytes and the partial collecting system. In the small intestine, Tns2 and Tns3 were highly expressed in crypt and villous epithelial cells. Furthermore, we found that Tns3 was colocalized with TJ protein ZO-1 in renal tubules. These results indicate distinct differences in the cellular expression of Tns1, Tns2, and Tns3, and suggest that they may be able to function independently of each other in the kidney and the small intestine.