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Vol. 9, Issue 6, 1425-1435, June 1998
8
1 and Potential Roles for This
Integrin-Ligand Interaction in Kidney Morphogenesis
Department of Physiology and Howard Hughes Medical Institute,
University of California San Francisco, San Francisco, California
94143-0724
Epithelio-mesenchymal interactions during kidney organogenesis are
disrupted in integrin 
8
1-deficient mice. However, the known ligands for integrin 81
fibronectin, vitronectin,
and tenascin-Care not appropriately localized to mediate all 81 functions in the kidney. Using a method of general utility for determining the distribution of unknown integrin ligands in
situ and biochemical characterization of these ligands, we identified osteopontin (OPN) as a ligand for 81. We have coexpressed the extracellular domains of the mouse 8 and 1 integrin
subunits as a soluble heterodimer with one subunit fused to alkaline
phosphatase (AP) and have used the 81-AP chimera as a
histochemical reagent on sections of mouse embryos. Ligand localization
with 81-AP in developing bone and kidney was observed to be
overlapping with the distribution of OPN. In "far Western" blots of
mouse embryonic protein extracts, bands were detected with sizes
corresponding to fibronectin, vitronectin, and unknown proteins, one of
which was identical to the size of OPN. In a solid-phase binding assay we demonstrated that purified OPN binds specifically to 81-AP. Cell adhesion assays using K562 cells expressing 81 were used to
confirm this result. Together with a recent report that anti-OPN antibodies disrupt kidney morphogenesis, our results suggest that interactions between OPN and integrin 81 may help
regulate kidney development and other morphogenetic processes.
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