Pax6 interacts with SPARC and TGF-β in murine eyes

PURPOSE To understand the mechanism of the function of paired box 6 (Pax6), a master regulator of eye development and functions, Pax6-interacting proteins were studied. It is presumed that the interaction of Pax6 with proteins in terms of morphogenesis and the maintenance of the functional anatomy of the eyes cannot be ignored. The interaction of Pax6 with matricellular protein and transforming growth factors (TGFs) is explored and presented in this report. METHODS Co-localization was studied through fluorescence microscopy. The physical interaction of Pax6 interacting proteins was explored through co-immunoprecipitation assay of samples from murine eyes. RESULTS It was interesting to observe the co-localization and physical interaction of Pax6, transforming growth factor-beta (TGF-β), and secreted protein acidic and rich in cysteine (SPARC) in murine eyes. CONCLUSIONS The interaction of Pax6, TGF-β, and SPARC in murine eyes indicates that Pax6 function is regulated through TGF-β, and SPARC influences the shuttling of Pax6 via the TGF-β/Smad signaling pathway.