Is actin in eye lens a possible factor in visual accomodation?

Actin has been purified from varius non-muscle cells and characterized by its molecular weight and ability to polymerize into filaments. Although the occurrence of this protein has been postulated in the mammalian eye lens after observation of actin-like filaments in the electron microscope, definite (bio)chemical proof has been provided only recently. Amino acid analysis, peptide mapping and affinity chromatography revealed the identity of lens actin with the corresponding protein in other tissues. As the filaments could be obtained by co-isolation with highly purified lens plasma membranes, we were interested to know how the actin-containing structures wre located in situ. In the experimental approach reported here, the indirect immunofluorescence technique (IFT) was applied to unfixed cryostat sections of lens tissue. The distribution of actin in calf, rat and pigeon lens is described, and evidence from this for the role of actin in visual accommodation discussed.