Intense myristoylation of a single protein in the ocular lens

A single protein of the ocular lens was intensely myristoylated following short term incubation of cultured bovine lens epithelial cells and intact rat lenses with 3H-myristic acid. It was acidic (pI <5), about 19 kDa and present exclusively in the cytosol of both cultured epithelial cells and the epithelium of the young rat lens. Fiber cell proteins were not labeled. The myristoylated protein was not seen in the epithelium of the adult rat. Essentially no protein mass was evident in the 19-20 kDa range when samples of the labeled-soluble protein were fractionated by either HPLC coupled with SDS-PAGE or 2D-electrophoresis. These findings suggest that the myristoylated-soluble protein of 19 kDa in lens (p19L) is a rapidly-turning over minor protein likely associated with lens growth. The absence of any apparent membrane association for a myristoylated protein appears unusual. The trace nature of p19L has frustrated attempts at its identification by MALDI-MS.