Ar. Prescott et al., THE INTERMEDIATE FILAMENT CYTOSKELETON OF THE LENS - AN EVER-CHANGINGNETWORK THROUGH DEVELOPMENT AND DIFFERENTIATION - A MINIREVIEW, Ophthalmic research, 28, 1996, pp. 58-61
In the eye lens, intermediate filament proteins form two morphological
ly distinct polymers, 10-nm intermediate-sized filaments and beaded fi
laments. Coincidently, the beaded filament polymer and the proteins fi
lensin and CP49 are specific to lens fibre cells and are therefore exc
ellent markers for fibre cell differentiation. In the adult lens, file
nsin and CP49 are maintained throughout all stages of lens fibre cell
differentiation whilst vimentin is apparently lost at a specific stage
from the deeper cortical fibres. The expression of CP49 and filensin
is coincident with the presence of beaded filaments suggesting these p
roteins are filament components. In association with alpha-crystallin,
CP49 and filensin form beaded filaments in vitro. During fibre cell d
ifferentiation, filensin and CP49 are post-translationally modified. I
n the case of filensin, proteolysis results in two functionally distin
ct fragment sets, one derived from the a-helical rod domain and the ot
her from the C-terminal tail domain of filensin. It is proposed that b
oth filensin and CP49 are critically involved in organising the cytopl
asmic and plasma membrane domains of the fibre cell and therefore esse
ntial to the optical properties of the lens.