Purpose. We previously demonst-ated that crystallins from young rats, but not from bovine, chick ot human, showed proteolytic insolubiuzatio However, nc data have directly tested if crystallm fragmerits from r:. dent lenses other than rat, become insoluble. Thus, the purposes ui inu experiment were to determine if cr/stallins from another dent, mouse, were susceptible to calpain-indud precipitation and if aging in mice abolished light scattering. Methods. Total soluble proteins from mouse lenses were proteolyzed by endogenous or exogenous m-calpain. Subsequent precipitation of crystall ns was measured by light scattering. SDS-PAGE and immunoblots fcr calpain assessed proteolysis of crystallins and activation of calpain Results. Total soluble proteins from young mouse showed massive light scattering, and this light scattering was associated with proteolysis of crystallins. Calpain molecule in incubation mixture decreased. This was further evidence for activation and subsequent degradation of m-calpain. The cause of the light scattering was due to activation of m-calpain since E64 inhibitor attenuated light scattering. Tola! so uble proteins from old mouse lenses did not show calpain-induced lig it scattering. Conclusions. These results suggested that prevention of light scattering during aging of mouse lenses may be loss in calpain activit/ and/or lack of protein susceptibility.
|Original language||English (US)|
|Journal||Investigative Ophthalmology and Visual Science|
|State||Published - Dec 1 1997|
ASJC Scopus subject areas
- Sensory Systems
- Cellular and Molecular Neuroscience