Amino Acid Transport and Protein Synthesis in Human Normal and Cataractous Lenses

Abstract

The ability of normal and cataractous human lenses to accumulate amino acids and synthesize proteins was studied under organ culture conditions. As expected, normal lenses regulate their internal ion levels, accumulate amino acids against a concentration gradient, and continue to synthesize proteins even in advanced age (> 60 yrs).

The cataractous lenses fell basically into two groups. Those with a low internal sodium and calcium content behaved in a similar manner to normal lenses, but cataractous lenses with high sodium and calcium contents showed a markedly reduced ability to accumulate amino acid and synthesized less low molecular weight protein. They incorporated, however, a much higher proportion of labelled amino acid into high molecular weight protein.

While sodium appears to be the ion involved in changes in amino acid accumulation, calcium seems to play a critical role in the disturbance of lens protein synthesis and also protein-protein interaction. Both loss of protein and accumulation of high molecular weight aggregates may be due to modifications induced by the calcium-activated protease, calpain.

None of the changes appeared to be correlated with increasing nuclear brunescence.