Two-dimensional electrophoretic analysis of ribosomal proteins from chronically injured liver.

Abstract

Proteins of the small and large ribosomal subunit, isolated at various times from long-term thioacetamide-damaged rat livers, were analysed by two-dimensional polyacrylamide gel electrophoresis and compared with those from normal liver. Chronic hepatic injury induced a number of time-dependent changes of the structural proteins of the small subunit, whereas the proteins of the large subparticle were essentially unaffected. The most significant alterations were an anodical dislocation of protein S6, a strong diminution in the amounts of proteins S9 and S10 and the occurrence of 3 to 4 additional small subunit proteins. By autoradiographic studies it was established that the modifications of S6 were brought about by an enhanced phosphorylation of this protein, which was the earliest sign of a ribosomal alteration in injured liver tissue.