Changes in nucleolar proteins and their phosphorylation patterns during liver regeneration.

Two-dimensional polyacrylamide gel electrophoresis of nucleolar proteins of rat liver revealed marked changes at various times after partial hepatectomy. Some of the non-histone protein spots including A11, A24, A25, C13, and C14 decreased in size and density. Others, including A15, B13, B16, B18, B24-25, B27, B33, B34, C1, C2, C8, C11, C17, and C23-24 were markedly increased in size and density. In vitro labeling of the nucleoli using [gamma-32P]ATP and subsequent analysis of the proteins by two-dimensional gel electrophoresis and autoradiography indicated that the uptake of 32P into proteins increased greatly during regeneration. In addition, the relative labelling of various spots changed throughout the regeneration process. With spot B33 as a reference, there was increased labeling of spots A1P, B2, B5, B24-25, C2, and C23-24 at 8 hours after hepatectomy. On the other hand, the labeling of spots A8P, A16, A20, B9, and B13 decreased at 8 hours after hepatectomy. Since the primary role of the nucleolus is the snythesis of ribosomal precursors, these changes in protein content and phosphorylation are presumably primarily associated with the increased processing and transport of peribosomal ribonucleoproteins in regenerating liver.