The stability of tyrosine aminotransferase and other proteins in enucleated rat hepatoma tissue culture cells

✍ Scribed by T. V. Gopalakrishanan; E. Brad Thompson

• Publisher: John Wiley and Sons
• Year: 1977
• Tongue: English
• Weight: 1017 KB
• Volume: 93
• Category: Article
• ISSN: 0021-9541
• DOI: 10.1002/jcp.1040930110

✦ Synopsis

Abstract

The role of the nucleus in bringing about the induction of tyrosine aminotransferase (TAT) by glucocorticosteroid hormone and its deinduction upon steroid removal has been studied in enucleated rat hepatoma tissue culture cells (FU5–5). Both processes require the presence of the nucleus. However, cytoplasts from preinduced cells show an intial rapid decline in enzyme activity immediately after enucleation followed by maintenance of a constant level of activity. This initial decline in enzyme activity can be partially prevented by trypan blue, an inhibitor of lysosomal activity. This suggests that the early fall in enzyme activity could be due to an increase in the level of lysosomal activity immediately after enucleation. The subsequent constant level of activity seems due to maintenance rather than synthesis and degradation since it is not affected by cycloheximide. The absence of degradation applies to other kinds of proteins in enucleated FU5–5 cells and enucleated mouse fibroblast L cells. Thsese experiments suggest that some kind of labile RNA or protein dependent on the presence of the nucleus is required for the degradation of all classes of proteins in diferent kinds of cells.