Plasma protein induction by isolated hepatocytes.

Hepatocytes can be maintained in culture for periods of a few hours to many days. This review summarizes the metabolic characteristics of these cultures and describes their use in studying the regulation of plasma protein synthesis. Hormones selectively stimulate the synthesis of certain proteins. Cortisol stimulates the synthesis of fibrinogen and other acute-phase proteins; whereas, insulin stimulates albumin synthesis. In the latter case insulin increases the rate of a nuclear process. Mediators elaborated by leukocytes stimulate acute-phase protein synthesis in hepatocytes. Plasmin-generated fibrin peptides stimulate fibrinogen synthesis via a leukocytic mediator. Lipoprotein synthesis is stimulated by fatty acids and is inhibited by albumin and other macromolecules. These and other processes are susceptible to detailed analysis using sub-cellular fractions (mRNA, nuclei, transcription factors, etc.) isolated from hepatocytes. Studies on fetal or embryonic hepatocytes and hepatomas are yielding information on the regulation of secretory protein synthesis during development and following neoplastic transformation.