Serum Apolipoprotein AI Synthesis in Rat Hepatocytes and its Secretion as Proform
- 1 January 1983
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 364 (1) , 439-446
- https://doi.org/10.1515/bchm2.1983.364.1.439
Abstract
Rat hepatocytes in monolayer or suspension culture synthesize serum lipoprotein AI. It is secreted into the serum-free culture medium. Synthesis and secretion processes were studied in the presence of radiolabeled amino acids. The synthesis product of the hepatocytes and the secretion product from the medium were isolated by immunoprecipitation with a monospecific rabbit antiserum against rat apolipoprotein AI. The intracellular and secreted products were homogeneous and identical in polyacrylamide gel electrophoresis but had reduced electrophoretic mobility as compared to native apolipoprotein AI. They were submitted to automated Edman degradation. They were present in their proform, the N-terminus of which is extended by a hexapeptide. In the presence of rat serum the proform is proteolytically transformed into the mature form of apolipoprotein AI.This publication has 4 references indexed in Scilit:
- Cell-Free Translation of Human Liver Apolipoprotein AI and All mRNA Processing of Primary Translation ProductsHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- Characterization, cell-free synthesis and processing of apolipoprotein A-I of rat high-density lipoproteinsBiochemistry, 1981
- On the permeability to lissamine green and other dyes in the course of cell injury and cell deathExperimental Cell Research, 1961