Protein synthesis and secretion by hamster, rat and mouse jejunum.

The synthesis and secretion of [35S]methionine-labelled proteins by hamster, rat and mouse jejunum has been measured in vitro after 60 min incubation in culture medium. Twenty-three major bands of radioactively labelled proteins were detected by PAGE analysis of enterocyte extracts. Three of these proteins having mol. wts of 28,000, 43,000 and 60,000 appeared to be synthesised preferentially by older enterocytes. A small number of radioactively labelled proteins also appeared in culture medium at the end of incubation. Three of these proteins, accounting for most of the recovered radioactivity, had mol. wts of 28,000, 43,000 and 60,000. Secretion of these proteins was inhibited by monensin. Further experiments showed these secreted proteins to be acidic and possibly glycoprotein in nature. Their rapid turnover, selective secretion and changing abundance in enterocytes of different ages all suggest that they may have important functions to perform in the intestine.