Stability of the mRNA encoding some pancreatic hydrolases is modulated by dietary protein intake in the rat

Abstract

Wistar rats fed on either a high-protein or a protein-free diet were examined to determine their pancreatic hydrolase mRNA stabilities in comparison with those of control animals receiving a standard diet. Actinomycin D was used to inhibit transcription and, after isolating the pancreatic RNA, the specific messengers were quantified by performing dot-blot hybridization with cDNA probes. In the rats fed on a high-protein diet, only the half-lives of anionic trypsinogen I and elastase I (EC3.4.21.36) were affected. Interestingly, when rats were fed on the protein-free diet, most of the hydrolase mRNA half-lives showed changes, except that corresponding to lipase. In these rats, the half-life values of the mRNA coding for anionic trypsinogen I, chymotrypsinogen and procarboxypeptidase B increased, in sharp contrast with those of the amylase and elastase I mRNA, which decreased. These results strongly suggest that the mechanism whereby the biosynthesis of pancreatic hydrolases is regulated, depending on the presence or absence of proteins in the diet, is not unique and provide evidence that the stability of mRNA encoding most, if not all, the hydrolases in pancreatic cells is modulated by the dietary protein content.