Pancreatic gene expression is altered during acute experimental pancreatitis in the rat

Abstract

We investigated pancreatic gene expression in the rat in response to taurocholate-induced acute pancreatitis. Concentrations of transcripts encoding pancreatic protein showed noncoordinated alterations. Contents in amylase, trypsinogen I, chymotrypsinogen B, elastase 1, and procarboxypeptidase A mRNAs decreased by greater than 50% during the acute phase (days 0-2), whereas actin and lithostathine mRNAs increased 5 and 0.6 times, respectively, and pancreatitis-associated protein (PAP) mRNA increased greater than 200 times, indicating redirection of the pattern of gene expression. Synthesis of pancreatic proteins was also altered in a noncoordinated manner. During the acute phase, it decreased more for trypsinogen I and chymotrypsinogen B than for amylase and lipase, whereas synthesis of the PAP increased dramatically. For amylase and chymotrypsinogen B, we compared the patterns of changes in mRNA concentrations, rates of synthesis, and pancreatic contents. Changes in enzyme contents and synthetic rates were temporally correlated during the acute phase. On the contrary, changes in mRNA concentrations and enzyme synthesis were not coordinated, suggesting that control of synthesis partly occurred at the posttranscriptional level. It was concluded that induction of pancreatitis is accompanied by transcriptional and posttranscriptional modifications resulting in rapid and massive rearrangement of the pattern of pancreatic protein gene expression.

Distribution of lithostathine in the mouse lemur brain with aging and Alzheimer's-like pathology

“…Although its physiological function in digestive organs remains debated (Bimmler et al, 1997;De Reggi et al, 1998), the protein tightly binds calcium carbonate crystals, suggesting an inhibitory activity on CaCO 3 crystal growth, thus preventing lithiasis (Bernard et al, 1992;Geider et al, 1996;Gerbaud et 4 al., 2000;Lee et al, 2003) . It has also been shown that acute pancreatitis induces Reg1 gene expression and protein production in the pancreas (Dusetti et al, 1996;Iovanna et al, 1991). This increase of Reg1 protein is associated with Reg1 receptor mRNA (Kobayashi et al, 2000) suggesting that an upregulation of the receptor expression may also be important in the proliferative response of pancreatic regeneration (Bluth et al, 2006).…”

“…Originally identified as a secretory protein produced in pancreas by acinar cells (Iovanna et al, 1991), lithosthatine is very susceptible to self-proteolysis under specific pH conditions (Cerini et al, 1999).…”

Pancreas-specific RelA/p65 truncation increases susceptibility of acini to inflammation-associated cell death following cerulein pancreatitis

“…Digestive enzymes such as amylase and lipase are downregulated and newly synthesized proteins are overexpressed, including secretory proteins such as pancreatitis-associated protein 1 (PAP1; also known as peptide 23, Reg-2, or RegIIIβ) and islet neogenesis associated protein (INGAP) (6)(7)(8). PAP1, together with the isoforms PAP2 and PAP3, and the pancreatic stone protein (PAP/Reg) constitute a family of proteins that belong to the C-type lectin family (9).…”

Pancreatitis-associated Protein I (PAP I), an Acute Phase Protein Induced by Cytokines

“…The acute phase of pancreatitis is characterized by a pattern of changes in the expression of secretory proteins (1). Whereas expression of most pancreatic enzymes decreases, mRNA levels of the rat pancreatitis-associated protein (PAP) 1 increase dramatically.…”

“…Whereas expression of most pancreatic enzymes decreases, mRNA levels of the rat pancreatitis-associated protein (PAP) 1 increase dramatically. Recently, we have described two other PAP-related mRNAs and named the corresponding proteins PAP II and PAP III (2,3).…”