Redistribution of protein kinase C isoforms in rat pancreatic acini during lactation and weaning

Abstract

Freshly enzymatically isolated pancreatic acini from lactating and weaning Wistar rats were used to investigate the role of protein kinase C (PKC) isoforms during these physiologically relevant pancreatic secretory and growth processes. The combination of immunoblot and immunohistochemical analysis shows that the PKC isoforms ¿, ¿, and ¿ are present in pancreatic acini from control, lactating and weaning rats. A vesicular distribution of PKC-¿, -¿, and -¿ was detected by immunohistochemical analysis in the pancreatic acini from all the experimental groups. PKC-¿ showed the strongest PKC immunoreactivity (PKC-IR). In this vesicular distribution, PKC-IR was located at the apical region of the acinar cells. No differences were observed between control, lactating and weaning rats. However, the immunoblot analysis of pancreatic PKC isoforms during lactation and weaning showed a significant translocation of PKC-¿ from the cytosol to the membrane fraction when compared with control animals. Translocation of PKC isoforms (¿, ¿ and ¿) in response to 12-O-tetradecanoyl phorbol 13-acetate (TPA) 1 ¿M (15 min, 37°C) was comparable in pancreatic acini from control, lactating and weaning rats. In the control group, a significant translocation of all the isoforms (¿, ¿ and ¿) from the cytosol to the membrane was observed. The PKC isoform most translocated by TPA was PKC-¿. In contrast, no statistically significant increase in PKC-¿ translocation was detected in pancreatic acini isolated from lactating or weaning rats. These results suggest that the PKC isoforms are already translocated to the surface of the acinar cells from lactating or weaning rats. In addition, they suggest that isoform specific spatial PKC distribution and translocation occur in association with the growth response previously described in the rat exocrine pancreas during lactation and weaning.