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Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA
¹ Laboratoire de Biologie de la Differentation et du Development, Universite Victor Segalen Bordeaux 2, 146 rue Leo Saignat 33076 Bordeaux cedex, France

(Requests for offprints should be addressed to N Sarvetnick; Email: noras{at}scripps.edu)

Activated signaling proteins regulate diverse processes, including the differentiation of the pancreatic islet cells during ontogeny. Here we uncover the in vivo phosphorylation status of major growth factor-activated signaling proteins in normal adult mice and during pancreatic islet regeneration. We report elevated phospho-mitogen-activated protein kinase (phospho-MAPK), phospho-c-Jun-NH₂-terminal kinase (phospho-JNK), and phospho-p38 MAPK expression during pancreatic regeneration. Immunoblotting experiments demonstrated elevated phosphorylation of p52 Src-homology/collagen (SHC) in the ductal network as well, substantiating the activation of this pathway. Furthermore, protein kinase B (PKB/Akt), a key signaling protein in the anti-apoptotic pathway, was phosphorylated to a greater extent in the ductal network from regenerating pancreas. We observed fibroblast growht factor (FGF)10 and platelet-derived growth factor (PDGF)AA expression in embryonic as well as regenerating adult pancreas. Epidermal growth factor (EGF) and PDGFAA stimulated MAPK and Akt phosphorylation, while FGF10 stimulated MAPK but not Akt phosphorylation in a time-dependent manner in freshly isolated cells from the adult ductal network. These data suggest that a heightened level of expression and stimulation of key signaling proteins underlie the expansion and differentiation processes that support pancreatic ontogeny and regeneration.

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				H. Hua, Y.-Q. Zhang, S. Dabernat, M. Kritzik, D. Dietz, L. Sterling, and N. Sarvetnick BMP4 Regulates Pancreatic Progenitor Cell Expansion through Id2 J. Biol. Chem., May 12, 2006; 281(19): 13574 - 13580. [Abstract] [Full Text] [PDF]