This Article Full Text Full Text (PDF) Purchase Article View Shopping Cart Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wang, S. Articles by Skogseid, B. Search for Related Content PubMed PubMed Citation Articles by Wang, S. Articles by Skogseid, B.

Subcellular Distribution of Phospholipase C Isoforms in Rodent Pancreas and Gastric Mucosa¹

Departments of Medicine Science (S.W., Y.Z., P.S., K.O., A.G., B.S.) and Genetics and Pathology (A.L.), University Hospital, S-751 85 Uppsala, Sweden

Address all correspondence and requests for reprints to: Britt Skogseid, M.D., Ph.D., Department of Medicine, University Hospital, S-751 85 Uppsala, Sweden. E-mail: Britt.Skogseid{at}medsci.uu.se

Phosphoinositide-specific phospholipase C (PLC) has been implicated as a participant in cell proliferation as well as enzyme and hormone secretion. Defining the subcellular distribution of PLC isoforms would possibly contribute to further understanding of their function. We investigated the intracellular distribution of four PLCs (ß1, ß2, ß3, and 1) in mouse pancreatic cells as well as mouse and rat gastric mucosa cells by ultrastructural immunocytochemistry. In pancreatic acinar cells, PLCß1 and PLC1 were demonstrated in the zymogen granules while PLCß2 was present in the granulae as well as the endoplasmic reticulum (ER), and PLCß3 was prominent in the ER. In the endocrine pancreas, PLCß2 immunolabeling was expressed in the secretory granulae of , ß, , and pancreatic polypeptide cells. PLCß3 showed a slight labeling in the nucleus and ER of all four pancreatic endocrine cell types while PLC1 was prominent in cell granulae. In the gastric mucosa cells, PLCß2 was highly expressed in the heterochromatin areas and in the ER of parietal, chief, mucous, and enterochromaffin-like cells. PLCß3 were expressed in a manner similar to PLCß2 in those cells; however, no immunoreaction was seen in the ER of parietal cell. PLC1 was demonstrated in the chief cell granulae. One possible, although yet speculative, interpretation of our results is that the studied PLC isoforms may be involved in processing in pancreatic secretory granulae and that nuclear PLCß2 and PLCß3 signaling pathways may be operative in the cells of the gastric mucosa.

This article has been cited by other articles:

				M. E. Doyle and J. M. Egan Pharmacological Agents That Directly Modulate Insulin Secretion Pharmacol. Rev., March 1, 2003; 55(1): 105 - 131. [Abstract] [Full Text] [PDF]

				A. Sawaguchi, K. Ishihara, J.-i. Kawano, T. Oinuma, K. Hotta, and T. Suganuma Fluid Dynamics of the Excretory Flow of Zymogenic and Mucin Contents in Rat Gastric Gland Processed by High-pressure Freezing/Freeze Substitution J. Histochem. Cytochem., February 1, 2002; 50(2): 223 - 234. [Abstract] [Full Text] [PDF]