Phosphoinositide-specific phospholipase C (PLC) has been implicated as a pa
rticipant in cell proliferation as well as enzyme and hormone secretion. De
fining the subcellular distribution of PLC isoforms would possibly contribu
te to further understanding of their function. We investigated the intracel
lular distribution of four PLCs (beta 1, beta 2, beta 3, and gamma 1) in mo
use pancreatic cells as well as mouse and rat gastric mucosa cells by ultra
structural immunocytochemistry. In pancreatic acinar cells, PLC beta 1 and
PLC gamma 1 were demonstrated in the zymogen granules while PLC beta 2 was
present in the granulae as well as the endoplasmic reticulum (ER), and PLC
beta 3 was prominent in the ER. In the endocrine pancreas, PLC beta 2 immun
olabeling was expressed in the secretory granulae of alpha, beta, delta, an
d pancreatic polypeptide cells. PLC beta S3 showed a slight labeling in the
nucleus and ER of all four pancreatic endocrine cell types while PLC gamma
1 was prominent in alpha cell granulae. In the gastric mucosa cells, PLC b
eta 2 was highly expressed in the heterochromatin areas and in the ER of pa
rietal, chief, mucous, and enterochromaffin-like cells. PLC beta 3 were exp
ressed in a manner similar to PLC beta 2 in those cells; however, no immuno
reaction was seen in the ER of parietal cell. PLC gamma 1 was demonstrated
in the chief cell granulae. One possible, although yet speculative, interpr
etation of our results is that the studied PLC isoforms may be involved in
processing in pancreatic secretory granulae and that nuclear PLC beta 2 and
PLC beta 3 signaling pathways may be operative in the cells of the gastric
mucosa.