BACKGROUND. Human pancreatic ribonuclease (RNase 1) is a pancreatic enzyme
that is present at high levels in the serum of most patients with pancreati
c adenocarcinoma. For this reason, the authors studied its patterns of expr
ession at the single-cell level in pancreatic adenocarcinoma tissues by imm
unohistochemical analysis and in situ hybridization (ISH).
METHODS. Immunohistochemical analysis with polyclonal antibodies against RN
ase 1 and by ISH with digoxigenin-labeled RNase 1 probe were used to detect
RNase 1 in the neoplastic cells of ductal type pancreatic adenocarcinomas.
RESULTS. Fifteen of 18 carcinoma samples were positive for RNase 1, demons
trating that the expression of ribonuclease that the authors observed previ
ously in human pancreatic adenocarcinoma cell lines was not an artifact of
cell culture. The authors also found RNase 1 in some of the metaplastic duc
ts and atrophic islets in 4 of 6 chronic pancreatitis samples, and they obs
erved RNase 1 immunostaining in hyperplastic ducts adjacent to one of the w
ell-differentiated adenocarcinomas.
CONCLUSIONS. The expression levels of RNase 1 by tumor cells from pancreati
c adenocarcinomas are consistent with the high RNase 1 levels found in the
serum of most patients with pancreatic adenocarcinoma. This expression of R
Nase 1, which is an acinar protein, demonstrates that the patterns of gene
expression in pancreatic adenocarcinoma are distinct from those of normal p
ancreatic duct cells. Conversely, RNase 1 expression levels in altered duct
al cells from some chronic pancreatitis tissues and hyperplastic ducts from
carcinoma tissues suggest that abnormal expression levels may be an early
event in pancreatic tumorigenesis. (C) 2000 American Cancer Society.