Rm. Payne et al., RAT PANCREATIC LIPASE AND 2 RELATED PROTEINS - ENZYMATIC-PROPERTIES AND MESSENGER-RNA EXPRESSION DURING DEVELOPMENT, The American journal of physiology, 266(5), 1994, pp. 70000914-70000921
We report the cDNA sequences of rat colipase, rat pancreatic lipase (r
PL), and a rat pancreatic lipase-related protein (rPLRP). Comparison t
o the human PLRP cDNA suggests that the isolated clone encodes rPLRP-2
. Both cDNA and a third cDNA encoding rPLRP-1 are secreted from Sf9 ce
lls infected with recombinant baculovirus. rPL and rPLRP-2 hydrolyze t
riolein, 8.0 and 4.4 mu mol.min(-1).mu g(-1), respectively. They are i
nhibited by bile salts, and activity is restored by (pro)colipase. PLR
P-1 has barely detectable activity against triolein, even with (pro)co
lipase present. The pattern of mRNA expression during development in t
he rat reveals that all mRNA are low in the fetal rat pancreas. Both P
LRP mRNA rise just before birth to a maximum 12 h after birth. They fa
ll to low levels in the adult. In contrast, the PL mRNA is low at birt
h and rises rapidly during the suckling-weanling transition. In conclu
sion, the rat has at least three genes encoding different lipases, and
these related genes have separate regulatory controls.