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Journal of Lipid Research, Vol 36, 2374-2382, Copyright © 1995 by Lipid Research, Inc.
ML Jennens and ME Lowe
The pancreas contains three homologous proteins, colipase-dependent
pancreatic lipase (PL) and two recently described pancreatic lipase-
related proteins, PLRP1 and PLRP2. Rat (r) PLRP2 was first identified as a
zymogen granule membrane protein, GP-3. Subsequently, we showed that rPLRP2
could cleave fatty acids from triglycerides, but the kinetic properties of
rPLRP2 have not been further investigated. To further characterize rPLRP2,
we expressed the recombinant enzyme in a baculovirus system, purified the
secreted protein, and measured its kinetic properties. rPLRP2 had a broad
pH optimum and the curve was similar to that of rPL. At pH 7.5, rPLRP2
cleaved short, medium, and long chain triglycerides by a kinetic mechanism
that did not include interfacial activation. The activity against these
substrates was not affected by bile salts. In particular, rPLRP2 did not
show the bile salt inhibition typical of PL. Although colipase increased
rPLRP2 activity in the presence of bile salts, the increase was only 2- to
5- fold compared to the absolute requirement for colipase that rPL had
under these conditions. Finally, rPLRP2 could hydrolyze phospholipids, a
substrate poorly hydrolyzed by PL. Our characterization of rPLRP2
demonstrates clear differences among the kinetic properties of rPLRP2 and
rPL, rPLRP2, and PLRP2 homologues isolated from guinea pig and coypu
pancreas. These findings have important implications for the physiological
function of rPLRP2.
ARTICLES
Rat GP-3 is a pancreatic lipase with kinetic properties that differ from colipase-dependent pancreatic lipase
Department of Pediatrics, Washington University School of Medicine, St. Louis Children's Hospital, MO 63110, USA.
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