Human pancreatic lipase-related protein 2 (
HPLRP2) was previously found to be secreted by the exocrine pancreas.
HPLRP2 shows a high level of activity on
galactolipids, and might be involved in the digestion of these common vegetable
lipids. Specific
antibodies were raised in rabbits using a synthetic
HPLRP2 peptide selected for its weak
amino acid homology with the corresponding
peptides of classical human pancreatic
lipase (HPL) and human
pancreatic lipase-related protein 1 (HPLRP1). ELISA and Western blotting data showed that these
antibodies did not react with HPL or HPLRP1. Various tissues from the digestive tract were subjected to Western blotting analysis with the specific anti-
peptide HPLRP2 antibody and the expression of
HPLRP2 was detected in the pancreas and colon. An ELISA was developed for specifically measuring the
HPLRP2 levels in pure pancreatic juice. This procedure was performed using the anti-
peptide HPLRP2 antibody as the captor antibody and a biotinylated anti-HPLRP2 polyclonal antibody as the detector antibody. The lowest
HPLRP2 quantification limit was found to be 50 microg/L and the reference range for the present assay was 50 microg-500 microg/L. HPL and
HPLRP2 levels were measured using specific ELISAs in pancreatic juice from patients with and without pancreatic disorders. Patients with chronic calcifying
pancreatitis (CCP) had significantly lower levels of both HPL and
HPLRP2 than the controls subjects. The mean
HPLRP2 to HPL ratio was estimated to be 28.30% (w/w) and 23.96% (w/w) in controls subjects and CCP patients, respectively, and the difference was not significant. The levels of HPL and
HPLRP2 are therefore similarly reduced in both healthy patients and CCP patients.