Disease relevance of PNLIPRP1

• Thus, prolonged infusion of EMU rich in PLRP leads to a hypercholesterolemia, or at least a dyslipoproteinemia, due to elevated LP-X, associated with a depletion of cells in CH, stimulating thus tissue cholesterogenesis [1].

High impact information on PNLIPRP1

• Despite their similar amino acid sequences, PTL, PLRP1, and PLRP2 differ in important kinetic properties [2].
• The two novel proteins show an amino acid sequence identity to hPL of 68 and 65% for hPLRP1 and 2, respectively [3].
• PURPOSE: In previous work, lacrimal glands of female mice were shown to express an mRNA encoding pancreatic lipase-related protein 1 (PLRP1), a member of the triacylglycerol lipase family [4].
• As soon as the EMU is infused, the PLRP enter into competition with the TAGRP, in the lipolysis process as well as for sites of binding and for catabolism [1].
• At present, it seems difficult to produce sufficiently stable parenteral EMU devoid of PLRP [1].

Biological context of PNLIPRP1

• An inactive pancreatic lipase-related protein is activated into a triglyceride-lipase by mutagenesis based on the 3-D structure [5].

Anatomical context of PNLIPRP1

• These two proteins were purified to homogeneity from canine pancreatic juice and no significant catalytic activity was observed with dog PLRP1 on any of the substrates tested: di- and tri-glycerides, phospholipids, etc [6].
• PLRP1 and PLRP2 were expressed in fetal pancreas, whereas PTL was not expressed until pups were several weeks old [7].
• Both classical pancreatic lipase (DPL) and pancreatic lipase-related protein 1 (DPLRP1) have been found to be secreted by dog exocrine pancreas [6].
• The metabolic fate of the PLRP is similar in several ways to that of the TAGRP: exchanges of PL with the PL of the different cellular membranes and of the lipoproteins; captation of free CH from these same structures; and enrichment in apolipoproteins [1].
• The sites for catabolism of the two types of PAR are not the same: adipose tissues and muscles utilize the fatty acids and monoacylglycerols released by the lipolysis of the TAGRP; hepatocytes take up their remnants; the RES and the hepatocytes participate in the catabolism of the PLRP and the LP-X [1].

Associations of PNLIPRP1 with chemical compounds

• Pure horse PL, horse PLRP2 and dog PLRP1 were incubated with RP solubilized in its physiological vehicles, i.e., triglyceride-rich lipid droplets, mixed micelles and vesicles [8].
• Pancreatic lipase and pancreatic lipase-related protein 2, but not pancreatic lipase-related protein 1, hydrolyze retinyl palmitate in physiological conditions [8].
• PLRP-1 has barely detectable activity against triolein, even with (pro)colipase present [9].
• Only Porcine Pancreatic Lipase (PPL) and recombinant Guinea Pig Pancreatic Lipase Related Protein of type 2 (r-GPL) hydrolyse pure tributyrin in the absence of any additive, as well as dicaprin films at low surface pressures [10].
• Samples were finally analyzed on a poly(styrene-divinylbenzene), PLRP-S 100 A (8 microns) 250 x 4.6 mm I.D. column at 60 degrees C and with a mobile phase consisting of acetonitrile-sodium octanesulphonate (pH 2.5; 0.02 M)-potassium phosphate buffer (pH 2.5; 0.2 M)-water (X:25:50:25-X, v/v, where X is variable) [11].

Other interactions of PNLIPRP1

• Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity [3].

Analytical, diagnostic and therapeutic context of PNLIPRP1

• The analytical method was liquid chromatography on a column packed with a poly(styrenedivinyl-benzene) material (8-microns PLRP-S 100 A) [12].
• The extracted HPOs were determined using a reversed phase polymer HPLC column (PLRP-S 100 A) and the gradient ion-pair mobile phase containing tetrabutylammonium chloride (5 mM) and EDTA (0.5 mM) [13].

References