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Gene Review

PNLIPRP1  -  pancreatic lipase-related protein 1

Homo sapiens

Synonyms: Inactive pancreatic lipase-related protein 1, PL-RP1, PLRP1
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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


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


Other interactions of PNLIPRP1


Analytical, diagnostic and therapeutic context of PNLIPRP1


  1. Phospholipid-rich particles in commercial parenteral fat emulsions. An overview. Bach, A.C., Férézou, J., Frey, A. Prog. Lipid Res. (1996) [Pubmed]
  2. Structure and activity of rat pancreatic lipase-related protein 2. Roussel, A., Yang, Y., Ferrato, F., Verger, R., Cambillau, C., Lowe, M. J. Biol. Chem. (1998) [Pubmed]
  3. Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. Giller, T., Buchwald, P., Blum-Kaelin, D., Hunziker, W. J. Biol. Chem. (1992) [Pubmed]
  4. mRNA encoding a new lipolytic enzyme expressed in rabbit lacrimal glands. Remington, S.G., Nelson, J.D. Invest. Ophthalmol. Vis. Sci. (2002) [Pubmed]
  5. An inactive pancreatic lipase-related protein is activated into a triglyceride-lipase by mutagenesis based on the 3-D structure. Bezzine, S., Roussel, A., de Caro, J., Gastinel, L., de Caro, A., Carrière, F., Leydier, S., Verger, R., Cambillau, C. Chem. Phys. Lipids (1998) [Pubmed]
  6. Reactivation of the totally inactive pancreatic lipase RP1 by structure-predicted point mutations. Roussel, A., de Caro, J., Bezzine, S., Gastinel, L., de Caro, A., Carrière, F., Leydier, S., Verger, R., Cambillau, C. Proteins (1998) [Pubmed]
  7. Discoordinate expression of pancreatic lipase and two related proteins in the human fetal pancreas. Yang, Y., Sanchez, D., Figarella, C., Lowe, M.E. Pediatr. Res. (2000) [Pubmed]
  8. Pancreatic lipase and pancreatic lipase-related protein 2, but not pancreatic lipase-related protein 1, hydrolyze retinyl palmitate in physiological conditions. Reboul, E., Berton, A., Moussa, M., Kreuzer, C., Crenon, I., Borel, P. Biochim. Biophys. Acta (2006) [Pubmed]
  9. Rat pancreatic lipase and two related proteins: enzymatic properties and mRNA expression during development. Payne, R.M., Sims, H.F., Jennens, M.L., Lowe, M.E. Am. J. Physiol. (1994) [Pubmed]
  10. Kinetic behaviour of pancreatic lipase in five species using emulsions and monomolecular films of synthetic glycerides. Gargouri, Y., Bensalah, A., Douchet, I., Verger, R. Biochim. Biophys. Acta (1995) [Pubmed]
  11. Liquid chromatographic separation of hexopyranosylated cytosine nucleosides from their degradation products. Thoithi, G., Van Schepdael, A., Herdewijn, P., Roets, E., Hoogmartens, J. Journal of pharmaceutical and biomedical analysis. (1997) [Pubmed]
  12. Evaluation of tetracycline raw materials and finished products found on the Kenyan market. Muritu, J.W., Kibwage, I.O., Maitai, C.K., Hoogmartens, J. Journal of pharmaceutical and biomedical analysis. (1994) [Pubmed]
  13. Liquid extraction and ion-pair HPLC for determination of hydrophilic 3-hydroxypyridin-4-one iron chelators. Liu, D.Y., Liu, Z.D., Lu, S.L., Hider, R.C. Journal of pharmaceutical and biomedical analysis. (1999) [Pubmed]
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