Pancreatic Lipase, Colipase and Enterostatin — A Lipolytic Triad

  • Charlotte Erlanson-Albertsson
Part of the NATO ASI Series book series (NSSA, volume 266)


Fat digestion occurs in the duodenum by the concerted action of pancreatic lipase and colipase [1,2]. The purpose of the present work is to discuss some properties of these two proteins and the more recently discovered peptide enterostatin [3], released from pancreatic procolipase, acting as a feed-back signal for regulation of fat intake.


Insulin Secretion Bile Salt Lipoprotein Lipase Pancreatic Lipase Lipase Gene 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Borgström, B. and Erlanson-Albertsson, C. Pancreatic colipase, in: Lipases, Borgström, B. and Brockman, H.L., Elsevier North-Holland, Amsterdam 1984; 151–184.Google Scholar
  2. 2.
    Verger, R. Pancreatic lipase, in: Lipases, Borgström, B. and Brockman, H.L., Elsevier North Holland, Amsterdam 1984; 83–150.Google Scholar
  3. 3.
    Erlanson-Albertsson, C. Enterostatin - the pancreatic procolipase activation peptide - a signal for regulation of fat intake. Nutr. Rev. 50: 1992; 307–310.PubMedCrossRefGoogle Scholar
  4. 4.
    Persson, B., Bengtsson-Olivecrona, G., Enerbäck, S., Olivecrona, T., and Jörnvall, H. Structural features of lipoprotein lipase, lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase. Eur. J. Biochem. 179: 1989; 39–45.PubMedCrossRefGoogle Scholar
  5. 5.
    Winkler, F.K., D’Arcy, A., and Hunziker, W. Structure of human pancreatic lipase. Nature 343: 1990; 771–774.PubMedCrossRefGoogle Scholar
  6. 6.
    Mickel, F.S., Weidenbach, F., Swarovsky, B., La Forge, K.S., and Scheele, G.A. Structure of the canine pancreatic lipase gene. J. Biol. Chem. 264: 1989; 12895–12901.PubMedGoogle Scholar
  7. 7.
    Duan, R. and Erlanson-Albertsson, C. The anticoordinate changes of pancreatic lipase and colipase activity to amylase activity by adrenalectomy in normal and diabetic rats. Int. J. Pancreatology 6: 1990; 271–279.Google Scholar
  8. 8.
    Borgström, B. and Erlanson, C. Pancreatic lipase and colipase. Interactions and effects of bile salts and other detergents. Eur. J. Biochem. 37: 1973; 60–68.PubMedCrossRefGoogle Scholar
  9. 9.
    Verger, R. Enzyme kinetics of lipolysis. Methods in Enzymology 64; 1980; 340–392.PubMedCrossRefGoogle Scholar
  10. 10.
    Erlanson-Albertsson, C. Pancreatic colipase. Structural and physiological aspects. Biochim. Biophys. Acta 1125: 1992; 1–7.PubMedCrossRefGoogle Scholar
  11. 11.
    Patton, J., Albertsson, P.A., Erlanson, C., and Borgström, B. Binding of porcine pancreatic lipase and colipase in the absence of substrate studied by two-phase partition and affinity chromatography. J. Biol. Chem. 253: 1978; 4195–4202.PubMedGoogle Scholar
  12. 12.
    Larsson, A. and Erlanson-Albertsson, C. The identity and properties of two forms of activated colipase from porcine pancreas. Biochim. Biophys. Acta 664: 1981; 538–548.PubMedCrossRefGoogle Scholar
  13. 13.
    van Tilbeurgh, H., Sarda, L., Verger, R., and Cambillau, C. Structure of the pancreatic lipase-procolipase complex. Nature 359: 1992; 159–162.PubMedCrossRefGoogle Scholar
  14. 14.
    Erlanson, C. Chemical modification of pancreatic lipase. Effect on the colipasereactivated and true lipase activity. FEBS Letters 84: 1977; 79–82.CrossRefGoogle Scholar
  15. 15.
    Erlanson-Albertsson, C. and Larsson, A. Importance of the N-terminal sequence in porcine pancreatic colipase. Biochim. Biophys. Acta 665: 1981; 250–255.PubMedCrossRefGoogle Scholar
  16. 16.
    McIntyre, J.C., Hundley, P., and Behnke, W.D. The role of aromatic side chain residues in micelle binding by pancreatic colipase. Biochem. J. 245: 1987; 821–829.PubMedGoogle Scholar
  17. 17.
    van Tilbeurgh, H., Egloff, M.P., Martinez, C., Rugani, N., Verger, R., and Cambillau, C. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by x-ray crystallography. Nature 362: 1993; 814–820.PubMedCrossRefGoogle Scholar
  18. 18.
    Erlanson-Albertsson, C. and Akerlund, H.E. Conformational change in pancreatic lipase induced by colipase. FEBS Letters 144: 1982; 38–42.PubMedCrossRefGoogle Scholar
  19. 19.
    Borgström, B., Wieloch, T., and Erlanson-Albertsson, C. Evidence for a pancreatic procolipase and its activation by trypsin. FEBS Letters 108: 1979; 407–410.PubMedCrossRefGoogle Scholar
  20. 20.
    Erlanson-Albertsson, C., Jie, M., Okada, S., York, D., and Bray, G.A.. Pancreatic procolipase propeptide, enterostatin, specifically inhibits fat intake. Phys. Behay. 49: 1991; 1191–1194.CrossRefGoogle Scholar
  21. 21.
    Okada, S., York, D.A., Bray, G.A., and Erlanson-Albertsson, C. Enterostatin (ValPro-Asp-Pro-Arg) the activation peptide of procolipase selectively reduces fat intake. Phys. Behay. 49: 1991; 1185–1189.CrossRefGoogle Scholar
  22. 22.
    Davies, R.C., Xia, Y., Mohandas, T., Schotz, M.C., and Lusis, A.J.. Assignment of the human pancreatic colipase gene to chromosome 6p21.1 pter. Genomics 10: 1991; 262–265.CrossRefGoogle Scholar
  23. 23.
    Fukuoka, S.-I., Zhang, D.-E., Taniguchi, Y., and Scheele, G.A. Structure of the pancreatic colipase gene includes two protein binding sites in the promotor region. J. Biol. Chem. 268: 1993; 11312–11320.PubMedGoogle Scholar
  24. 24.
    Okada, S., York, D.A., and Bray, G.A. Procolipase mRNA: Tissue localization and effects of diet and adrenalectomy. Biochem. J. 292: 1993; 787–789.PubMedGoogle Scholar
  25. 25.
    Wicker, C. and Puigserver, A. Effects of inverse changes in dietary lipid and carbohydrate on the synthesis of some pancreatic secretory proteins. Fur. J. Biochem. 162: 1987; 25–30.Google Scholar
  26. 26.
    Duan, R.-D. and Erlanson-Albertsson, C. The effect of pretranslational regulation on synthesis of pancreatic colipase in streptozotocin-induced diabetes in rats. Pancreas 7: 1992; 465–471.PubMedCrossRefGoogle Scholar
  27. 27.
    Hildebrand, H., Borgström, B., Békâssy, A., Erlanson-Albertsson, C., and Helin, I. Isolated colipase deficiency in two brothers. Gut 23: 1982; 243–246.PubMedCrossRefGoogle Scholar
  28. 28.
    Duan, R.-D., Wicker, C., and Erlanson-Albertsson, C. Effect of insulin administration on contents, secretion and synthesis of pancreatic lipase and colipase in rats. Pancreas 6: 1991; 595–602.PubMedCrossRefGoogle Scholar
  29. 29.
    Duan, R. and Erlanson-Albertsson, C. Pancreatic lipase and colipase activity increase in pancreatic acinar tissue of diabetic rats. Pancreas 4: 1989; 329–334.PubMedCrossRefGoogle Scholar
  30. 30.
    Duan, R., Poensgen, J., Wicker, C., Weström, B., and Erlanson-Albertsson, C. Increase in pancreatic lipase and trypsinogen activities and their mRNA levels in streptozotocin - induced diabetic rats. Dig. Dis. Sci. 34: 1989; 1243–1248.PubMedCrossRefGoogle Scholar
  31. 31.
    Erlanson-Albertsson, C., Mei, J., Sörhede, M., and Ohlsson, A. Enterostatin - a new gut hormone that regulates appetite. The Faseb Journal 7: 1993; A 89 (Abstract).Google Scholar
  32. 32.
    Shargill, N.S., Tsujii, S., Bray, G.A., and Erlanson-Albertsson, C. Enterostatin suppresses food intake following injection into the third ventricle of rats. Brain Research 544: 1991; 137–140.PubMedCrossRefGoogle Scholar
  33. 33.
    Miner, J.L., Erlanson-Albertsson, C., Paterson, J.A., and Baile, C.A. Enterostatin and feed intake in sheep. (1993). Manuscript in preparation.Google Scholar
  34. 34.
    Weatherfood, S.C., Lattermann, D.F., Sipols, A.J., Chavez, M., Kermani, Z.R., York, F.S., Bray, G.A., Porte, D., Jr, and Woods, S.C. Intraventricular administration of enterostatin decreases food intake in baboons. Appetite 19: 1992; 225.CrossRefGoogle Scholar
  35. 35.
    Sörhede, M., Mei, J., and Erlanson-Albertsson, C. Enterostatin–a brain-gut peptide-regulating fat intake. J. Physiol. 87: 1993; 273–275.Google Scholar
  36. 36.
    Huneau, J.-F., Erlanson-Albertsson, C., and Tomé, D. Absorption of enterostatin across the rabbit ileum in vitro. The Faseb Journal 7: 1993; A 89 (Abstract).Google Scholar
  37. 37.
    Lin, L., Mc Clanahan, S., York, D.A., and Bray, G.A. The peptide enterostatin may produce early satiety. Physiol. Behay. 53: 1993; 789–794.CrossRefGoogle Scholar
  38. 38.
    Mei, J., Cheng, Y., and Erlanson-Albertsson, C. Enterostatin - its ability to inhibit insulin secretion and to decrease a lipid-enriched meal. Int. J. Obesity,1993. In press.Google Scholar
  39. 39.
    Okada, S., Lin, L., York, D.A., and Bray, G.A.. Chronic effects of intracerebral ventricular enterostatin in Osborne-Mendel rats fed a high-fat diet. Physiol. Behay. 54: 1993; 325–330.CrossRefGoogle Scholar
  40. 40.
    Sternby, B., Nilsson, A., Melin, T., and Borgström, B. Pancreatic lipolytic enzymes in human duodenal contents. Scand. J. Gastroenterol. 26: 1991; 859–866.PubMedCrossRefGoogle Scholar
  41. 41.
    Borgström, A., Erlanson-Albertsson, C., and Borgström, B. Pancreatic proenzymes are activated at different rates. Scand. J. Gastroenterol. 28: 1993; 455–459.PubMedCrossRefGoogle Scholar
  42. 42.
    Erlanson-Albertsson, C., Mei, J., and Thesleff, P. Enterostatin in man. Int. J. Obesity 16: 1992; 12 (Abstract).Google Scholar
  43. 43.
    Jacobs, F. Evolution and tinkering. Science 196: 1977; 1161–1166.CrossRefGoogle Scholar
  44. 44.
    Bowyer, R.C., Jehanli, A.M.T., Patel, G., and Hermon-Taylor, J.. Development of enzyme-linked immunosorbent assay for free human pro-colipase activation peptide (APGPR). Clin. Chim. Acta 200: 1991; 137–152.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Charlotte Erlanson-Albertsson
    • 1
  1. 1.Dpt Medical and Physiological Chemistry 4LundSweden

Personalised recommendations