Pancreatic Cholesteryl Esterase in Health and Disease

  • Eric Mas
  • Dominique Lombardo
Part of the NATO ASI Series book series (NSSA, volume 266)


Pancreatic cholesterol esterase, also called carboxyl ester lipase or bile salt-dependent lipase (BSDL, E. C. 3. 1. 1.13), catalyzes the hydrolysis of ester substrates as well as some phospholipids and lysophospholipids[1]. In addition, the bile salt-dependent lipase is the unique enzyme in the pancreatic juice capable of hydrolyzing fat-soluble-vitamins and cholesteryl esters[2]. This latter function strongly suggests that BSDL is important for catalyzing the lymphatic absorption of dietary cholesterol and fat-soluble vitamins. BSDL from the rat, dog, pig, bovine and human pancreas has been purified to homogeneity. The molecular mass differs significantly among species[3]: human BSDL 100 kDa; dog 87–93 kDa; pig 80–90 kDa; bovine BSDL occurs predominantly as a 72 kDa protein; and that of the rat is 67 kDa. Recently, the full-length cDNA of pancreatic BSDL from different species has been cloned and sequenced[4–6]. Jacobson et al.[7] have reported that rat BSDL is a glycosylated protein which contains a potential N-linked glycosylation site at Asn at position 187, [4–6], this site is conserved in the bovine and human protein. The sugar composition of the human pancreatic BSDL agrees with the presence one N-linked oligosaccharide of complex or hybrid type and of 0-linked oligosaccharides[8]. The transfer en bloc of the precursor dolichol-pyrophosphate oligomannoside is essential for the setting up of the active conformation and secretion of the enzyme[9]. The trimming and the processing of the highmannose structure does not affect either the enzyme activity or its secretion[9].


Acute Pancreatitis Pancreatic Juice Human Pancreas Pancreatic Pathology Benign Liver Disease 
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  1. 1.
    D. Lombardo, J. Fauvel and O. Guy, Studies on the Substrate Specificity of a Carboxyl Ester Hydrolase from Human Pancreatic Juice, Biochim. Biophys. Acta., 611, (1980), 136 - 146.PubMedCrossRefGoogle Scholar
  2. 2.
    D. Lombardo and O. Guy, Studies on the Substrate Specificity of a Carboxyl Ester Hydrolase from Human Pancreatic Juice. II. Action on Cholesterol Esters and Lipid-Soluble Vitamin Esters, Biochim. Biophys. Acta., 611, (1980), 147 - 155.PubMedCrossRefGoogle Scholar
  3. 3.
    N. Abouakil, E. Rogalska, J. Bonicel and D. Lombardo, Purification of Pancreatic Carboxylic-Ester Hydrolase by Immunoaffinity and its Application to the Human Bile-Salt-Stimulated Lipase, Biochim. Biophys. Acta. 961, (1988), 299 - 308.PubMedCrossRefGoogle Scholar
  4. 4.
    J.H. Han, C. Stratowa and W.J. Rutter, Isolation of Full-Length Putative Rat Lysophospholipase cDNA Using Improved Methods for mRNA Isolation and cDNA Cloning, Biochemistry. 26, (1987), 1617 - 1625.PubMedCrossRefGoogle Scholar
  5. 5.
    E.M. Kyger, R.C. Wiegand and L.G. Lange, Cloning of the Bovine Pancreatic Cholesterol Esterase/Lysophospholipase, Biochem. Biophys. Res. Comm. 164, (1989), 1302 - 1309.PubMedCrossRefGoogle Scholar
  6. 6.
    K. Reue, J. Zambaux, H. Wong, G. Lee, T.H. Leete, M. Ronk, J.E. Shively, B. Sternby, B. Borgstrom, D. Ameis, and M.C. Schotz, cDNA Cloning of Carboxyl Ester Lipase from Human Pancreas Reveals a Unique Proline-Rich Repeat Unit, J. Lipid Res. 32, (1991), 267 - 276.PubMedGoogle Scholar
  7. 7.
    P.W. Jacobson, P.W.Wiesenfeld, and L.L. Gallo, Sodium Cholate-Induced Changes in the Conformation and Activity of Rat Pancreatic Cholesterol Esterase, J. Biol. Chem. 265, (1990), 515 - 521.PubMedGoogle Scholar
  8. 8.
    O. Guy, D. Lombardo, and J.G. Brahms, Structure and Conformation of Human Pancreatic Carboxyl-Ester Hydrolase, Eur. J. Biochem. 117, (1981), 457 - 460.PubMedCrossRefGoogle Scholar
  9. 9.
    N. Abouakil, E. Mas, N. Bruneau, A. Benajiba, and D. Lombardo, Bile-Salt Dependent Lipase Biosynthesis in Rat Pancreatic AR 4-2 J Cells: Essential requirement of N-linked oligosaccharide for secretion and expression of a fully active enzyme. J. Biol. Chem. in pressGoogle Scholar
  10. 10.
    T. Baba, D. Downs, K.W. Jackson, J.Tang, and C. Wang, Structure of Human Milk Bile Salt Activated Lipase, Biochemistry. 30, (1990), 500 - 510.CrossRefGoogle Scholar
  11. 11.
    M.J. Escribano and S. Imperial, Purification and Molecular Characterization of FAP a Feto-acinar Protein Associated with the Differentiation of Human Pancreas, J. Biol. Chem. 264, (1989), 21865 - 21871.PubMedGoogle Scholar
  12. 12.
    E. Mas, N. Abouakil, S. Roudani, F. Miralles, O. Guy-Crotte, C. Figarella, M.J. Escribano, and D. Lombardo, Human Fetoacinar Pancreatic Protein: an Oncofetal Glycoform of the Normally Secreted Pancreatic Bile-salt Dependent Lipase. Biochem J. 289, (1993), 609 - 615.PubMedGoogle Scholar
  13. 13.
    T. Sugo, E. Mas, N.Abouakil, T. Endo, M.J. Escribano, A. Kobata, and D. Lombardo, The Structure of N-linked Oligosaccharides of Human Pancreatic Bile-salt Dependent Lipase. Eur. J. Biochem. in pressGoogle Scholar
  14. 14.
    E. Mas, N.Abouakil, S. Roudani, J-L. Franc, J. Montreuil and D. Lombardo, Variation of the Glycosylation of Human Pancreatic Bile-salt Dependent Lipase. Eur. J. Biochem. in pressGoogle Scholar
  15. 15.
    T.W.Rademacher, R.B. Parekh, and R.A. Dwek, Glycobiology. Ann. Rev. Biochem. 57, (1988), 785 - 836.CrossRefGoogle Scholar
  16. 16.
    R. Kornfeld and S. Kornfeld, Assembly of Asparagine-linked Oligosaccharides. Ann. Rev. Biochem. 54, (1985), 631 - 664.PubMedCrossRefGoogle Scholar
  17. 17.
    D. Lombardo, G. Montalto, S. Roudani, E. Mas, R. Laugier, V. Sbarra, and N. Abouakil, Is Bile Salt-dependent Lipase Concentration in Serum of any Help in Pancreatic Cancer Diagnosis. Pancreas. 8, (1993), 581 - 588.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Eric Mas
    • 1
  • Dominique Lombardo
    • 1
  1. 1.Faculté de MédecineINSERM U260Marseille Cedex 5France

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