Human bile salt-dependent lipase efficiency on medium-chain acyl-containing substrates: Control by sodium taurocholate

Journal of Biochemistry

Volumn 149, Issue 2, 2011, Pages 145-151

  Fontbonne, Hervé ^a   Brisson, Lydie ^a   Vérine, Alain ^b   Puigserver, Antoine ^a   Lombardo, Dominique ^b   Ajandouz, El Hassan ^a  

^a AIX MARSEILLE UNIVERSITÉ   (France)

^b University of the Mediterranean Aix Marseille II   (France)

Author keywords

bile salt activation; human milk BSDL; kinetic constants; purification and characterization; substrate chain length

Indexed keywords

4 NITROPHENYLACETIC ACID; 4 NITROPHENYLBUTYRATE; 4 NITROPHENYLCAPRYLATE; 4 NITROPHENYLLAURATE; 4 NITROPHENYLPALMITATE; BILE SALT; CARBON; PHOSPHONIC ACID ESTER; TAUROCHOLIC ACID; UNCLASSIFIED DRUG;

ARTICLE; BREAST MILK; CATALYSIS; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; HUMAN; HYDROLYSIS;

BILE ACIDS AND SALTS; CATALYSIS; ENZYME ACTIVATION; ESTERS; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MICELLES; MILK, HUMAN; NITROPHENOLS; STEROL ESTERASE; SUBSTRATE SPECIFICITY; TAUROCHOLIC ACID;

EID: 79251507610     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvq132     Document Type: Article

References (29)

1. Blackberg, L., Lombardo, D., Hernell, O., Guy, O., and Olivecrona, T. (1981) Bile salt-stimulated lipase in human milk and carboxyl ester hydrolase in pancreatic juice: are they identical enzymes? FEBS Lett. 136, 284-288
2. Alemi, B., Hamosh, M., Scanlon, J. W., Salzman-Mann, C., and Hamosh, P. (1981) Fat digestion in very low-birth-weight infants: effect of addition of human milk to low-birth-weight formula. Pediatrics 68, 484-489
3. Li, X., Lindquist, S., Lowe, M., Noppa, L., and Hernell, O. (2007) Bile salt-stimulated lipase and pancreatic lipase-related protein 2 are the dominating lipases in neonatal fat digestion in mice and rats. Pediatric Res. 62, 537-541
4. Lombardo, D., Fauvel, J., and Guy, O. (1980) Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. I. Action on carboxyl esters, glycerides and phospholipids. Biochim. Biophys. Acta 611, 136-146
5. Lombardo, D. and Guy, O. (1980) 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, 147-155
6. Wang, C. S. and Lee, D. M. (1985) Kinetic properties of human milk bile salt-activated lipase: studies using long chain triacylglycerol as substrate. J. Lipid Res. 26, 824-830
7. Chen, Q., Sternby, B., Akesson, B., and Nilsson, A. (1990) Effects of human pancreatic lipase-colipase and carboxyl ester lipase on eicosapentaenoic and arachidonic acid ester bonds of triacylglycerols rich in fish oil fatty acids. Biochim. Biophys. Acta 1044, 111-117
8. Wang, C. S. (1991) Acyl-chain specificity of human milk bile-salt-activated lipase. Biochem. J. 279, 297-302
9. Howles, P. N., Carter, C. P., and Hui, D. Y. (1996) Dietary free and esterified cholesterol absorption in cholesterol esterase (bile salt-stimulated lipase) gene-targeted mice. J. Biol. Chem. 271, 7196-7202
10. Wang, X., Wang, C. S., Tang, J., Dyda, F., and Zhang, X. C. (1997) The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism. Structure 5, 1209-1118
11. Blackberg, L. and Hernell, O. (1993) Bile salt-stimulated lipase in human milk. Evidence that bile salt induces lipid binding and activation via binding to different sites. FEBS Lett. 323, 207-210
12. Aubert, E., Sbarra, V., Le Petit-Thevenin, J., Valette, A., and Lombardo, D. (2002) Site-directed mutagenesis of the basic N-terminal cluster of pancreatic bile salt-dependent lipase. Functional significance. J. Biol. Chem. 277, 34987-34996
13. Aubert-Jousset, E., Sbarra, V., and Lombardo, D. (2004) Site-directed mutagenesis of the distal basic cluster of pancreatic bile salt-dependent lipase. J. Biol. Chem. 279, 39697-39704
14. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
15. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
16. Robertson, E. F., Dannelly, H. K., Malloy, P. J., and Reeves, H. C. (1987) Rapid isoelectric focusing in a vertical polyacrylamide minigel system. Anal. Biochem. 167, 290-294
17. Panicot-Dubois, L., Aubert, M., Franceschi, C., Mas, E., Silvy, F., Crotte, C., Bernard, J-P., Lombardo, D., and Sadoulet, M.-O. (2004) Monoclonal antibody 16D10 to the C-terminal domain of the feto-acinar pancreatic protein binds to membrane of human pancreatic tumoral SOJ-6 cells and inhibits the growth of tumor xenografts. Neoplasia 6, 713-724
18. Brisson, L., Castan, S., Fontbonne, H., Nicoletti, C., Puigserver, A., and Ajandouz, E. H. (2008) Alphatocopheryl acetate is absorbed and hydrolyzed by Caco-2 cells: Comparative studies with alpha-tocopherol. Chem. Phys. Lip. 154, 33-37
19. Blackberg, L. and Hernell, O. (1981) The bile-saltstimulated lipase in human milk. Purification and characterization. Eur. J. Biochem. 116, 221-225
20. Raeder, H., Johansson, S., Holm, P. I., Haldorsen, I. S., Mas, E., Sbarra, V., Nermoen, I., Eide, S. A., Grevle, L., Bjørkhaug, L., Sagen, J. V., Aksnes, L., Søvik, O., Lombardo, D., Molven, A., and Njølstad, P. R. (2006) Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic exocrine dysfunction. Nat. Genet. 38, 54-62
21. Labow, R. S., Adams, K. A., and Lynn, K. R. (1983) Porcine cholesterol esterase, a multiform enzyme. Biochim. Biophys. Acta 749, 32-41
22. Wang, C. S., Hartsuck, J. A., and Downs, D. (1988) Kinetics of acylglycerol sequential hydrolysis by human milk bile salt activated lipase and effect of taurocholate as fatty acid acceptor. Biochemistry 27, 4834-4840
23. Abouakil, N., Mas, E., Bruneau, N., Benajiba, A., and Lombardo, D. (1988) Purification of pancreatic carboxylic-ester hydrolase by immunoaffinity and its application to the human bile-salt-stimulated lipase. Biochim. Biophys. Acta 961, 299-308
24. Tanaka, H., Mierau, I., and Ito, F. (1999) Purification and characterization of bovine pancreatic bile salt-activated lipase. J. Biochem. 125, 883-890
25. Momsen, W. E. and Brockman, H. L. (1977) Purification and characterization of cholesterol esterase from porcine pancreas. Biochim. Biophys. Acta 486, 103-113
26. Rudd, E. A., Mizuno, N. K., and Brockman, H. L. (1987) Isolation of two forms of carboxylester lipase (cholesterol esterase) from porcine pancreas. Biochim. Biophys. Acta 918, 106-114
27. Ajandouz, E. H. and Marchis-Mouren, G. J. (1995) Subsite mapping of porcine pancreatic alpha-amylase I and II using 4-nitrophenyl-alpha- maltooligosaccharides. Carbohydr. Res. 268, 267-277
28. Terzyan, S., Wang, C. S., Downs, D., Hunter, B., and Zhang, X. C. (2000) Crystal structure of the catalytic domain of human bile salt activated lipase. Protein Sci. 9, 1783-1790
29. Negre-Salvayre, A., Abouakil, N., Lombardo, D., and Salvayre, R. (1990) Hydrolysis of fluorescent pyrene-acyl esters by human pancreatic carboxylic ester hydrolase and bile salt-stimulated lipase. Lipids 25, 428-434