Bile salt-dependent lipase (or BSDL), also known as carboxyl ester lipase (or CEL) is an enzyme produced by the adult pancreas and aids in the digestion of fats. Bile salt-stimulated lipase (or BSSL) is an equivalent enzyme found within breast milk. BSDL has been found in the pancreatic secretions of all species in which it has been looked for. BSSL, originally discovered in the milk of humans and various other primates, has since been found in the milk of many animals including dogs, cats, rats, and rabbits.[5]
More than 95% of the fat present in human milk and in infant formulas is in the form of triacylglycerols (TG).[6] In adults, TGs are thought to be broken down or hydrolyzed mainly by the colipase-dependent lipase (CDL) enzyme. In the newborn, CDL activity in the duodenum is lower than in adults.[6]
However, newborn infants absorb lipids relatively well, considering the low level of CDL and BSDL they produce. This observation has led to the suggestion that BSDL produced by lactating mammary gland and present within milk, may compensate for the low levels of other TG-digesting enzymes and aid newborns in lipid absorption. The importance of BSSL in breast milk for the preterm infant nutrition was suggested at 2007.[9] It was also directly shown recently.[10]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000170835 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000026818 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Swan JS, Hoffman MM, et al. (1992). "Two forms of human milk bile-salt-stimulated lipase". Biochem. J. 283 (1): 119–122. doi:10.1042/bj2830119. PMC1131002. PMID 1567358.
^ abLombardo, D. (2001). "Bile salt-dependent lipase: its pathophysiological implications". Biochimica et Biophysica Acta. 1533 (1): 1–28. doi:10.1016/S1388-1981(01)00130-5. PMID 11514232.
^*Murasugi A, Asami Y, Mera-Kikuchi Y (2001). "Production of recombinant human bile-salt-stimulated lipase in Pichia pastoris". Protein Expression and Purification. 23 (2): 282–288. doi:10.1006/prep.2001.1509. PMID 11676603.
^Sbarra V, Bruneau N, et al. (1998). "Molecular cloning of the bile salt-dependent lipase of ferret lactating mammary gland: an overview of functional residues". Biochimica et Biophysica Acta. 1393 (1): 80–89. doi:10.1016/S0005-2760(98)00067-8. PMID 9714751.
^Andersson Y, Sävman K, et al. (2007). "Pasteurization of mother's own milk reduces fat absorption and growth in preterm infants". Acta Paediatrica. 96 (10): 1445–1449. doi:10.1111/j.1651-2227.2007.00450.x. PMID 17714541. S2CID 995002.
^Maggio, L.; Bellagamba, M.; et al. "A prospective, randomized, double-blind crossover study comparing rhBSSL (recombinant human Bile Salt Stimulated Lipase) and placebo added to infant formula during one week of treatment in preterm infants born before 32 weeks of gestational age: preliminary results" (PDF). Swedish Orphan Biovitrum.
Further readingedit
Kumar BV, Aleman-Gomez JA, Colwell N, et al. (1992). "Structure of the human pancreatic cholesterol esterase gene". Biochemistry. 31 (26): 6077–81. doi:10.1021/bi00141a017. PMID 1627550.
Lidberg U, Nilsson J, Strömberg K, et al. (1992). "Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene". Genomics. 13 (3): 630–40. doi:10.1016/0888-7543(92)90134-E. PMID 1639390.
Taylor AK, Zambaux JL, Klisak I, et al. (1991). "Carboxyl ester lipase: a highly polymorphic locus on human chromosome 9qter". Genomics. 10 (2): 425–31. doi:10.1016/0888-7543(91)90328-C. PMID 1676983.
Nilsson J, Bläckberg L, Carlsson P, et al. (1990). "cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase". Eur. J. Biochem. 192 (2): 543–50. doi:10.1111/j.1432-1033.1990.tb19259.x. PMID 1698625.
Lindström MB, Persson J, Thurn L, Borgström B (1991). "Effect of pancreatic phospholipase A2 and gastric lipase on the action of pancreatic carboxyl ester lipase against lipid substrates in vitro". Biochim. Biophys. Acta. 1084 (2): 194–7. doi:10.1016/0005-2760(91)90220-C. PMID 1854805.
Baba T, Downs D, Jackson KW, et al. (1991). "Structure of human milk bile salt activated lipase". Biochemistry. 30 (2): 500–10. doi:10.1021/bi00216a028. PMID 1988041.
Christie DL, Cleverly DR, O'Connor CJ (1991). "Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases". FEBS Lett. 278 (2): 190–4. doi:10.1016/0014-5793(91)80114-I. PMID 1991511. S2CID 28123400.
Reue K, Zambaux J, Wong H, et al. (1991). "cDNA cloning of carboxyl ester lipase from human pancreas reveals a unique proline-rich repeat unit". J. Lipid Res. 32 (2): 267–76. doi:10.1016/S0022-2275(20)42088-7. PMID 2066663.
Hui DY, Kissel JA (1991). "Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase". FEBS Lett. 276 (1–2): 131–4. doi:10.1016/0014-5793(90)80525-N. PMID 2265692. S2CID 10716446.
Escribano MJ, Imperial S (1990). "Purification and molecular characterization of FAP, a feto-acinar protein associated with the differentiation of human pancreas". J. Biol. Chem. 264 (36): 21865–71. doi:10.1016/S0021-9258(20)88264-7. PMID 2600091.
Erlanson-Albertsson C, Sternby B, Johannesson U (1985). "The interaction between human pancreatic carboxylester hydrolase (bile-salt-stimulated lipase of human milk) and lactoferrin". Biochim. Biophys. Acta. 829 (2): 282–7. doi:10.1016/0167-4838(85)90199-2. PMID 3995055.
Chekhranova MK, Il'ina EN, Shuvalova ER, et al. (1994). "[Cloning, determination of primary structure, and expression of the C-terminal segment of human cholesterol-esterase/lipase, containing the antigenic determinant of the protein, in Escherichia coli]". Mol. Biol. (Mosk.). 28 (2): 464–7. PMID 7514266.
Roudani S, Miralles F, Margotat A, et al. (1995). "Bile salt-dependent lipase transcripts in human fetal tissues". Biochim. Biophys. Acta. 1264 (1): 141–50. doi:10.1016/0167-4781(95)00141-3. PMID 7578248.
Bruneau N, de la Porte PL, Sbarra V, Lombardo D (1995). "Association of bile-salt-dependent lipase with membranes of human pancreatic microsomes". Eur. J. Biochem. 233 (1): 209–18. doi:10.1111/j.1432-1033.1995.209_1.x. PMID 7588748.
Wang CS, Dashti A, Jackson KW, et al. (1995). "Isolation and characterization of human milk bile salt-activated lipase C-tail fragment". Biochemistry. 34 (33): 10639–44. doi:10.1021/bi00033a039. PMID 7654718.
Nilsson J, Hellquist M, Bjursell G (1993). "The human carboxyl ester lipase-like (CELL) gene is ubiquitously expressed and contains a hypervariable region". Genomics. 17 (2): 416–22. doi:10.1006/geno.1993.1341. PMID 7691717.
Bruneau N, Lombardo D (1995). "Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase". J. Biol. Chem. 270 (22): 13524–33. doi:10.1074/jbc.270.22.13524. PMID 7768954.
Mas E, Abouakil N, Roudani S, et al. (1993). "Human fetoacinar pancreatic protein: an oncofetal glycoform of the normally secreted pancreatic bile-salt-dependent lipase". Biochem. J. 289 (2): 609–15. doi:10.1042/bj2890609. PMC1132213. PMID 8424803.
Shamir R, Johnson WJ, Morlock-Fitzpatrick K, et al. (1996). "Pancreatic carboxyl ester lipase: a circulating enzyme that modifies normal and oxidized lipoproteins in vitro". J. Clin. Invest. 97 (7): 1696–704. doi:10.1172/JCI118596. PMC507234. PMID 8601635.
Landberg E, Påhlsson P, Krotkiewski H, et al. (1997). "Glycosylation of bile-salt-stimulated lipase from human milk: comparison of native and recombinant forms". Arch. Biochem. Biophys. 344 (1): 94–102. doi:10.1006/abbi.1997.0188. PMID 9244386.
External linksedit
Human CEL genome location and CEL gene details page in the UCSC Genome Browser.
Human FAP genome location and FAP gene details page in the UCSC Genome Browser.
Human LIPA genome location and LIPA gene details page in the UCSC Genome Browser.
January 01, 1970
bile, salt, dependent, lipase, bsdl, also, known, carboxyl, ester, lipase, enzyme, produced, adult, pancreas, aids, digestion, fats, bile, salt, stimulated, lipase, bssl, equivalent, enzyme, found, within, breast, milk, bsdl, been, found, pancreatic, secretion. Bile salt dependent lipase or BSDL also known as carboxyl ester lipase or CEL is an enzyme produced by the adult pancreas and aids in the digestion of fats Bile salt stimulated lipase or BSSL is an equivalent enzyme found within breast milk BSDL has been found in the pancreatic secretions of all species in which it has been looked for BSSL originally discovered in the milk of humans and various other primates has since been found in the milk of many animals including dogs cats rats and rabbits 5 CELAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes1F6W 1JMYIdentifiersAliasesCEL BAL BSDL BSSL CELL CEase FAP FAPP LIPA MODY8 Bile salt dependent lipase carboxyl ester lipaseExternal IDsOMIM 114840 MGI 88374 HomoloGene 37529 GeneCards CELGene location Human Chr Chromosome 9 human 1 Band9q34 13Start133 061 981 bp 1 End133 071 861 bp 1 Gene location Mouse Chr Chromosome 2 mouse 2 Band2 A3 2 19 38 cMStart28 445 807 bp 2 End28 453 415 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inbody of pancreaspituitary glandanterior pituitarycorpus epididymiscaput epididymisduodenumright uterine tuberight lobe of liverkidneyright coronary arteryTop expressed inpyloric antrumislet of Langerhansepithelium of stomachduodenumsexually immature organismmucous cell of stomachtracheobronchial treeleft lobe of liverspleenlarge intestineMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionheparin binding acylglycerol lipase activity catalytic activity protein binding hydrolase activity hydrolase activity acting on ester bonds carboxylic ester hydrolase activity triglyceride lipase activity sterol esterase activity signaling receptor activity neurexin family protein bindingCellular componentcytoplasm extracellular region extracellular exosome extracellular space integral component of plasma membrane cell surface synapse presynapseBiological processfatty acid catabolic process lipid digestion protein esterification lipid metabolism cholesterol catabolic process pancreatic juice secretion intestinal lipid catabolic process lipid catabolic process intestinal cholesterol absorption triglyceride metabolic process neuron cell cell adhesion synaptic vesicle endocytosis modulation of chemical synaptic transmission postsynaptic membrane assembly presynaptic membrane assemblySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez105612613EnsemblENSG00000170835ENSMUSG00000026818UniProtP19835Q64285RefSeq mRNA NM 001807NM 009885RefSeq protein NP 001798NP 034015Location UCSC Chr 9 133 06 133 07 MbChr 2 28 45 28 45 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Enzymatic activity 2 References 3 Further reading 4 External linksEnzymatic activity editMore than 95 of the fat present in human milk and in infant formulas is in the form of triacylglycerols TG 6 In adults TGs are thought to be broken down or hydrolyzed mainly by the colipase dependent lipase CDL enzyme In the newborn CDL activity in the duodenum is lower than in adults 6 Both BSDL and BSSL have a broad substrate specificity and like CDL are capable of hydrolyzing triacylglycerides in addition to phospholipids esters of cholesterol and lipid soluble vitamins In particular they can hydrolyze esters of the essential fatty acids n 3 and n 6 PUFAs and DHA 7 BSDL production in the newborn pancreas is quite low when compared with production in the mammary gland or adult pancreas 8 However newborn infants absorb lipids relatively well considering the low level of CDL and BSDL they produce This observation has led to the suggestion that BSDL produced by lactating mammary gland and present within milk may compensate for the low levels of other TG digesting enzymes and aid newborns in lipid absorption The importance of BSSL in breast milk for the preterm infant nutrition was suggested at 2007 9 It was also directly shown recently 10 References edit a b c GRCh38 Ensembl release 89 ENSG00000170835 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000026818 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Swan JS Hoffman MM et al 1992 Two forms of human milk bile salt stimulated lipase Biochem J 283 1 119 122 doi 10 1042 bj2830119 PMC 1131002 PMID 1567358 a b Lombardo D 2001 Bile salt dependent lipase its pathophysiological implications Biochimica et Biophysica Acta 1533 1 1 28 doi 10 1016 S1388 1981 01 00130 5 PMID 11514232 Murasugi A Asami Y Mera Kikuchi Y 2001 Production of recombinant human bile salt stimulated lipase in Pichia pastoris Protein Expression and Purification 23 2 282 288 doi 10 1006 prep 2001 1509 PMID 11676603 Sbarra V Bruneau N et al 1998 Molecular cloning of the bile salt dependent lipase of ferret lactating mammary gland an overview of functional residues Biochimica et Biophysica Acta 1393 1 80 89 doi 10 1016 S0005 2760 98 00067 8 PMID 9714751 Andersson Y Savman K et al 2007 Pasteurization of mother s own milk reduces fat absorption and growth in preterm infants Acta Paediatrica 96 10 1445 1449 doi 10 1111 j 1651 2227 2007 00450 x PMID 17714541 S2CID 995002 Maggio L Bellagamba M et al A prospective randomized double blind crossover study comparing rhBSSL recombinant human Bile Salt Stimulated Lipase and placebo added to infant formula during one week of treatment in preterm infants born before 32 weeks of gestational age preliminary results PDF Swedish Orphan Biovitrum Further reading editKumar BV Aleman Gomez JA Colwell N et al 1992 Structure of the human pancreatic cholesterol esterase gene Biochemistry 31 26 6077 81 doi 10 1021 bi00141a017 PMID 1627550 Lidberg U Nilsson J Stromberg K et al 1992 Genomic organization sequence analysis and chromosomal localization of the human carboxyl ester lipase CEL gene and a CEL like CELL gene Genomics 13 3 630 40 doi 10 1016 0888 7543 92 90134 E PMID 1639390 Taylor AK Zambaux JL Klisak I et al 1991 Carboxyl ester lipase a highly polymorphic locus on human chromosome 9qter Genomics 10 2 425 31 doi 10 1016 0888 7543 91 90328 C PMID 1676983 Nilsson J Blackberg L Carlsson P et al 1990 cDNA cloning of human milk bile salt stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase Eur J Biochem 192 2 543 50 doi 10 1111 j 1432 1033 1990 tb19259 x PMID 1698625 Lindstrom MB Persson J Thurn L Borgstrom B 1991 Effect of pancreatic phospholipase A2 and gastric lipase on the action of pancreatic carboxyl ester lipase against lipid substrates in vitro Biochim Biophys Acta 1084 2 194 7 doi 10 1016 0005 2760 91 90220 C PMID 1854805 Baba T Downs D Jackson KW et al 1991 Structure of human milk bile salt activated lipase Biochemistry 30 2 500 10 doi 10 1021 bi00216a028 PMID 1988041 Christie DL Cleverly DR O Connor CJ 1991 Human milk bile salt stimulated lipase Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases FEBS Lett 278 2 190 4 doi 10 1016 0014 5793 91 80114 I PMID 1991511 S2CID 28123400 Reue K Zambaux J Wong H et al 1991 cDNA cloning of carboxyl ester lipase from human pancreas reveals a unique proline rich repeat unit J Lipid Res 32 2 267 76 doi 10 1016 S0022 2275 20 42088 7 PMID 2066663 Hui DY Kissel JA 1991 Sequence identity between human pancreatic cholesterol esterase and bile salt stimulated milk lipase FEBS Lett 276 1 2 131 4 doi 10 1016 0014 5793 90 80525 N PMID 2265692 S2CID 10716446 Escribano MJ Imperial S 1990 Purification and molecular characterization of FAP a feto acinar protein associated with the differentiation of human pancreas J Biol Chem 264 36 21865 71 doi 10 1016 S0021 9258 20 88264 7 PMID 2600091 Erlanson Albertsson C Sternby B Johannesson U 1985 The interaction between human pancreatic carboxylester hydrolase bile salt stimulated lipase of human milk and lactoferrin Biochim Biophys Acta 829 2 282 7 doi 10 1016 0167 4838 85 90199 2 PMID 3995055 Chekhranova MK Il ina EN Shuvalova ER et al 1994 Cloning determination of primary structure and expression of the C terminal segment of human cholesterol esterase lipase containing the antigenic determinant of the protein in Escherichia coli Mol Biol Mosk 28 2 464 7 PMID 7514266 Roudani S Miralles F Margotat A et al 1995 Bile salt dependent lipase transcripts in human fetal tissues Biochim Biophys Acta 1264 1 141 50 doi 10 1016 0167 4781 95 00141 3 PMID 7578248 Bruneau N de la Porte PL Sbarra V Lombardo D 1995 Association of bile salt dependent lipase with membranes of human pancreatic microsomes Eur J Biochem 233 1 209 18 doi 10 1111 j 1432 1033 1995 209 1 x PMID 7588748 Wang CS Dashti A Jackson KW et al 1995 Isolation and characterization of human milk bile salt activated lipase C tail fragment Biochemistry 34 33 10639 44 doi 10 1021 bi00033a039 PMID 7654718 Nilsson J Hellquist M Bjursell G 1993 The human carboxyl ester lipase like CELL gene is ubiquitously expressed and contains a hypervariable region Genomics 17 2 416 22 doi 10 1006 geno 1993 1341 PMID 7691717 Bruneau N Lombardo D 1995 Chaperone function of a Grp 94 related protein for folding and transport of the pancreatic bile salt dependent lipase J Biol Chem 270 22 13524 33 doi 10 1074 jbc 270 22 13524 PMID 7768954 Mas E Abouakil N Roudani S et al 1993 Human fetoacinar pancreatic protein an oncofetal glycoform of the normally secreted pancreatic bile salt dependent lipase Biochem J 289 2 609 15 doi 10 1042 bj2890609 PMC 1132213 PMID 8424803 Shamir R Johnson WJ Morlock Fitzpatrick K et al 1996 Pancreatic carboxyl ester lipase a circulating enzyme that modifies normal and oxidized lipoproteins in vitro J Clin Invest 97 7 1696 704 doi 10 1172 JCI118596 PMC 507234 PMID 8601635 Landberg E Pahlsson P Krotkiewski H et al 1997 Glycosylation of bile salt stimulated lipase from human milk comparison of native and recombinant forms Arch Biochem Biophys 344 1 94 102 doi 10 1006 abbi 1997 0188 PMID 9244386 External links editHuman CEL genome location and CEL gene details page in the UCSC Genome Browser Human FAP genome location and FAP gene details page in the UCSC Genome Browser Human LIPA genome location and LIPA gene details page in the UCSC Genome Browser Retrieved from https en wikipedia org w index php title Bile salt dependent lipase amp oldid 1216669084, wikipedia, wiki, book, books, library,
