Bile salt-dependent lipase

Carboxyl ester lipase (bile salt-stimulated lipase)

PDB rendering based on 1f6w.
Identifiers
Symbols CEL; BAL; BSDL; BSSL; CELL; CEase; FAP; FAPP; LIPA; MODY8
External IDs OMIM: 114840 MGI: 88374 HomoloGene: 37529 GeneCards: CEL Gene
EC number 3.1.1.3
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 1056 12613
Ensembl ENSG00000170835 ENSMUSG00000026818
UniProt P19835 Q3V2H7
RefSeq (mRNA) NM_001807.3 NM_009885.1
RefSeq (protein) NP_001798.2 NP_034015.1
Location (UCSC) Chr 9:
135.94 – 135.95 Mb		 Chr 2:
28.41 – 28.42 Mb
PubMed search [1] [2]

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.[1]

Enzymatic activity

More than 95% of the fat present in human milk and in infant formulas is in the form of triacylglycerols (TG).[2] In adults, TGs are thought to be broken down or hydrolyzed mainly by the colipase-dependent lipase enzyme. In the newborn, CDL activity in the duodenum is lower than in adults.[2]

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). BSDL production in the newborn pancreas is quite low when compared with production in the mammary gland or adult pancreas.[3]

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.

References

  1. ^ Swan, JS, Hoffman MM. et al. (1992). "Two forms of human milk bile-salt-stimulated lipase". Biochem. J. 283 (1): 119–122. PMID 1567358. 
  2. ^ a b Lombardo, D. (2001). "Bile salt-dependent lipase: its pathophysiological implications". Biochim. Biophys. Acta. 1533 (1): 1–28. PMID 11514232. 
  3. ^ 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". Biochim. Biophys. Acta. 1393 (1): 80–89. PMID 9714751. 

Further reading

  • 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. 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. 
  • 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. 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. 
  • 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. 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. 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. 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 ( Pt 2): 609–15. 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. 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. 
  • Murasugi A, Asami Y, Mera-Kikuchi Y (2001). "Production of recombinant human bile-salt-stimulated lipase in Pichia pastoris.". Protein Expr. Purif. 23 (2): 282–288. doi:10.1006/prep.2001.1509. PMID 11676603. 
3.1.1: Carboxylic ester hydrolases
3.1.2: Thioesterase
3.1.3: Phosphatase
3.1.4: Phosphodiesterase
3.1.6: Sulfatase
Nuclease (includes
deoxyribonuclease and
ribonuclease)
either deoxy- or ribo-
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6