Jump to content
 







Main menu
   


Navigation  



Main page
Contents
Current events
Random article
About Wikipedia
Contact us
Donate
 




Contribute  



Help
Learn to edit
Community portal
Recent changes
Upload file
 








Search  

































Create account

Log in
 









Create account
 Log in
 




Pages for logged out editors learn more  



Contributions
Talk
 



















Contents

   



(Top)
 


1 Enzymatic activity  





2 References  





3 Further reading  





4 External links  














Bile salt-dependent lipase






Cymraeg
Deutsch
Русский
Türkçe
Українська
 

Edit links
 









Article
Talk
 

















Read
Edit
View history
 








Tools
   


Actions  



Read
Edit
View history
 




General  



What links here
Related changes
Upload file
Special pages
Permanent link
Page information
Cite this page
Get shortened URL
Download QR code
Wikidata item
 




Print/export  



Download as PDF
Printable version
 
















Appearance
   

 






From Wikipedia, the free encyclopedia
 

(Redirected from Bile salt dependent lipase)

CEL
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCEL, BAL, BSDL, BSSL, CELL, CEase, FAP, FAPP, LIPA, MODY8, Bile salt-dependent lipase, carboxyl ester lipase
External IDsOMIM: 114840; MGI: 88374; HomoloGene: 37529; GeneCards: CEL; OMA:CEL - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001807

NM_009885

RefSeq (protein)

NP_001798

NP_034015

Location (UCSC)Chr 9: 133.06 – 133.07 MbChr 2: 28.45 – 28.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Bile salt-dependent lipase (orBSDL), also known as carboxyl ester lipase (orCEL) is an enzyme produced by the adult pancreas and aids in the digestion of fats. Bile salt-stimulated lipase (orBSSL) 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]

Enzymatic activity

[edit]

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]

Both BSDL and BSSL have a broad substrate specificity and, like CDL, are capable of hydrolyzing triacylglycerides (in addition to phospholipids, estersofcholesterol, 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]
  • ^ "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, 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 reading

    [edit]
    • 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. 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, 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.
  • [edit]
    Retrieved from "https://en.wikipedia.org/w/index.php?title=Bile_salt-dependent_lipase&oldid=1216669084"

    Categories: 
    Genes on human chromosome 9
    Milk
    Enzymes
    Hidden categories: 
    Articles with short description
    Short description matches Wikidata
     



    This page was last edited on 1 April 2024, at 10:04 (UTC).

    Text is available under the Creative Commons Attribution-ShareAlike License 4.0; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization.



    Privacy policy

    About Wikipedia

    Disclaimers

    Contact Wikipedia

    Code of Conduct

    Developers

    Statistics

    Cookie statement

    Mobile view



    Wikimedia Foundation
    Powered by MediaWiki