Bile salt-dependent lipase

CEL
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1F6W, 1JMY
Identifiers
Aliases	CEL, BAL, BSDL, BSSL, CELL, CEase, FAP, FAPP, LIPA, MODY8, Bile salt-dependent lipase, carboxyl ester lipase
External IDs	OMIM: 114840; MGI: 88374; HomoloGene: 37529; GeneCards: CEL; OMA:CEL - orthologs
Gene location (Human)
Chr.	Chromosome 9 (human)
End	133,071,861 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	28,453,415 bp
RNA expression pattern
	Top expressed in
	body of pancreas; ; beta cell; ; pituitary gland; ; anterior pituitary; ; corpus epididymis; ; caput epididymis; ; duodenum; ; right hemisphere of cerebellum; ; right uterine tube; ; paraflocculus of cerebellum;
	Top expressed in
	pyloric antrum; ; islet of Langerhans; ; lactiferous gland; ; epithelium of stomach; ; duodenum; ; sexually immature organism; ; mucous cell of stomach; ; migratory enteric neural crest cell; ; embryo; ; tracheobronchial tree;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	heparin 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 binding;
Cellular component	cytoplasm; extracellular region; extracellular exosome; extracellular space; integral component of plasma membrane; cell surface; synapse; presynapse;
Biological process	fatty 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 assembly;
	Sources:Amigo / QuickGO
Orthologs
	1056
	12613
	ENSG00000170835
	ENSMUSG00000026818
	P19835
	Q64285
	NM_001807
	NM_009885
	NP_001798
	NP_034015
	Wikidata
View/Edit Human	View/Edit Mouse

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]

Enzymatic activity

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, 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

^ ^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, 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.

External links

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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000170835 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000026818 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] 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.

[lombardo-6] 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-7] *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-8] 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.

[9] 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.

[10] 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.

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Bile salt-dependent lipase

Enzymatic activity

References

Further reading

External links

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