Bile salt-dependent lipase

Last updated
CEL
PBB Protein CEL image.jpg
Available structures
PDB Ortholog search: PDBe RCSB
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
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 Mb Chr 2: 28.45 – 28.45 Mb
PubMed search [3] [4]
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]

Contents

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]

Related Research Articles

Very-low-density lipoprotein (VLDL), density relative to extracellular water, is a type of lipoprotein made by the liver. VLDL is one of the five major groups of lipoproteins that enable fats and cholesterol to move within the water-based solution of the bloodstream. VLDL is assembled in the liver from triglycerides, cholesterol, and apolipoproteins. VLDL is converted in the bloodstream to low-density lipoprotein (LDL) and intermediate-density lipoprotein (IDL). VLDL particles have a diameter of 30–80 nm. VLDL transports endogenous products, whereas chylomicrons transport exogenous (dietary) products. In the early 2010s both the lipid composition and protein composition of this lipoprotein were characterised in great detail.

<span class="mw-page-title-main">Digestive enzyme</span> Class of enzymes

Digestive enzymes are a group of enzymes that break down polymeric macromolecules into their smaller building blocks, in order to facilitate their absorption into the cells of the body. Digestive enzymes are found in the digestive tracts of animals and in the tracts of carnivorous plants, where they aid in the digestion of food, as well as inside cells, especially in their lysosomes, where they function to maintain cellular survival. Digestive enzymes of diverse specificities are found in the saliva secreted by the salivary glands, in the secretions of cells lining the stomach, in the pancreatic juice secreted by pancreatic exocrine cells, and in the secretions of cells lining the small and large intestines.

<span class="mw-page-title-main">Colipase</span> Mammalian protein found in Homo sapiens

Colipase, abbreviated CLPS, is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides.

<span class="mw-page-title-main">Lipid signaling</span> Biological signaling using lipid molecules

Lipid signaling, broadly defined, refers to any biological signaling event involving a lipid messenger that binds a protein target, such as a receptor, kinase or phosphatase, which in turn mediate the effects of these lipids on specific cellular responses. Lipid signaling is thought to be qualitatively different from other classical signaling paradigms because lipids can freely diffuse through membranes. One consequence of this is that lipid messengers cannot be stored in vesicles prior to release and so are often biosynthesized "on demand" at their intended site of action. As such, many lipid signaling molecules cannot circulate freely in solution but, rather, exist bound to special carrier proteins in serum.

<span class="mw-page-title-main">Lecithin–cholesterol acyltransferase</span> Mammalian protein found in Homo sapiens

Lecithin–cholesterol acyltransferase is an enzyme, in many animals including humans, that converts free cholesterol into cholesteryl ester, which is then sequestered into the core of a lipoprotein particle, eventually making the newly synthesized HDL spherical and forcing the reaction to become unidirectional since the particles are removed from the surface. The enzyme is bound to high-density lipoproteins (HDLs) (alpha-LCAT) and LDLs (beta-LCAT) in the blood plasma. LCAT deficiency can cause impaired vision due to cholesterol corneal opacities, anemia, and kidney damage. It belongs to the family of phospholipid:diacylglycerol acyltransferases.

<span class="mw-page-title-main">Hormone-sensitive lipase</span> Enzyme

Hormone-sensitive lipase (EC 3.1.1.79, HSL), also previously known as cholesteryl ester hydrolase (CEH), sometimes referred to as triacylglycerol lipase, is an enzyme that, in humans, is encoded by the LIPE gene, and catalyzes the following reaction:

<span class="mw-page-title-main">Gastric lipase</span> Class of enzymes

Gastric lipase, also known as LIPF, is an enzymatic protein that, in humans, is encoded by the LIPF gene.

The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction

<span class="mw-page-title-main">PLA2G1B</span> Protein-coding gene in the species Homo sapiens

Phospholipase A2, group 1B is an enzyme that in humans is encoded by the PLA2G1B gene.

<span class="mw-page-title-main">SOAT2</span> Protein-coding gene in the species Homo sapiens

Sterol O-acyltransferase 2, also known as SOAT2, is an enzyme that in humans is encoded by the SOAT2 gene.

<span class="mw-page-title-main">GDI2</span> Protein-coding gene in the species Homo sapiens

Rab GDP dissociation inhibitor beta is a protein that in humans is encoded by the GDI2 gene.

<span class="mw-page-title-main">FABP6</span> Mammalian protein found in Homo sapiens

Fatty acid binding protein 6, ileal (gastrotropin), also known as FABP6, is a protein which in humans is encoded by the FABP6 gene.

<span class="mw-page-title-main">GP2 (gene)</span> Protein-coding gene in the species Homo sapiens

Pancreatic secretory granule membrane major glycoprotein GP2 is a protein that in humans is encoded by the GP2 gene.

<span class="mw-page-title-main">Pancreatic lipase family</span> Mammalian protein found in Homo sapiens

Triglyceride lipases are a family of lipolytic enzymes that hydrolyse ester linkages of triglycerides. Lipases are widely distributed in animals, plants and prokaryotes.

<span class="mw-page-title-main">LYPLA1</span> Protein-coding gene in the species Homo sapiens

Acyl-protein thioesterase 1 is an enzyme that in humans is encoded by the LYPLA1 gene.

<span class="mw-page-title-main">CELA3B</span> Protein-coding gene in the species Homo sapiens

Chymotrypsin-like elastase family member 3B also known as elastase-3B, protease E, or fecal elastase is an enzyme that in humans is encoded by the CELA3B gene.

<span class="mw-page-title-main">COQ2</span> Protein-coding gene in the species Homo sapiens

Para-hydroxybenzoate—polyprenyltransferase, mitochondrial is an enzyme that in humans is encoded by the COQ2 gene.

<span class="mw-page-title-main">ENPP7</span> Protein-coding gene in the species Homo sapiens

Ectonucleotide pyrophosphatase/phosphodiesterase family member 7 also known as alkaline sphingomyelin phosphodiesterase (Alk-SMase) or intestinal alkaline sphingomyelinase is an enzyme that in humans is encoded by the ENPP7 gene.

<span class="mw-page-title-main">Dehydrodolichyl diphosphate synthase</span> Protein-coding gene in the species Homo sapiens

Dehydrodolichyl diphosphate synthase is an enzyme that in humans is encoded by the DHDDS gene.

<span class="mw-page-title-main">Lipase</span> Class of enzymes

Lipase is a family of enzymes that catalyzes the hydrolysis of fats. Some lipases display broad substrate scope including esters of cholesterol, phospholipids, and of lipid-soluble vitamins and sphingomyelinases; however, these are usually treated separately from "conventional" lipases. Unlike esterases, which function in water, lipases "are activated only when adsorbed to an oil–water interface". Lipases perform essential roles in digestion, transport and processing of dietary lipids in most, if not all, organisms.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000170835 - Ensembl, May 2017
  2. 1 2 3 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.
  6. 1 2 Lombardo, D. (2001). "Bile salt-dependent lipase: its pathophysiological implications". Biochim. Biophys. 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 Expr. Purif. 23 (2): 282–288. doi:10.1006/prep.2001.1509. PMID   11676603.
  7. 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. doi: 10.1016/S0005-2760(98)00067-8 . PMID   9714751.
  8. Andersson Y, Sävman K, et al. (2007). "Pasteurization of mother's own milk reduces fat absorption and growth in preterm infants". Acta Paediatr. 96 (10): 1445–1449. doi:10.1111/j.1651-2227.2007.00450.x. PMID   17714541. S2CID   995002.
  9. 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. [ permanent dead link ]

Further reading