Biology:Pancreatic lipase family

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Short description: Protein family found in humans
Complex of human pancreatic lipase with colipase
Identifiers
SymbolLipase
PfamPF00151
InterProIPR013818
PROSITEPDOC00110
SCOP21lpa / SCOPe / SUPFAM
OPM superfamily127
OPM protein1lpa

The Pancreatic lipase family is a family of proteins which includes pancreatic lipase (PNLIP) and a number of similar lipases.[1] Lipases are enzymes that break the ester bonds linking fatty acids to fat molecules, especially triglycerides.[2] In humans and other animals, the lipases in this family fill a wide range of roles from digesting dietary fat to regulating lipid levels in blood.[1]

The pancreatic lipase family is one of the best understood lipase families.[1] It contains the traditional lipases (EC 3.1.1.3): pancreatic lipase (PNLIP), hepatic lipase (LIPC), endothelial lipase (LIPG), and PNLIPRP2, but also some non-traditional lipases like lipoprotein lipase (LPL, EC 3.1.1.34) and even the phospholipase: phosphatidylserine phospholipase A1 (PLA1A, EC 3.1.1.111).[1] It also contains some related proteins like PNLIPRP1[1] which seem to have lost their ability to function as enzymes in humans.[3][4]

This family is part of the larger α/β hydrolase superfamily of proteins, and so its members possess α/β hydrolase domains. For example, Pancreatic lipase contains two protein domains. The one toward the N terminus is the α/β hydrolase, whereas the one toward the C terminus plays a role in binding to colipase, a protein needed in order for the lipase to become activated.[5] The related lipases gastric lipase/lingual lipase (LIPF), lysosomal lipase (LIPA), and carboxyl ester lipase (CEL) are part of the larger α/β hydrolase superfamily but not considered part of the pancreatic lipase family.[1]

The most conserved region in all these proteins is centred on a serine residue which has been shown[6] to participate, with a histidine and an aspartic acid residue, in a charge relay system. Such a region is also present in lipases of prokaryotic origin and in lecithin-cholesterol acyltransferase (EC 2.3.1.43) (LCAT),[7] which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol.

In humans

Family members

  • Pancreatic lipase (PNLIP): the namesake member, which is also known as pancreatic triacylglycerol lipase or steapsin. This pancreas enzyme is one of the primary digestive enzymes involved in breaking down dietary fats.[8][9]
  • Hepatic lipase (LIPC)
  • Endothelial lipase (LIPG)
  • Lipase member H (LIPH)
  • Lipase member I (LIPI)
  • Lipoprotein lipase (LPL)
  • Phospholipase A1 member A (PLA1A)
  • Pancreatic lipase related protein 1 (PNLIPRP1)
  • Pancreatic lipase related protein 2 (PNLIPRP2)
  • Pancreatic lipase related protein 3 (PNLIPRP3)

Diagnostic importance

Pancreatic lipase is secreted into the duodenum through the duct system of the pancreas. Its concentration in serum is normally very low. Under extreme disruption of pancreatic function, such as pancreatitis or pancreatic adenocarcinoma, the pancreas may begin to autolyse and release pancreatic enzymes including pancreatic lipase into serum. Thus, through measurement of serum concentration of pancreatic lipase, acute pancreatitis can be diagnosed.[10]

Inhibitors

Lipase inhibitors such as orlistat can be used as a treatment for obesity.[11]

One peptide selected by phage display was found to inhibit pancreatic lipase.[12]

See also

  • Orlistat (a pancreatic lipase inhibitor marketed as an anti-obesity medication)

References

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 "Lipases: it's not just pancreatic lipase!". American journal of veterinary research 83 (8). 2022-08-01. doi:10.2460/ajvr.22.03.0048. 
  2. ↑ "Minireview on pancreatic lipase and colipase". Biochimie 70 (9): 1223–1234. 1988. doi:10.1016/0300-9084(88)90188-5. PMID 3147715. 
  3. ↑ "P54315 · LIPR1_HUMAN". UniProt consortium. https://www.uniprot.org/uniprotkb/P54315/entry. 
  4. ↑ "Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase". Eur. J. Biochem. 179 (1): 39–45. 1989. doi:10.1111/j.1432-1033.1989.tb14518.x. PMID 2917565. 
  5. ↑ "The C-terminal domain of pancreatic lipase: functional and structural analogies with c2 domains". Curr. Protein Pept. Sci. 1 (1): 91–103. 2000. doi:10.2174/1389203003381487. PMID 12369922. 
  6. ↑ Blow D (1990). "Enzymology. More of the catalytic triad". Nature 343 (6260): 694–695. doi:10.1038/343694a0. PMID 2304545. Bibcode: 1990Natur.343..694B. 
  7. ↑ "Cloning and expression of human lecithin-cholesterol acyltransferase cDNA". Proc. Natl. Acad. Sci. U.S.A. 83 (8): 2335–2339. 1986. doi:10.1073/pnas.83.8.2335. PMID 3458198. Bibcode: 1986PNAS...83.2335M. 
  8. ↑ "Entrez Gene: pancreatic lipase". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=5406. 
  9. ↑ "Assignment of human pancreatic lipase gene (PNLIP) to chromosome 10q24-q26". Genomics 11 (4): 1164–6. December 1991. doi:10.1016/0888-7543(91)90048-J. PMID 1783385. 
  10. ↑ "Serum levels of pancreatic enzymes and their clinical significance". Clin Gastroenterol 13 (3): 739–61. September 1984. doi:10.1016/S0300-5089(21)00756-2. PMID 6207965. 
  11. ↑ "US orlistat label". FDA. August 2015. https://www.accessdata.fda.gov/drugsatfda_docs/label/2015/020766s035lbl.pdf.  For label updates see FDA index page for NDA 020766
  12. ↑ Lunder, M.; Bratkovič, T.; Kreft, S.; Štrukelj, B. (2005). "Peptide inhibitor of pancreatic lipase selected by phage display using different elution strategies". Journal of Lipid Research 46 (7): 1512–1516. doi:10.1194/jlr.M500048-JLR200. PMID 15863836. 

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR013818



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