WordNet

an enzyme secreted in the digestive tract that catalyzes the breakdown of fats into individual fatty acids that can be absorbed into the bloodstream
of or involving the pancreas; "pancreatic cancer"

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リパーゼ(脂肪分解酵素)
膵臓の

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/03/12 10:56:38」(JST)

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Pancreatic lipase, also known as pancreatic triacylglycerol lipase, is secreted from the pancreas, and is the primary lipase (enzyme) that hydrolyzes (breaks down) dietary fat molecules in the human digestive system, converting triglyceride substrates found in ingested oils to monoglycerides and free fatty acids.

Triacylglycerol + 2 H₂O 2-monoacylglycerol + 2 fatty acid anions

Bile salts secreted from the liver and stored in gallbladder are released into the duodenum, where they coat and emulsify large fat droplets into smaller droplets, thus increasing the overall surface area of the fat, which allows the lipase to break apart the fat more effectively. The resulting monomers (2 free fatty acids and one 2-monoacylglycerol) are then moved by way of peristalsis along the small intestine to be absorbed into the lymphatic system by a specialized vessel called a lacteal. This protein belongs to pancreatic lipase family.

Unlike some pancreatic enzymes that are activated by proteolytic cleavage (e.g., trypsinogen), pancreatic lipase is secreted in its final form. However, it becomes efficient only in the presence of colipase in the duodenum.

In humans, pancreatic lipase is encoded by the PNLIP gene.^[2]^[3]

§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.^[4]

§See also

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

§References

^ PDB 1LPB; Egloff MP, Marguet F, Buono G, Verger R, Cambillau C, van Tilbeurgh H (March 1995). "The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate". Biochemistry 34 (9): 2751–62. doi:10.1021/bi00009a003. PMID 7893686.
^ Davis R, Diep A, Hunziker W, Klisak I, Mohandas T, Schotz M et al. (December 1991). "Assignment of human pancreatic lipase gene (PNLIP) to chromosome 10q24-q26". Genomics 11 (4): 1164–6. doi:10.1016/0888-7543(91)90048-J. PMID 1783385.
^ "Entrez Gene: pancreatic lipase".
^ Koop H (September 1984). "Serum levels of pancreatic enzymes and their clinical significance". Clin Gastroenterol 13 (3): 739–61. PMID 6207965.

§Further reading

Crandall W, Lowe M (2001). "Colipase residues Glu64 and Arg65 are essential for normal lipase-mediated fat digestion in the presence of bile salt micelles". J. Biol. Chem. 276 (16): 12505–12. doi:10.1074/jbc.M009986200. PMID 11278590.
Freie A, Ferrato F, Carrière F, Lowe M (2006). "Val-407 and Ile-408 in the beta5'-loop of pancreatic lipase mediate lipase-colipase interactions in the presence of bile salt micelles". J. Biol. Chem. 281 (12): 7793–800. doi:10.1074/jbc.M512984200. PMC 3695395. PMID 16431912.
Hegele R, Ramdath D, Ban M, Carruthers M, Carrington C, Cao H (2001). "Polymorphisms in PNLIP, encoding pancreatic lipase, and associations with metabolic traits". J. Hum. Genet. 46 (6): 320–4. doi:10.1007/s100380170066. PMID 11393534.
Chahinian H, Sias B, Carrière F (2000). "The C-terminal domain of pancreatic lipase: functional and structural analogies with c2 domains". Curr. Protein Pept. Sci. 1 (1): 91–103. PMID 12369922.
Ranaldi S, Belle V, Woudstra M, Rodriguez J, Guigliarelli B, Sturgis J et al. (2009). "Lid opening and unfolding in human pancreatic lipase at low pH revealed by site-directed spin labeling EPR and FTIR spectroscopy". Biochemistry 48 (3): 630–8. doi:10.1021/bi801250s. PMID 19113953.
Grupe A, Li Y, Rowland C, Nowotny P, Hinrichs A, Smemo S et al. (2006). "A scan of chromosome 10 identifies a novel locus showing strong association with late-onset Alzheimer disease". Am. J. Hum. Genet. 78 (1): 78–88. doi:10.1086/498851. PMC 1380225. PMID 16385451.
Thomas A, Allouche M, Basyn F, Brasseur R, Kerfelec B (2005). "Role of the lid hydrophobicity pattern in pancreatic lipase activity". J. Biol. Chem. 280 (48): 40074–83. doi:10.1074/jbc.M502123200. PMID 16179352.
van Tilbeurgh H, Egloff M, Martinez C, Rugani N, Verger R, Cambillau C (1993). "Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography". Nature 362 (6423): 814–20. doi:10.1038/362814a0. PMID 8479519.
Lessinger J, Arzoglou P, Ramos P, Visvikis A, Parashou S, Calam D et al. (2003). "Preparation and characterization of reference materials for human pancreatic lipase: BCR 693 (from human pancreatic juice) and BCR 694 (recombinant)". Clin. Chem. Lab. Med. 41 (2): 169–76. doi:10.1515/CCLM.2003.028. PMID 12667003.
Colin D, Deprez-Beauclair P, Allouche M, Brasseur R, Kerfelec B (2008). "Exploring the active site cavity of human pancreatic lipase". Biochem. Biophys. Res. Commun. 370 (3): 394–8. doi:10.1016/j.bbrc.2008.03.043. PMID 18353248.
Ramos P, Coste T, Piémont E, Lessinger J, Bousquet J, Chapus C et al. (2003). "Time-resolved fluorescence allows selective monitoring of Trp30 environmental changes in the seven-Trp-containing human pancreatic lipase". Biochemistry 42 (43): 12488–96. doi:10.1021/bi034900e. PMID 14580194.
Yang Y, Lowe M (1998). "Human pancreatic triglyceride lipase expressed in yeast cells: purification and characterization". Protein Expr. Purif. 13 (1): 36–40. doi:10.1006/prep.1998.0874. PMID 9631512.
Sims H, Jennens M, Lowe M (1993). "The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family". Gene 131 (2): 281–5. doi:10.1016/0378-1119(93)90307-O. PMID 8406023.
Grandval P, De Caro A, De Caro J, Sias B, Carrière F, Verger R et al. (2004). "Critical evaluation of a specific ELISA and two enzymatic assays of pancreatic lipases in human sera". Pancreatology 4 (6): 495–503; discussion 503–4. doi:10.1159/000080246. PMID 15316225.
Belle V, Fournel A, Woudstra M, Ranaldi S, Prieri F, Thomé V et al. (2007). "Probing the opening of the pancreatic lipase lid using site-directed spin labeling and EPR spectroscopy". Biochemistry 46 (8): 2205–14. doi:10.1021/bi0616089. PMID 17269661.
Lowe M (1997). "Structure and function of pancreatic lipase and colipase". Annu. Rev. Nutr. 17: 141–58. doi:10.1146/annurev.nutr.17.1.141. PMID 9240923.
Bourbon-Freie A, Dub R, Xiao X, Lowe M (2009). "Trp-107 and trp-253 account for the increased steady state fluorescence that accompanies the conformational change in human pancreatic triglyceride lipase induced by tetrahydrolipstatin and bile salt". J. Biol. Chem. 284 (21): 14157–64. doi:10.1074/jbc.M901154200. PMC 2682864. PMID 19346257.
Ranaldi S, Belle V, Woudstra M, Bourgeas R, Guigliarelli B, Roche P et al. (2010). "Amplitude of pancreatic lipase lid opening in solution and identification of spin label conformational subensembles by combining continuous wave and pulsed EPR spectroscopy and molecular dynamics". Biochemistry 49 (10): 2140–9. doi:10.1021/bi901918f. PMID 20136147.

UpToDate Contents

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1. 血清アミラーゼまたは血清リパーゼの上昇が認められる患者へのアプローチ approach to the patient with elevated serum amylase or lipase
2. 急性膵炎の臨床症状および診断 clinical manifestations and diagnosis of acute pancreatitis
3. 慢性膵炎の治療 treatment of chronic pancreatitis
4. 成人における外傷による十二指腸および膵臓損傷のマネージメント management of duodenal and pancreatic trauma in adults
5. 嚢胞性線維症：膵機能不全の評価およびマネージメント cystic fibrosis assessment and management of pancreatic insufficiency

English Journal

Sphingoid esters from the molecular distillation of squid oil: A preliminary bioactivity determination.

Saliu F1, Longhin E2, Salanti A3, Degano I4, Della Pergola R3.
Food chemistry.Food Chem.2016 Jun 15;201:23-8. doi: 10.1016/j.foodchem.2016.01.056. Epub 2016 Jan 14.
A mixture of sphingoid esters was isolated (1.4% w/w) from the molecular distillation of crude squid visceral oil. A preliminary investigation on the bioactivity profile and toxic potential of this residue was carried out by in vitro experiments. No cytotoxicity and a moderate lipase inhibition acti
PMID 26868543

Crocus cancellatus subsp. damascenus stigmas: chemical profile, and inhibition of α-amylase, α-glucosidase and lipase, key enzymes related to type 2 diabetes and obesity.

Loizzo MR1, Marrelli M1, Pugliese A2, Conforti F1, Nadjafi F3, Menichini F1, Tundis R1.
Journal of enzyme inhibition and medicinal chemistry.J Enzyme Inhib Med Chem.2016 Apr;31(2):212-8. doi: 10.3109/14756366.2015.1016510. Epub 2015 Mar 20.
Spices are appreciated for their medicinal properties besides their use as food adjuncts to enhance the sensory quality of food. In this study, Crocus cancellatus subsp. damascenus was investigated for its antioxidant activities employing different in vitro systems. Stigma extract demonstrated a rad
PMID 25792502

Effects of Nicotine and Vagus Nerve in Severe Acute Pancreatitis-Associated Lung Injury in Rats.

Ma P1, Yu K, Yu J, Wang W, Ding Y, Chen C, Chen X, Zhao K, Zuo T, He X, Shi Q, Ren J.
Pancreas.Pancreas.2016 Apr;45(4):552-60. doi: 10.1097/MPA.0000000000000575.
OBJECTIVES: The cholinergic anti-inflammatory pathway has been elucidated as a regulator of inflammatory responses in several experimental models of diseases. This regulatory mechanism is mediated by acetylcholine, released from efferent vagus nerve, interacts with α7 nicotinic acetylcholine recept
PMID 26684861

Japanese Journal

SEW2871 Alleviates the Severity of Caerulein-Induced Acute Pancreatitis in Mice

Zou Lei,Ke Lu,Wu Congye [他],Tong Zhihui,Li Weiqin,Li Ning,Li Jieshou
Biological and Pharmaceutical Bulletin 38(7), 1012-1019, 2015
… Severity of AP, serum amylase and lipase activity, levels of serum cytokines, pancreatic myeloperoxidase (MPO) activity, CD45+CD4+ T lymphocytes in blood, CD4+ T cell infiltration in the pancreas, and proinflammatory cytokine production were assessed. …
NAID 130005086280

Measurement of feline lipase activity using a dry-chemistry assay with a triolein substrate and comparison with pancreas-specific lipase (Spec fPLTM)

OISHI Mariko,OHNO Koichi,SATO Toru,TAMAMOTO Takashi,KANEMOTO Hideyuki,FUKUSHIMA Kenjiro,TSUJIMOTO Hajime
Journal of Veterinary Medical Science advpub(0), 2015
… Pancreatic lipase immunoreactivity (Spec fPL) is currently considered to be the most accurate blood test for the diagnosis of feline pancreatitis. … In this study, we measured lipase activity in cats using a newer catalytic lipase assay of dry-chemistry system (FDC-v-LIP) to determine the reference range and compared the results with those for Spec fPL. …
NAID 130005074219

SEW2871 alleviates the severity of caerulein-induced acute pancreatitis in mice

Zou Lei,Ke Lu,Wu Congye,Tong Zhihui,Li Weiqin,Li Ning,Li Jieshou
Biological and Pharmaceutical Bulletin advpub(0), 2015
… Severity of AP, serum amylase and lipase activity, levels of serum cytokines, pancreatic myeloperoxidase (MPO) activity, CD45+CD4+ T lymphocytes in blood, CD4+ T cell infiltration in the pancreas, and proinflammatory cytokine production were assessed. …
NAID 130005068106

「膵リパーゼ」

Pancreatic lipase
	; Cartoon diagram of human pancreatic lipase (colored by secondary structure: alpha helices in red, beta sheets in yellow, and random coil in green) in complex with pig colipase (colored blue) and a small molecule inhibitor (upper left).
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1LPA, 1LPB, 1N8S
Identifiers
Symbols	PNLIP ; PL; PNLIPD; PTL
External IDs	OMIM: 246600 MGI: 97722 HomoloGene: 30999 ChEMBL: 1812 GeneCards: PNLIP Gene
EC number	3.1.1.3
Gene ontology
Molecular function	• triglyceride lipase activity; • metal ion binding; • retinyl-palmitate esterase activity;
Cellular component	• extracellular region;
Biological process	• retinoid metabolic process; • lipid metabolic process; • phototransduction, visible light; • lipid catabolic process; • intestinal cholesterol absorption; • lipid digestion; • small molecule metabolic process;
	Sources: Amigo / QuickGO
Orthologs
	This box: view; talk; edit;

　　[★]

英: pancreatic lipase
同: ステアプシン steapsin
関: リパーゼ

膵リパーゼによる反応は可逆的。
分解産物の濃度が高まると反応が停止。

至適pH 8.0
colipaseの存在下複合体を形成し至適pH 6.0となる。また、胆汁酸による酵素活性の抑制を受けない。

「pancreatic」

　　[★]

adj.

膵臓の、膵性の、膵の

関: pancreas、pancreata

[pmid7893686-1] PDB 1LPB; Egloff MP, Marguet F, Buono G, Verger R, Cambillau C, van Tilbeurgh H (March 1995). "The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate". Biochemistry 34 (9): 2751–62. doi:10.1021/bi00009a003. PMID 7893686.

[pmid1783385-2] Davis R, Diep A, Hunziker W, Klisak I, Mohandas T, Schotz M et al. (December 1991). "Assignment of human pancreatic lipase gene (PNLIP) to chromosome 10q24-q26". Genomics 11 (4): 1164–6. doi:10.1016/0888-7543(91)90048-J. PMID 1783385.

[entrez-3] "Entrez Gene: pancreatic lipase".

[pmid6207965-4] Koop H (September 1984). "Serum levels of pancreatic enzymes and their clinical significance". Clin Gastroenterol 13 (3): 739–61. PMID 6207965.

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案内

案内

pancreatic lipase