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Gastric lipase - Wikipedia

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Gastric lipase

Crystal structure of human gastric lipase (PDB 1hlg).^[1]

Identifiers

Symbol

LIPF

Other data

Chr. 10 q23

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Gastric lipase, also known as LIPF, is an enzymatic protein that, in humans, is encoded by the LIPF gene.^[2]^[3]

Function

Gastric lipase is an acidic lipase secreted by the gastric chief cells in the fundic mucosa in the stomach. It has a pH optimum of 3–6.^[4] Gastric lipase, together with lingual lipase, comprise the two acidic lipases. These lipases, unlike alkaline lipases (such as pancreatic lipase), do not require bile acid or colipase for optimal enzymatic activity. Acidic lipases make up 30% of lipid hydrolysis occurring during digestion in the human adult, with gastric lipase contributing the most of the two acidic lipases. In neonates, acidic lipases are much more important, providing up to 50% of total lipolytic activity.

Gastric lipase hydrolyzes the ester bonds of triglycerides in the stomach. Fatty acids and diacylglycerols are produced from this reaction. The long chain free fatty acids have the ability to prevent gastric lipase from hydrolyzing more triglycerides. In this case, gastric acid will be responsible for less than 30% of lipid hydrolysis.^[5] These enzymes are found in the cytoplasm and cell membranes of gastric cells. Gastric lipase is not the primary lipase needed for the majority of triglyceride hydrolysis. Outside of the stomach, gastric lipase can hydrolyze triacylglycerol in the duodenum with the help of other lipases and bile secretion. It is an essential enzyme for hydrolyzing milk fat globule membranes.^[6] For a newborn with an underdeveloped pancreas, LIPF plays a more important role in lipid digestion compared to an adult with a fully functioning pancreas. There is typically an increase in production of LIPF when the pancreas is unable to operate at its optimal potential.^[7] Low levels of LIPF are typically seen in the tumors of gastric cancer patients.^[8]

Clinical significance

Gastric lipase can partially compensate for the decrease in production of pancreatic lipase associated with pancreatic dysfunction, giving some means for the body to digest lipids. A limitation of acidic lipases is that they remove only one fatty acid from each triacylglycerol. The free fatty acid can readily cross the epithelial membrane lining the gastrointestinal tract, but the diacylglycerol cannot be transported across. This leaves the acidic lipases less efficient than alkaline lipases.^{[citation needed]}

Structure

Gastric lipase is a polypeptide of 371 residues in length. The structure of gastric lipase was determined using X-ray diffraction with a resolution of 3.00 Å, and is composed of 41% helices and 14% beta sheets.^[1] Gastric lipase belongs to the α/β-hydrolase-fold family. It possesses a classical catalytic triad (Ser-153, His-353, Asp-324) and an oxyanion hole (backbone NH groups of Gln-154 and Leu-67) analogous to serine proteases.

References

^ ^a ^b PDB: 1hlg; Roussel A, Canaan S, Egloff MP, Rivière M, Dupuis L, Verger R, Cambillau C (June 1999). "Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest". The Journal of Biological Chemistry. 274 (24): 16995–7002. doi:10.1074/jbc.274.24.16995. PMID 10358049.
^ Bodmer MW, Angal S, Yarranton GT, Harris TJ, Lyons A, King DJ, et al. (August 1987). "Molecular cloning of a human gastric lipase and expression of the enzyme in yeast". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 909 (3): 237–44. doi:10.1016/0167-4781(87)90083-2. PMID 3304425.
^ "Entrez Gene: gastric lipase".
^ Link Text
^ Pafumi Y, Lairon D, de la Porte PL, Juhel C, Storch J, Hamosh M, Armand M (August 2002). "Mechanisms of inhibition of triacylglycerol hydrolysis by human gastric lipase". The Journal of Biological Chemistry. 277 (31): 28070–9. doi:10.1074/jbc.M202839200. PMID 11940604.
^ Bourlieu C, Mahdoueni W, Paboeuf G, Gicquel E, Ménard O, Pezennec S, et al. (February 2020). "Physico-chemical behaviors of human and bovine milk membrane extracts and their influence on gastric lipase adsorption". Biochimie. 169: 95–105. doi:10.1016/j.biochi.2019.12.003. PMID 31866313.
^ Aloulou A, Carrière F (March 2008). "Gastric lipase: an extremophilic interfacial enzyme with medical applications". Cellular and Molecular Life Sciences. 65 (6): 851–4. doi:10.1007/s00018-008-7546-z. PMC 11131824. PMID 18213443. S2CID 45128975.
^ Kong Y, Zheng Y, Jia Y, Li P, Wang Y (October 2016). "Decreased LIPF expression is correlated with DGKA and predicts poor outcome of gastric cancer". Oncology Reports. 36 (4): 1852–60. doi:10.3892/or.2016.4989. PMC 5022960. PMID 27498782.

External links

gastric+lipase,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4:
Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)

3.1.11-16:
Exonuclease

Exodeoxyribonuclease	RecBCD
Exoribonuclease	Oligonucleotidase

3.1.21-31:
Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme;see {{Restriction enzyme}} UvrABC endonuclease
Endoribonuclease	RNase III Drosha: Microprocessor complex Dicer: RNA-induced silencing complex RNase H 1 2A 2B 2C RNase P RNase A RNase Z RNase E 1 2 3 4/5 RNase T1
either deoxy- or ribo-	Nuclease S1 Mung bean nuclease Serratia marcescens nuclease Micrococcal nuclease

Category:

Genes on human chromosome 10

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