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- | Human gastric lipase (HGL, E.C. 3.1.1.3) (PBD ID: 1hlg) is a type of [[lipase]] (of the enzyme class [[hydrolase]]) that is responsible for initiating the digestion of dietary fats in the stomach <ref name="armand">PMID:7598069</ref>. This enzyme is secreted by the fundic chief cells of the human stomach and catalyzes 10-20% of total lipolytic processes (i.e., those involving fat breakdown) in healthy adults <ref name="armand" />. HGL specifically catalyzes the hydrolysis of triacylglycerol in order to produce diacylglycerol and a carboxylate byproduct <ref name="roussel">PMID:10358049</ref>, a process that facilitates subsequent fat breakdown by [[pancreatic lipase]] <ref name="dogs">PMID:20965171</ref>. In terms of disease implications, there is evidence to suggest that HGL secretion is altered in individuals with gastritis <ref name="gastritis">PMID:23899880</ref>. | + | Human gastric lipase (HGL, E.C. 3.1.1.3) (PBD ID: 1hlg) is a type of [[lipase]] (of the enzyme class [[hydrolase]]) that is responsible for initiating the digestion of dietary fats in the stomach <ref name="armand">PMID:7598069</ref>. This enzyme is secreted by the fundic chief cells of the human stomach and catalyzes 10-20% of total lipolytic processes (i.e., those involving fat breakdown) in healthy adults <ref name="armand" />. HGL specifically catalyzes the hydrolysis of triacylglycerol in order to produce diacylglycerol and a carboxylate byproduct <ref name="roussel">PMID:10358049</ref>, a process that facilitates subsequent fat breakdown by pancreatic lipase <ref name="dogs">PMID:20965171</ref>. In terms of disease implications, there is evidence to suggest that HGL secretion is altered in individuals with gastritis <ref name="gastritis">PMID:23899880</ref>. |
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Revision as of 21:43, 8 April 2016
Introduction
Human gastric lipase (HGL, E.C. 3.1.1.3) (PBD ID: 1hlg) is a type of lipase (of the enzyme class hydrolase) that is responsible for initiating the digestion of dietary fats in the stomach [1]. This enzyme is secreted by the fundic chief cells of the human stomach and catalyzes 10-20% of total lipolytic processes (i.e., those involving fat breakdown) in healthy adults [1]. HGL specifically catalyzes the hydrolysis of triacylglycerol in order to produce diacylglycerol and a carboxylate byproduct [2], a process that facilitates subsequent fat breakdown by pancreatic lipase [3]. In terms of disease implications, there is evidence to suggest that HGL secretion is altered in individuals with gastritis [4].
Function
Disease
Relevance
Structural highlights
HGL, a 379 amino acid residue-long lipase enzyme, possesses a catalytic arm consisting of residues Ser-153, His-353, and Asp-324 [2].
References
- ↑ 1.0 1.1 Armand M, Hamosh M, DiPalma JS, Gallagher J, Benjamin SB, Philpott JR, Lairon D, Hamosh P. Dietary fat modulates gastric lipase activity in healthy humans. Am J Clin Nutr. 1995 Jul;62(1):74-80. PMID:7598069
- ↑ 2.0 2.1 Roussel A, Canaan S, Egloff MP, Riviere M, Dupuis L, Verger R, Cambillau C. Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J Biol Chem. 1999 Jun 11;274(24):16995-7002. PMID:10358049
- ↑ Selvan A, Seniya C, Chandrasekaran SN, Siddharth N, Anishetty S, Pennathur G. Molecular dynamics simulations of human and dog gastric lipases: insights into domain movements. FEBS Lett. 2010 Nov 19;584(22):4599-605. doi: 10.1016/j.febslet.2010.10.021. Epub, 2010 Oct 20. PMID:20965171 doi:http://dx.doi.org/10.1016/j.febslet.2010.10.021
- ↑ Tomasik PJ, Wedrychowicz A, Rogatko I, Zajac A, Fyderek K, Sztefko K. Gastric lipase secretion in children with gastritis. Nutrients. 2013 Jul 29;5(8):2924-32. doi: 10.3390/nu5082924. PMID:23899880 doi:http://dx.doi.org/10.3390/nu5082924