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doi : PMID Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase". More of the catalytic triad".
Bibcode : Natur. S2CID Bibcode : PNAS PMC Hirzel Wissenschaftliche Verlagsgesellschaft, Stuttgart, 2. Auflage, , S. Clin Gastroenterol. August Retrieved 18 April Journal of Lipid Research.
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Clin Gastroenterol Hepatol. Lipases are water-soluble enzymes that hydrolyze water-insoluble lipid molecules, such as triglycerides, phospholipids, and galactolipids.
They are ubiquitous in nature and are present in humans, animals, insects, plants, fungi, and microorganisms. While we commonly consider pancreatic lipase, this review provides an overview of several lipases that are important for the digestion and metabolism of lipids in veterinary species.
The pancreatic lipase gene family is one of the best characterized lipase gene families and consists of 7 mammalian subfamilies: pancreatic lipase, pancreatic lipase related proteins 1 and 2, hepatic lipase, lipoprotein lipase, endothelial lipase, and phosphatidylserine phospholipase A1.
Other mammalian lipases that play integral roles in lipid digestion include carboxyl ester lipase and gastric lipase. Although most enzymes have preferred substrate specificity, much overlap occurs across the plethora of lipases because of the similarities in their structures.
This has major implications for the development and clinical utilization of diagnostic assays. These implications are further explored in our companion Currents in One Health article by Lim et al in the August issue of the Journal of American Veterinary Medical Association , which focuses on pancreatic lipase assays for the diagnosis of pancreatitis.
L ipases are water-soluble enzymes that hydrolyze ester bonds of water-insoluble substrates, such as triglycerides, into diglycerides, monoglycerides, and fatty acids Figure 1. Citation: American Journal of Veterinary Research 83, 8; Lipases are ubiquitous in nature and are present in humans, animals, insects, plants, fungi, and microorganisms.
Many lipases are phylogenetically related. This Currents in One Health article provides an overview of endogenous lipases important for the digestion and metabolism of dietary lipids in veterinary species.
Using pancreatic lipase as a model, we will introduce the general structure and function of digestive lipases. Subsequently, we will look at selected subfamilies of the pancreatic lipase gene family, as well as carboxyl ester lipase and gastric lipase, focusing specifically on their distribution in various important species and their enzymatic functions.
Although most enzymes have their preferred substrate s , much overlap may occur across the plethora of digestive lipases. Measurement of specific lipases is also of diagnostic use in clinical patients.
Veterinary medicine is leading the way in the use of immunological assays that specifically quantify pancreatic lipase for the diagnosis of pancreatitis. This may have been driven by more challenging access to the advanced imaging modalities that are routinely used in humans with suspected pancreatitis and are considered far more sensitive and specific than is the case for dogs and cats.
The principles behind these assays do, however, have translational significance and could be of value in humans unable to undergo advanced imaging for a variety of reasons. Additionally, utilization of such assays may reduce diagnostic cost.
While lipases are commonly used as disease biomarkers, they play critical roles in the digestion of dietary fats among other physiologic roles.
The most abundant dietary fats are neutral fats, also known as triglycerides. Each molecule of triglyceride is composed of a glycerol backbone with 3 fatty acid side-chains Figure 1.
Other than triglycerides, small amounts of phospholipids and cholesterol esters are also present in the diet. Depending on the species, lipid digestion begins in the mouth or stomach through its mechanical and enzymatic function.
Emulsification enhances lipid digestion by producing micelles, which are small droplets of lipid dispersed in an aqueous matrix, thus increasing surface area for the hydrolytic action of pancreatic enzymes. Dietary fat is hydrolyzed by various pancreatic enzymes, which will be detailed in later sections of this review.
Pancreatic enzymes hydrolyze dietary fat eg, triglycerides, cholesterol esters, and phospholipids to lipolysis products, such as monoglycerides, cholesterol, and free fatty acids, that are then being solubilized and transported in micelles that are readily absorbed by enterocytes.
Each chylomicron is assembled within secretory vesicles of the Golgi apparatus and then migrates to the basolateral membrane of the enterocyte. Chylomicrons travel through the lymphatic circulations and empty into the circulatory system via the thoracic duct. A complete overview on lipid metabolism is beyond the scope of this article, and readers are encouraged to refer to readily available resources for a more comprehensive discussion on this topic.
These lipases are further discussed below. The pancreatic lipase gene family is the largest and, arguably, the most important family of lipases in veterinary medicine.
Pancreatic lipase was discovered by the French physiologist Claude Bernard in and was the first mammalian lipase of its gene family to be identified.
The partial primary sequence of pancreatic lipase porcine was first reported in and completed in Hepatic rat and lipoprotein lipases bovine were discovered later and added to this gene family.
Subsequently, pancreatic lipase-related proteins 1 PLRP1; human and 2 PLRP2; human , endothelial lipase mice , and phosphatidylserine phospholipase A1 rat and human were identified and the gene family was expanded further.
These mammalian and invertebrate lipases are grouped in the pancreatic lipase gene family because of the homology in their amino acid sequence and gene organization Figure 2. Within this gene family, PLRP1 and PLRP2 are most closely related to classical pancreatic lipase.
Lipase structure is closely related to its function. Therefore, knowing the 3-dimensional structure of a lipase helps us understand its function and substrate selectivity. These structures will be discussed using pancreatic lipase as a general model with notable similarities and differences between members of the gene family highlighted along the way.
Pancreatic lipase has 2 distinct domains, an N-terminal domain consisting of amino acid residues 1 to and a C-terminal domain consisting of amino acid residues to Figure 3.
It is common to all mammalian lipases of the pancreatic lipase gene family, carboxyl ester lipase, and gastric lipase.
When in the active form, the lid opens to expose the catalytic triad. When dietary fat is present in the intestinal lumen, bile salt lines up along the surface of this insoluble substrate, forming micelles Figure 4.
Colipase is secreted together with pancreatic lipase and is a cofactor for optimal pancreatic lipase activity. In the presence of micelles, pancreatic lipase changes from the inactive to the active form, with the 2 forms being present in equilibrium in the intraluminal fluid matrix.
Colipase also favors formation of active pancreatic lipase by stabilizing the mobile lid structure. This plateau is important for the interaction of water-soluble pancreatic lipase with water-insoluble lipid at the lipid-water interface.
This interaction results in the interfacial activation of pancreatic lipase. Because lipases of this gene family have a large degree of homology, there is much overlap in their function.
Generally speaking, apart from PLRP1 that has no apparent enzymatic activity, all other family members display variable substrate selectivity for triglycerides, phospholipids, and galactolipids. The pancreatic lipase gene family consists of 3 lipase subfamilies of pancreatic origin, namely, pancreatic lipase, PLRP1, and PLRP2.
Immunohistochemistry has demonstrated that pancreatic lipase is found exclusively in zymogen granules of pancreatic acinar cells and is thus pancreatic specific.
However, when the pancreas is inflamed, apical secretion is blocked, and large amounts of pancreatic lipase are released into the circulation via the basolateral aspect. Readers are referred to the companion Currents in One Health article by Lim et al in the August issue of the Journal of American Veterinary Medical Association , focusing on lipase assays for the diagnosis of pancreatitis.
Pancreatic lipase-related proteins 1 and 2 are found in the pancreas at lower concentrations than pancreatic lipase. Compared with pancreatic lipase, PLRP2 has a wider substrate specificity. In addition to triglycerides, PLRP2 also hydrolyzes phospholipids, galactolipids, retinyl esters vitamin A , and cholesterol esters.
Despite this tight association, it appears in media from cultured rat acinar cells and in pancreatic juice. In contrast to pancreatic lipase, which has low expression in neonates, PLRP2 and carboxyl ester lipase are highly expressed in neonates and are the 2 dominant lipases in milk-fat digestion.
Apart from the pancreas, PLRP2 is present in cultured mouse cytotoxic T-cells, enterocytes, Paneth cells of the human small intestines, seminal fluid from goats, THP-1 human monocyte cell line, and mouse antigen presenting cells.
Further studies on the functions and potential diagnostic utility of PLRP2 are urgently required. Hepatic lipase and lipoprotein lipase share a closer sequence homology with each other than with pancreatic lipase.
Lipoprotein lipase is synthesized by adipose tissue and muscle and is anchored to capillary endothelial cells. Similar to pancreatic lipase, hepatic and lipoprotein lipases are 2-domain enzymes i. It is mobilized into circulation and subsequently activated by high concentration of circulating high-density lipoproteins.
When activated, it preferentially hydrolyzes triglycerides in high-density lipoproteins. Similar to hepatic lipase, lipoprotein lipase binds via its heparin-binding site to HSPG located on endothelial cells.
It hydrolyzes triglycerides in triglyceride-rich lipoproteins, such as very-low density lipoproteins and chylomicrons. Lipoprotein lipase, however, requires activation by cofactor apolipoprotein C-II present on these triglyceride-rich lipoproteins. Because of their preferential binding to exogenous heparin, both hepatic and lipoprotein lipases are released into circulation by injection of heparin.
The activity level of circulating hepatic and lipoprotein lipases is dependent on various factors, including species and breed, 42 body condition score, 42 presence of postprandial hypertriglyceridemia, and sex hormone concentrations.
Triglyceride lipasd EC 3. These lipases Pancreattic closely related Pancreatic lipase each other and Herbal remedies online lipoprotein Pancreatic lipase EC 3. The most conserved Pacreatic in all these Panrceatic is centred Pajcreatic a serine residue which has Pancreatic lipase shown [3] to lipasf, with a histidine and Pancreativ 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. Pancreatic lipasealso known as pancreatic triacylglycerol lipase or steapsinis an enzyme secreted from the pancreas. As the primary lipase enzyme that hydrolyzes breaks down dietary fat molecules in the human digestive system, it is one of the main digestive enzymesconverting triglyceride substrates like 1 found in ingested oils to monoglycerides 3 and free fatty acids 2a and 2b. Thank you for visiting nature. You are using a browser version with Fat loss nutrition tips support for CSS. Lipaee obtain the best Pnacreatic, we recommend you use a more up to date browser or turn off compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. Pancreatic lipase PL and its related protein 1 PLRP1 are regulated by the amount of dietary fat through an apparent transcriptional mechanism.
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