where is pancreatic lipase found in the body
Discovery and development of gastrointestinal lipase inhibitors


the pancreatic juice to the small intestine, is stimulated by hormones. These hormones are induced in the stomach by hydrolysed products in gastric digestion. The pancreatic lipase is secreted to the small intestine where it is most active, at pH 7-7,5. Pancreatic lipase hydrolyses triglycerides and diglycerides by cleaving acyl chains at the sn-1 and sn-3 position and releases free fatty acids and 2-monoglycerides. The pancreatic lipase consists of 465 amino acids. Schematic picture of pancreatic lipase is shown in figure 2. Pancreatic and gastric lipases share little homology but
13869099
Gastric lipase


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 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
2531503
Pancreatic lipase family


system by a specialized vessel called a lacteal. This protein belongs to the 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. 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
620832
Lipase


signaling and inflammation. Thus, some lipase activities are confined to specific compartments within cells while others work in extracellular spaces. The main lipases of the human digestive system are pancreatic lipase (PL) and pancreatic lipase related protein 2 (PLRP2), which are secreted by the pancreas. Humans also have several other related enzymes, including hepatic lipase, endothelial lipase, and lipoprotein lipase. Not all of these lipases function in the gut (see table). Other lipases include , , , , , , , , , and
7317289
Pancreatic lipase family


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 () (LCAT), which catalyzes fatty acid transfer between phosphatidylcholine and cholesterol. "Pancreatic lipase", also known as "pancreatic triacylglycerol lipase" or "steapsin", is 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 enzymes
620830
Acute pancreatitis


necrosis can extend to include fascial layers in the immediate vicinity of the pancreas. The differential diagnosis includes: Regarding selection on these tests, two practice guidelines state: Most, but not all individual studies support the superiority of the lipase. In one large study, there were no patients with pancreatitis who had an elevated amylase with a normal lipase. Another study found that the amylase could add diagnostic value to the lipase, but only if the results of the two tests were combined with a discriminant function equation. While often quoted
19187085
Bile salt-dependent lipase


Bile salt-dependent lipase (or BSDL), also known as carboxyl ester lipase (or CEL) is an enzyme produced by the adult pancreas and aids in the digestion of fats. Bile salt-stimulated lipase (or BSSL) is an equivalent enzyme found within breast milk. BSDL has been found in the pancreatic secretions of all species in which it has been looked for. BSSL, originally discovered in the milk of humans and various other primates, has since been found in the milk of many animals including dogs,
2532114
Lipoprotein lipase


Lipoprotein lipase (LPL) () is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. It is a water-soluble enzyme that hydrolyzes triglycerides in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL), into two free fatty acids and one monoacylglycerol molecule. It is also involved in promoting the cellular uptake of chylomicron remnants, cholesterol-rich lipoproteins, and free fatty acids. LPL requires ApoC-II as a cofactor. LPL
4368042
Pancreatic enzymes (medication)


is sold as pancrelipase, which contains more active lipase enzyme than does pancreatin. The trypsin found in pancreatin works to hydrolyze proteins into oligopeptides; amylase hydrolyzes starches into oligosaccharides and the disaccharide maltose; and lipase hydrolyzes triglycerides into fatty acids and glycerols. Pancreatin is an effective enzyme supplement for replacing missing pancreatic enzymes, and aids in the digestion of foods in cases of pancreatic insufficiency. Pancreatin reduces the absorption of iron from food in the duodenum during digestion Some contact lens-cleaning solutions contain porcine pancreatin extractives to assist in the intended
15585862
Discovery and development of gastrointestinal lipase inhibitors


are excreted undigested with faeces. With this mode of action calorie uptake from fat in food is limited, hence body weight is reduced. The main role of lipase inhibitors is therefore to inhibit lipases in the gastrointestinal tract, but they do not have significant activity against proteases, amylases or other digestive enzymes. Cetilistat has a bicyclic structure but lacks the β-lactone ring. It acts in a similar way as a typical lipase inhibitor that has the β-lactone structure. As further discussed, orlistat is a pancreatic and gastric
13869093
Pancreatic lipase family


Triglyceride lipases () are a family of lipolytic enzymes that hydrolyse ester linkages of triglycerides. Lipases are widely distributed in animals, plants and prokaryotes. At least three tissue-specific isozymes exist in higher vertebrates, pancreatic, hepatic and gastric/lingual. These lipases are closely related to each other and to lipoprotein lipase (), which hydrolyses triglycerides of chylomicrons and very low density lipoproteins (VLDL). The most conserved region in all these proteins is centred on a serine residue which has been shown to participate, with an
620829
Lingual lipase


. Studies have shown that even in these cases, lingual lipase is present in normal amounts, and contributes to greater than 90% of total lipase activity in duodenum. This can be attributed to the fact that lingual lipase has a low pH optimum and can thus remain active through the stomach into the duodenum, where there is a low pH in patients with CF. It has, thus, been proposed that a possible treatment option for exocrine pancreatic insufficiency would be enzyme replacement therapy using lingual lipase, increasing the amount of dietary
7822595
Pancreatic enzymes (medication)


by the exocrine cells of the pancreas. It is composed of amylase, lipase and protease. This mixture is used to treat conditions in which pancreatic secretions are deficient, such as surgical pancreatectomy, pancreatitis and cystic fibrosis. It has been claimed to help with food allergies, celiac disease, autoimmune disease, cancer and weight loss. Pancreatin is sometimes called "pancreatic acid", although it is neither a single chemical substance nor an acid. Pancreatin contains the pancreatic enzymes trypsin, amylase and lipase. A similar mixture of enzymes
15585861
Human digestive system


occurs through the action of peristalsis, waves of muscular contractions that move along the stomach wall. This allows the mass of food to further mix with the digestive enzymes. Gastric lipase secreted by the chief cells in the fundic glands in the gastric mucosa of the stomach, is an acidic lipase, in contrast with the alkaline pancreatic lipase. This breaks down fats to some degree though is not as efficient as the pancreatic lipase. The pylorus, the lowest section of the stomach which attaches to the duodenum via the pyloric canal,
11200364
Discovery and development of gastrointestinal lipase inhibitors


deglycosylation of the enzyme does not affect the activity of the enzyme. The hydrophobic region around Ser152, which has the hexapeptide sequence Val-Gly-His-Ser-Gln-Gly, is essential for the catalytic activity of gastric lipase. At the N-terminal, Lys4 is necessary for the enzyme to bind at lipid-water interfaces. Pancreatic lipase is the most important lipolytic enzyme in the gastrointestinal tract and is essential for fat digestion. Pancreatic lipase is secreted from acinar cells in the pancreas and its secretion, with
13869098
Lingual lipase


fetus from 26 weeks of gestation on. After birth, fat in mother's milk or a milk substitute becomes the major source of nutrition. Absorptive rates of dietary fat are much lower in neonates than in adults, 65–80% as compared to 95% respectively, which can be attributed to low pancreatic lipase activity. Furthermore, milk fat is not a good substrate for pancreatic lipase. This fact, in combination with the bile salt deficiency and low pH throughout the gastrointestinal tract of the neonate, demands that lingual lipase be the
7822597
Pancreatic lipase family


, converting triglyceride substrates like 1 found in ingested oils to monoglycerides 3 and free fatty acids 2a and 2b. 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
620831
Lipid metabolism


Ingested cholesterol is not broken down by the lipases and stays intact until it enters the epithelium cells of small intestine. Lipids then continue to the stomach where chemical digestion continues by gastric lipase and mechanical digestion begins (peristalsis). The majority of lipid digestion and absorption, however, occurs once the fats reach the small intestines. Chemicals from the pancreas (pancreatic lipase family and bile salt-dependent lipase) are secreted into the small intestines to help breakdown the triglycerides, along with further mechanical digestion, until they are individual fatty
16960118
Discovery and development of gastrointestinal lipase inhibitors


Alli). Lipase inhibitors have also shown anticancer activity, by inhibiting fatty acid synthase. Pancreatic lipase inhibitor was originally discovered and isolated from fermented broth of the Streptomyces toxytricini bacterium in 1981 and named lipstatin. It is a selective and potent irreversible inhibitor of human gastric and pancreatic lipases. Tetrahydrolipstatin, more commonly known as orlistat, is a saturated derivative produced from hydrogen reaction. It was developed in 1983 by Hoffmann-La Roche and is a more simple and stable compound than lipstatin. For that reason orlistat was chosen over lipstatin
13869088
Gastric lipase


Gastric lipase, also known as LIPF, is an enzymatic protein that, in humans, is encoded by the "LIPF" gene. 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. 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
2531502
Colipase


Colipase is a protein co-enzyme required for optimal enzyme activity of pancreatic lipase. It is secreted by the pancreas in an inactive form, procolipase, which is activated in the intestinal lumen by trypsin. Its function is to prevent the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. In humans, the colipase protein is encoded by the "CLPS" gene. Colipase is also a family of evolutionarily related proteins. Colipase is a small protein cofactor needed by pancreatic lipase for
3514258
Management of obesity


structured setting, 67% of people who lost greater than 10% of their body mass maintained or continued to lose weight one year later. An average maintained weight loss of more than or 3% of total body mass could be sustained for five years. Several anti-obesity medications are currently approved by the FDA for long term use. Orlistat reduces intestinal fat absorption by inhibiting pancreatic lipase. Lorcaserin has been found to be effective in the treatment of obesity with a weight loss of 5.8 kg at one year as opposed to
11423999
Sphincter of Oddi dysfunction


, lasts 30 minutes or longer, and is not associated with a structural abnormality that could lead to these symptoms. The disorder is classified into two subtypes: functional biliary sphincter of Oddi disorder, where there is no disturbance in pancreatic enzyme measurements, such as amylase and lipase; and, functional pancreatic sphincter of Oddi disorder, where pancreatic enzyme measurements are elevated. Attacks can be precipitated by opioid analgesics, particularly in patients having undergone a cholecystectomy or bariatric surgery. Functional disorders of the gallbladder, bile duct and pancreas have been
337903
Colipase


efficient dietary lipid hydrolysis. Efficient absorption of dietary fats is dependent on the action of pancreatic triglyceride lipase. Colipase binds to the C-terminal, non-catalytic domain of lipase, thereby stabilising an active conformation and considerably increasing the hydrophobicity of its binding site. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture. Colipase is a small protein (12K) with five conserved disulphide bonds. Structural analogies have been recognised between a developmental protein (Dickkopf), the pancreatic lipase C-
3514259
Lipase


A lipase (, ) is any enzyme that catalyzes the hydrolysis of fats (lipids). Lipases are a subclass of the esterases. Lipases perform essential roles in digestion, transport and processing of dietary lipids (e.g. triglycerides, fats, oils) in most, if not all, living organisms. Genes encoding lipases are even present in certain viruses. Most lipases act at a specific position on the glycerol backbone of a lipid substrate (A1, A2 or A3)(small intestine). For example, human pancreatic lipase (HPL)
7317286
Pancreatitis


S—scorpion sting, H—hyperlipidemia, hypothermia, hyperparathyroidism, E—endoscopic retrograde cholangiopancreatography, D—drugs (commonly azathioprine, valproic acid, liraglutide) The differential diagnosis for pancreatitis includes but is not limited to cholecystitis, choledocholithiasis, perforated peptic ulcer, bowel infarction, small bowel obstruction, hepatitis and mesenteric ischemia. Diagnosis requires 2 of the 3 following criteria: Amylase and lipase are 2 enzymes produced by the pancreas. Elevations in lipase are generally considered a better indicator for pancreatitis as it has greater specificity and has
16668816
Discovery and development of gastrointestinal lipase inhibitors


Lipase inhibitors belong to a drug class that is used as an antiobesity agent. Their mode of action is to inhibit gastric and pancreatic lipases, enzymes that play an important role in the digestion of dietary fat. Lipase inhibitors are classified in the ATC-classification system as A08AB (peripherally acting antiobesity products). Numerous compounds have been either isolated from nature, semi-synthesized, or fully synthesized and then screened for their lipase inhibitory activity but the only lipase inhibitor on the market (October 2016) is orlistat (Xenical,
13869087
Lipase


traditional catalyst in processing biodiesel, as this enzyme replaces chemicals in a process which is otherwise highly energy intensive, and can be more environmentally friendly and safe. Industrial application of lipases requires process intensification for continuous processing using tools like continuous flow microreactors at small scale. Lipases are generally animal sourced, but can also be sourced microbially. Blood tests for lipase may be used to help investigate and diagnose acute pancreatitis and other disorders of the pancreas. Measured serum lipase values may vary depending on the method of analysis. Lipase can also
7317291
Antinutrient


the environment. Without the need to use milling to reduce phytate (including nutrient), the amount of phytic acid is commonly reduced in animal feeds by adding histidine acid phosphate type of phytases to them. Protease inhibitors are substances that inhibit the actions of trypsin, pepsin and other proteases in the gut, preventing the digestion and subsequent absorption of protein. For example, Bowman–Birk trypsin inhibitor is found in soybeans. Lipase inhibitors interfere with enzymes, such as human pancreatic lipase, that catalyze the hydrolysis of some lipids,
14075142
Sphincter of Oddi dysfunction


if the testing of liver enzymes, conjugated bilirubin, and pancreatic enzymes (amylase and lipase) are normal. If all of the above criteria are met, individuals are classified as having a functional biliary sphincter of Oddi disorder, if the testing of pancreatic enzymes (amylase and lipase) is normal. The old Milwaukee classification of biliary sphincter of Oddi dysfunction (SOD) used to divide the condition into three subtypes: but it is no longer in use. Type I included patients with biliary-type abdominal pain, with all
337905
Acinar cell carcinoma of the pancreas


nodules (due to fat necrosis) and arthralgias, caused by release of lipase. ACC are associated with increased serum lipase and manifest in the classic presentation as the "Schmid triad" (subcutaneous fat necrosis, polyarthritis, eosinophilia). ACC are typically large, up to 10 cm, and soft compared to pancreatic adenocarcinoma, lacking its dense stroma. They can arise in any part of the pancreas. Histomorphologically, the tumour resembles the cells of the pancreatic acini and, typically, have moderate granular cytoplasm that stain with both
19268708
Lingual lipase


the conserved catalytic triad, a diacylglycerol and a free fatty acid. Monoacylglyceride is also present in a lower concentration and is produced following a second round of hydrolysis by the same mechanism. It acts on tryglicerides to help breakdown food as a part of saliva composition. Patients with cystic fibrosis (CF) have an 85% chance of additionally experiencing the effects of exocrine pancreatic insufficiency. In the most extreme cases, these patients will produce no pancreatic lipase, yet even when the enzyme is completely absent, dietary fat is still absorbed
7822594
Human digestive system


where it is released to continue this digestion of fats. The presence of salivary lipase is of prime importance in young babies whose pancreatic lipase has yet to be developed. As well as its role in supplying digestive enzymes, saliva has a cleansing action for the teeth and mouth. It also has an immunological role in supplying antibodies to the system, such as immunoglobulin A. This is seen to be key in preventing infections of the salivary glands, importantly that of parotitis. Saliva also contains a glycoprotein called haptocorrin which is a binding
11200345
Digestion


acids. The digestive enzymes however are mostly secreted as their inactive precursors, the zymogens. For example, trypsin is secreted by pancreas in the form of trypsinogen, which is activated in the duodenum by enterokinase to form trypsin. Trypsin then cleaves proteins to smaller polypeptides. Digestion of some fats can begin in the mouth where lingual lipase breaks down some short chain lipids into diglycerides. However fats are mainly digested in the small intestine. The presence of fat in the small intestine produces hormones that stimulate the release of pancreatic lipase from
4159134
Discovery and development of gastrointestinal lipase inhibitors


of lipase inhibitors in fat digestion is shown in figure 1. These inhibitors bind covalently as an ester to the serine hydroxyl group at the active site on pancreatic- and gastric lipases and form a stable complex. This results in a conformational change in the enzyme which causes exposing of the catalytic active site. When the active site is exposed, the hydroxyl group on the serine residue is acylated. This leads to irreversible inactivation of the enzyme. The inactive lipase is incapable of hydrolysing fats into absorbable fatty acids and monoglycerides, therefore triglycerides
13869092
Biliary colic


complete blood count, liver function tests and lipase. In biliary colic, lab findings are usually within normal limits. Alanine aminotransferase and aspartate transaminase are usually suggestive of liver disease whereas elevation of bilirubin and alkaline phosphatase suggests common bile duct obstruction. Pancreatitis should be considered if the lipase value is elevated; gallstone disease is the major cause of pancreatitis. Biliary pain is most frequently caused by obstruction of the common bile duct or the cystic duct by a gallstone. However, the presence of gallstones is a frequent incidental finding and does
1987839
Pancreatic enzymes (medication)


Pancreatic enzymes, also known as pancrelipase and pancreatin, are commercial mixtures of amylase, lipase, and protease. They are used to treat malabsorption syndrome due to certain pancreatic problems. These pancreatic problems may be due to cystic fibrosis, surgical removal of the pancreas, long term pancreatitis, or pancreatic cancer, among others. The preparation is taken by mouth. Common side effects include vomiting, abdominal pain, constipation, and diarrhea. Other side effects include perianal irritation and high blood uric acid. The enzymes are from pigs.
15585858
Pancreatitis


, and certain genetic disorders such as cystic fibrosis among others. Smoking increases the risk of both acute and chronic pancreatitis. Diagnosis of acute pancreatitis is based on a threefold increase in the blood of either amylase or lipase. In chronic pancreatitis these tests may be normal. Medical imaging such as ultrasound and CT scan may also be useful. Acute pancreatitis is usually treated with intravenous fluids, pain medication, and sometimes antibiotics. Typically eating and drinking are disallowed, and a nasogastric tube is placed in the stomach. A procedure known
16668805
Exocrine pancreatic insufficiency


test, and a direct pancreatic function test. The latter is a limitedly used test that assesses exocrine function in the pancreas by inserting a tube into the small intestine to collect pancreatic secretions. EPI is often treated with pancreatic enzyme replacement products (PERPs) such as pancrelipase, that are used to break down fats (via a lipase), proteins (via a protease), and carbohydrates (via amylase) into units that can be digested. Pancrelipase is typically porcine derived and requires large doses. Chronic pancreatitis is the most
7499686
Pancreatic juice


Pancreatic juice is a liquid secreted by the pancreas, which contains a variety of enzymes, including trypsinogen, chymotrypsinogen, elastase, carboxypeptidase, pancreatic lipase, nucleases and amylase. The pancreas is located in the visceral region, and is a major part of the digestive system required for proper digestion and subsequent assimilation of macronutrient substances required for living. Pancreatic juice is alkaline in nature due to the high concentration of bicarbonate ions. Bicarbonate is useful in neutralizing the acidic gastric acid, allowing for effective enzymic changes. Pancreatic juice secretion is
9151714
Lipoprotein lipase deficiency


have been found to cause familial lipoprotein lipase deficiency so far. Treatment of LPLD has two different objectives: immediate prevention of pancreatitis attacks and long term reduction of cardiovascular disease risk. Treatment is mainly based on medical nutrition therapy to maintain plasma triglyceride concentration below 11,3 mmol/L (1000 mg/dL). Maintenance of triglyceride levels below 22,6 mmol/L (2000 mg/dL) prevents in general from recurrent abdominal pain. Strict low fat diet and avoidance of simple carbohydrates Restriction of dietary fat to not more than 20
19125753
Chronic pancreatitis


severe epigastric pain beginning in childhood. It is an autosomal dominant disease, chronic pancreatitis disease is identified in the cationic trypsinogen gene PRSS1, and mutation, R122H. R122H is the most common mutation for hereditary chronic pancreatitis with replacement of arginine with histidine at amino acid position 122 of the trypsinogen protein. There are, of course, other mechanisms – alcohol, malnutrition, smoking – each exhibiting its own effect on the pancreas. The diagnosis of chronic pancreatitis is based on tests on pancreatic structure and function. Serum amylase and lipase may
19187151
Discovery and development of gastrointestinal lipase inhibitors


have the same hydrophobic region at the active site, which is important for the lipolytic activity. The hydrophobic region has the hexapeptide sequence Val-Gly-His-Ser-Gln-Gly and is at Ser153 in pancreatic lipases but Ser152 in gastric lipases. The chemical structure of compounds play an important role in binding to their target. The most important and necessary chemical group for the binding and activity of these compounds is the β-lactone (beta-lactone) ring which is the central pharmacophore. The β-lactone
13869100
Acute pancreatitis


of pancreatic fat and vessel necrosis (hemorrhage). These are produced by intrapancreatic activation of pancreatic enzymes. Lipase activation produces the necrosis of fat tissue in pancreatic interstitium and peripancreatic spaces as well as vessel damage. Necrotic fat cells appear as shadows, contours of cells, lacking the nucleus, pink, finely granular cytoplasm. It is possible to find calcium precipitates (hematoxylinophilic). Digestion of vascular walls results in thrombosis and hemorrhage. Inflammatory infiltrate is rich in neutrophils. Due to the pancreas lacking a capsule, the inflammation and
19187084
Discovery and development of gastrointestinal lipase inhibitors


when given in combination. It can increase INR which can lead to insufficient anticoagulant treatment and bleeding. These adverse effects of orlistat are more common early in the therapy but usually decrease with time. Pancreatic lipases do not only affect the hydrolysis of triglycerides but are also necessary for hydrolysis of fat soluble vitamins. Due to this, the absorption of fat-soluble vitamins may decrease. Therefore, it is recommended to take a multiple-vitamin supplement during orlistat therapy. Cetilistat, a new lipase inhibitor, is an experimental drug for
13869090
Alpha-amylase


a shift to a starchy diet during human evolution. Pancreatic α-amylase randomly cleaves the α(1-4) glycosidic linkages of amylose to yield dextrin, maltose, or maltotriose. It adopts a double displacement mechanism with retention of anomeric configuration. The test for amylase is easier to perform than that for lipase, making it the primary test used to detect and monitor pancreatitis. Medical laboratories will usually measure either pancreatic amylase or total amylase. If only pancreatic amylase is measured, an increase will not be noted with mumps or other
14452950
Discovery and development of gastrointestinal lipase inhibitors


lipase inhibitor. Orlistat is also a potent thioesterase inhibitor and therefore inhibits fatty acid synthase (FAS). Since FAS is essential for tumor cells, for its growth and survival, and is upregulated and overexpressed in variety of tumors, scientists have high expectations for FAS as an oncology drug target. Orlistat inhibits FAS with the same mechanism as it does with pancreatic lipase, that is by binding covalently to the active serine site. Because of the difference in FAS expression between normal cells and cancer cells, orlistat selectively targets tumor cells
13869094
Glycerol monostearate


animal fats) and glycerol. Glycerol monostearate occurs naturally in the body as a product of the breakdown of fats by pancreatic lipase. It is present at very low levels in certain seed oils. GMS is a food additive used as a thickening, emulsifying, anticaking, and preservative agent; an emulsifying agent for oils, waxes, and solvents; a protective coating for hygroscopic powders; a solidifier and control release agent in pharmaceuticals; and a resin lubricant. It is also used in cosmetics and hair-care products. GMS
21064054
Abdominal ultrasonography


commonly used in the setting of abdominal pain or an acute abdomen (sudden and/or severe abdominal pain syndrome in which surgical intervention might be necessary), in which it can diagnose appendicitis or cholecystitis. Ultrasound can also be used if there is suspicion of enlargement of one or more organs, such as used in screening for abdominal aortic aneurysm, investigation for splenomegaly or urinary retention. Ultrasound can be used for additional anatomical information for patients with an abnormal kidney function or pancreatic enzymes (pancreatic amylase and pancreatic lipase). It can be
18919643
Lundh's test


Lundh's test is a test of function of the exocrine function of the pancreas gland. The exocrine role of the pancreas involves release of various digestive enzymes, including lipase and proteases, such as trypsin, in response to hormonal stimulation after eating. Disorders of the pancreas including chronic pancreatitis, cystic fibrosis and pancreatic cancer can lead to decreased pancreatic exocrine activity. Lundh's test involves placing a tube with multiple channels in to the duodenum. This tube has holes in the stomach and in the duodenum. A meal consisting of proteins
2320064
Secretin


by the products of protein digestion bathing the mucosa of the upper small intestine. Secretin release is inhibited by H antagonists, which reduce gastric acid secretion. As a result, if the pH in the duodenum increases above 4.5, secretin cannot be released. Secretin primarily functions to neutralize the pH in the duodenum, allowing digestive enzymes from the pancreas (e.g., pancreatic amylase and pancreatic lipase) to function optimally. Secretin targets the pancreas; pancreatic centroacinar cells have secretin receptors in their plasma membrane. As secretin binds to these
5266021
Trypsinogen


Trypsinogen (EC 3.4.23.18/20/21/23/24/26) () is the precursor form or zymogen of trypsin, a digestive enzyme. Produced by the pancreas, it is found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. It is activated by enterokinase, which is found in the intestinal mucosa, to form trypsin. Once activated, the trypsin can activate more trypsinogen into trypsin. Trypsin cleaves the peptide bond on the carboxyl side of basic amino acids such as arginine and lysine. Trypsinogen, as a precursor of trypsin, functions as
7485754
Johanson–Blizzard syndrome


Johanson–Blizzard syndrome is a rare, sometimes fatal autosomal recessive multisystem congenital disorder featuring abnormal development of the pancreas, nose and scalp, with mental retardation, hearing loss and growth failure. It is sometimes described as a form of ectodermal dysplasia. The disorder is especially noted for causing profound developmental errors and exocrine dysfunction of the pancreas, and it is considered to be an inherited pancreatic disease. The most prominent effect of JBS is pancreatic exocrine insufficiency. Varying degrees of decreased secretion of lipases, pancreatic juices such as trypsin,
13430569
Acute pancreatitis


lipase levels of 3 or more times the upper-limit of normal is diagnostic of pancreatitis, there are also other differential diagnosis to be considered relating to this rise. Regarding the need for computed tomography, practice guidelines state: CT is an important common initial assessment tool for acute pancreatitis. Imaging is indicated during the initial presentation if: CT is recommended as a delayed assessment tool in the following situations: CT abdomen should not be performed before the first 12 hours of onset of symptoms as early CT (12 hours) may
19187086
Anti-obesity medication


Anti-obesity medication or weight loss medications are pharmacological agents that reduce or control weight. These medications alter one of the fundamental processes of the human body, weight regulation, by altering either appetite, or absorption of calories. The main treatment modalities for overweight and obese individuals remain dieting and physical exercise. In the United States orlistat (Xenical) is currently approved by the FDA for long-term use. It reduces intestinal fat absorption by inhibiting pancreatic lipase. Rimonabant (Acomplia), a second medication, works via a
16148857
PLAT domain


In molecular biology the PLAT domain is a protein domain that is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase , which mediates membrane association. This domain is found in a variety of membrane or lipid associated proteins. It forms a beta-sandwich composed of two β-sheets of four β-strands each. ALOX12; ALOX12B
18998608
Pancreatic enzymes (medication)


the wholesale cost of this amount is about 300 to 900. In 2016 it was the 255th most prescribed medication in the United States with more than a million prescriptions. Pancrelipases are generally a first line approach in treatment of exocrine pancreatic insufficiency and other digestive disorders, accompanying cystic fibrosis, complicating surgical pancreatectomy, or resulting from chronic pancreatitis. The formulations are generally hard capsules filled with gastro-resistant granules. Pancrelipases and pancreatins are similar, except pancrelipases has an increased lipase component. Pancreatin is a mixture of several digestive enzymes produced
15585860
Dexelvucitabine


Dexelvucitabine is a failed experimental agent for the management of HIV infection. Dexelvucitabine is a cytidine nucleoside analog and nucleoside reverse transcriptase inhibitor. It was found to inhibit HIV-1 replication in vitro and during Phase II clinical trials, it was found to decrease mean viral load in patients with HIV. On April 3, 2006, Pharmasset and Incyte, the pharmaceutical companies developing dexelvucitabine announced the decision to cease further trials and development of the drug due to an increased incidence of grade 4 hyperlipasemia (an excess of the pancreatic enzyme, lipase)
15494486
Human digestive system


, bile salts, mucus and pigments, 1% fats and inorganic salts. Bilirubin is its major pigment. Bile acts partly as a surfactant which lowers the surface tension between either two liquids or a solid and a liquid and helps to emulsify the fats in the chyme. Food fat is dispersed by the action of bile into smaller units called micelles. The breaking down into micelles creates a much larger surface area for the pancreatic enzyme, lipase to work on. Lipase digests the triglycerides which are broken down into two fatty acids
11200371
Orlistat


may reduce plasma levels of ciclosporin (also known as "cyclosporin" or "cyclosporine", trade names Sandimmune, Gengraf, Neoral, etc.), an immunosuppressive drug frequently used to prevent transplant rejection; the two drugs should therefore not be administered concomitantly. Orlistat can also impair absorption of the antiarrhythmic amiodarone. The MHRA has recently suggested that Orlistat could theoretically reduce the absorption of antiretroviral HIV medications. Orlistat works by inhibiting gastric and pancreatic lipases, the enzymes that break down triglycerides in the intestine. When lipase activity is
15707199
Pancreas


central abdomen, that often radiates to the back, and may be associated with nausea or vomiting. Severe pancreatitis may lead to bleeding or perforation of the pancreas resulting in shock or a systemic inflammatory response syndrome, bruising of the flanks or the region around the belly button. These severe complications are often managed in an intensive care unit. In pancreatitis, enzymes of the exocrine pancreas damage the structure and tissue of the pancreas. Detection of some of these enzymes, such as amylase and lipase in the blood, along with symptoms
17478315
Iodolactonization


. They were able to synthesize the "cis" and "trans" five membered lactones by adjusting reactions conditions such as temperature and reaction time. The "trans" product was formed under thermodynamic conditions (e.g. a long reaction time) while the "cis" product was formed under kinetic conditions (e.g. a relatively shorter reaction time). Iodolactonization has been used in the syntheses of many biologically important products such as the tumor growth inhibitors vernolepin and vernomenin, the pancreatic lipase inhibitor vibralactone, and prostaglandins, a lipid found in
16594763
Yerba mate


cholesterol or aortic TBARS and antioxidant enzymes. The consumption of hot mate tea is associated with oral cancer, esophageal cancer, cancer of the larynx, and squamous cell cancers of the head and neck. Studies show a correlation between tea temperature and likelihood of cancer, making it unclear how much of a role mate itself plays as a carcinogen. Yerba mate contains polyphenols such as flavonoids and phenolic acids, which work by inhibiting enzymes like pancreatic lipase and lipoprotein lipase, which in turn play a role in fat metabolism. Yerba mate
4159445
Acid lipase disease


Acid lipase disease or deficiency is a name used to describe two related disorders of fatty acid metabolism. Acid lipase disease occurs when the enzyme lysosomal acid lipase that is needed to break down certain fats that are normally digested by the body is lacking or missing .This results in the toxic buildup of these fats in the body’s cells and tissues. These fatty substances, called lipids, include waxes, oils, and cholesterol. Three rare lipid storage diseases are caused by the deficiency of the enzyme lysosomal acid lipase: The prevalence of
14110981
Acute pancreatitis


, presumably patients whose only laboratory abnormality is an elevated lipase or amylase do not need assessment with the APACHE-II; however, this approach is not studied. The APACHE-II score can be calculated at www.sfar.org. Practice guidelines state: The Ranson score is used to predict the severity of acute pancreatitis. They were introduced in 1974. The criteria for point assignment is that a certain breakpoint be met at any time during that 48 hour period, so that in some situations it can be calculated shortly after admission. It
19187102
Ascariasis


the ampulla of Vater, or go into the main pancreatic duct, resulting in acute pancreatitis with raised serum levels of amylase and lipase. Occasionally, a worm can travel through the billiary tree and even into the gallbladder, causing acute cholangitis or acute cholecystitis. Ascariasis may result in allergies to shrimp and dustmites due to the shared antigen, tropomyosin; this has not been confirmed in the laboratory. The worms in the intestine may cause malabsorption and anorexia which contribute to malnutrition. The malabsorption may be due to a loss of brush
20149550
Fatty acid metabolism


cannot be absorbed by the intestine. They are broken down into mono- and di-glycerides plus free fatty acids (but no free glycerol) by pancreatic lipase, which forms a 1:1 complex with a protein called colipase (also a constituent of pancreatic juice), which is necessary for its activity. The activated complex can work only at a water-fat interface. Therefore, it is essential that fats are first emulsified by bile salts for optimal activity of these enzymes. The digestion products consisting of a mixture of tri-
3618915
Enterostatin


Enterostatin is a pentapeptide derived from a proenzyme in the gastrointestinal tract called procolipase. It reduces food intake, in particular fat intake, when given peripherally or into the brain. Enterostatin is created in the intestine by pancreatic procolipase, the other colipase serving as an obligatory cofactor for pancreatic lipase during fat digestion. Enterostatin can be created in the gastric mucosa and the mucosal epithelia in the small intestine. An increased high fat diets will cause the procolipase gene transcription and enterostatin to release into the gastrointestinal lumen. Enterostatin appears in the lymph
9634488
Apolipoprotein C2


Apolipoprotein C2 or apolipoprotein C-II is a protein that in humans is encoded by the "APOC2" gene. The protein encoded by this gene is secreted in plasma where it is a component of very low density lipoproteins and chylomicrons. This protein activates the enzyme lipoprotein lipase in capillaries, which hydrolyzes triglycerides and thus provides free fatty acids for cells. Mutations in this gene cause hyperlipoproteinemia type IB, characterized by xanthomas, pancreatitis, and hepatosplenomegaly, but no increased risk for atherosclerosis. Lab tests will show elevated blood levels of
9394527
Laxative


making a user less able to move feces through the colon on their own. A study of patients with chronic constipation found that 28% of chronic stimulant laxative users lost haustral folds over the course of one year, while none of the control group did. Castor oil is a glyceride that is hydrolyzed by pancreatic lipase to ricinoleic acid, which produces laxative action by an unknown mechanism. Properties Long-term use of castor oil may result in loss of fluid, electrolytes, and nutrients. These are motility stimulants that work through
6216943
Pancreas


regress. 10,000 protein coding genes (50% of all genes) are expressed in the normal human pancreas. Less than 100 of these genes are more specifically expressed in the pancreas. Similar to the salivary glands, most of the pancreas specific genes encode for secreted proteins. Corresponding pancreas specific proteins are either expressed in the exocrine cellular compartment and have functions related to digestion of food uptake such as digestive chymotrypsinogen enzymes and pancreatic lipase PNLIP, or expressed in the various cells of the endocrine pancreatic islets and have functions related to secreted
17478301
Ampulla of Vater


form the common bile duct. This duct subsequently joins with the pancreatic duct; this junction is known as the ampulla of Vater. The pancreatic duct delivers substances such as bicarbonate and digestive enzymes to the duodenum. The bile from the gallbladder contains salts which emulsify large fat droplets into much smaller units. This provides a large surface area for the lipase enzymes to act on. The bicarbonate neutralises the acidic chyme, creating alkaline conditions for enzymes such as chymotrypsin and amylase to function optimally. Various smooth muscle sphincters regulate the flow of
17539598
Lipoprotein lipase deficiency


an emergent acute abdomen. Other typical symptoms are eruptive xanthomas (in about 50% of patients), lipemia retinalis and hepatosplenomegaly. "Complications:" Patients with LPLD are at high risk of acute pancreatitis, which can be life-threatening, and can lead to chronic pancreatic insufficiency and diabetes. Lab tests show massive accumulation of chylomicrons in the plasma and corresponding severe hypertriglyceridemia. Typically, the plasma in a fasting blood sample appears creamy (plasma lactescence). Familial LPL deficiency should be considered in anyone with severe hypertriglyceridemia and
19125750
Anti-obesity medication


inhibiting pancreatic lipase, an enzyme that breaks down triglycerides in the intestine. Without this enzyme, triglycerides from the diet are prevented from being hydrolyzed into absorbable free fatty acids and are excreted undigested. A published phase 2 trial found cetilistat significantly reduced weight with and was better tolerated than orlistat. Lorcaserin (Belviq) was approved June 28, 2012 for obesity with other co-morbidities. The average weight loss by study participants was modest, but the most common side effects of the medication are considered benign. It reduces appetite by
16148868
Spleen pain


pain requires a broad differential approach. Lab evaluation may help rule in other causes of abdominal pain. Elevated liver function tests, bilirubin or lipase, may suggest a hepatobiliary or pancreatic source for pain. Leukocytosis and elevated lactate dehydrogenase (LDH) may be found in splenic infarction. However, these results lack specificity to splenic infarct. Radiographic testing is required to detect this rare illness. In the hyperacute phase of infarction, abdominal CT scan performed with intravenous contrast is the imaging modality of choice in suspected splenic infarction. Splenic infarct
4628901
Leptospirosis


For those with liver involvement, mild elevations of transaminases and direct bilirubin can be observed in liver function tests. The "Leptospira Icterohaemorrhagiae" serogroup is most commonly associated with jaundice and elevated bilirubin levels. In those with glucose-6-phosphate dehydrogenase deficiency, leptospirosis can contribute to acute hemolytic anaemia and conjugated hyperbilirubinemia. Abnormal serum amylase and lipase levels (associated with pancreatitis) can be common in those who are admitted into a hospital due to leptospirosis. Impaired kidney function with creatinine clearance less than 50 ml/min is associated with elevated pancreatic enzymes
6028650
Endothelial lipase


Endothelial lipase (LIPG) is a form of lipase secreted by vascular endothelial cells in tissues with high metabolic rates and vascularization, such as the liver, lung, kidney, and thyroid gland. The LIPG enzyme is a vital component to many biological process. These processes include lipoprotein metabolism, cytokine expression, and lipid composition in cells. Unlike the lipases that hydrolyze Triglycerides, endothelial lipase primarily hydrolyzes phospholipids. Due to the hydrolysis specificity, endothelial lipase contributes to multiple vital systems within the body. On the contrary to the beneficial
2531390
Hepatic lipase


then interact with LDL and IDL by transferring over fatty acids that have accumulated in the plaque. Hepatic lipase can then catalyze the conversion of IDL to LDL by breaking down triacylglycerides in IDL and release free fatty acids to be used by other cells with low concentrations of cholesterol or stored in the liver for later use. The human body contains two inactive forms of HL. One inactive form is found on the liver bound to HSPG (heparin sulfate proteoglycans) and the second inactive form is found in the blood bound to HDL,
2071967
Endothelial lipase


roles that LIPG plays within the body, endothelial lipase is thought of to play a potential role in cancer and inflammation. Knowledge obtained in vitro and in vivo suggest the relations to these conditions, but human interaction knowledge lacks due to the recent discovery of endothelial lipase. Endothelial lipase was first characterized in 1999. The two independent research groups which are notable for this discovery cloned the endothelial lipase gene and identified the novel lipase secreted from endothelial cells. The anti-Atherosclerosis opportunity through alleviating plaque blockage and prospective ability to raise High
2531391
Lysosomal acid lipase deficiency


Lysosomal acid lipase deficiency (LAL deficiency or LAL-D), is an autosomal recessive inborn error of metabolism that results in the body not producing enough active lysosomal acid lipase (LAL) enzyme. This enzyme plays an important role in breaking down fatty material (cholesteryl esters and triglycerides) in the body. Infants, children and adults that suffer from LAL deficiency experience a range of serious health problems. The lack of the LAL enzyme can lead to a build-up of fatty material in a number of body organs including
11266832
Hepatic lipase


lipase gene. Clinical features are not well understood and there are no characteristic xanthomas. There is an association with a delay in atherosclerosis in an animal model. In many studies that have been conducted, hepatic lipase is also closely related to obesity. In one test, an experiment was created by Cedó et al where mouse cells were created to have a mutated HL protein that has lost its function. They found that a build-up of triglyceride levels lead to nonalcoholic fatty liver disease. This was due to HL’s inability
2071972
Acid lipase disease


Wolman's disease there is a mutation with in the LIPA gene,which maps to chromosome 10q23.2, has 10 exons and is approximately 45 kb in length, thatencodes for the lysosomal acid lipase enzyme. This mutation causes a loss of function in the gene.This results in the toxic buildup of fats in the body's cells and tissues, which causes an array of symptoms. In both Wolman disease and Cholesteryl ester storage disease there is a deficiency of lysosomal acid lipase which causes an array of symptoms with in the body.
14110984
Pancreatic cancer


secondary cancers that have spread from other parts of the body. This is uncommon, found in only about 2% of cases of pancreatic cancer. Kidney cancer is by far the most common cancer to spread to the pancreas, followed by colorectal cancer, and then cancers of the skin, breast, and lung. Surgery may be performed on the pancreas in such cases, whether in hope of a cure or to alleviate symptoms. Risk factors for pancreatic adenocarcinoma include: Drinking alcohol excessively is a major cause of chronic pancreatitis,
5634763
Acid lipase disease


the cell. When the lysosomal acid lipase enzyme is functioning properly, fats such as triglycerides and cholesteryl esters are broken down into their simpler lipid components through hydrolysis. After triglycerides are broken down, the fatty acids are used for energy. Cholesteryl esters are broken down into its cholesterol and fatty acid components, this delivers cholesterol to the cell. These lipids are either used by the body or sent to the liver for removal. In acid lipase disease the lysosomal acid lipase enzyme is either lacking or missing. In both CESD and
14110983
Hormone-sensitive lipase


diglyceride lipase, and the third enzyme that cleaves the final fatty acid is called monoglyceride lipase. Only the initial enzyme is affected by hormones, hence its hormone-sensitive lipase name. The diglyceride and monoglyceride enzymes are tens to hundreds of times faster, hence HSL is the rate-limiting step in cleaving fatty acids from the triglyceride molecule. HSL is activated when the body needs to mobilize energy stores, and so responds positively to catecholamines, ACTH. It is inhibited by insulin. Previously, glucagon was thought to activate HSL
4083776
Progenitor cell


that these progenitor cells could move through the body and migrate towards the tissue where they are needed. Many properties are shared by adult stem cells and progenitor cells. Progenitor cells are found in adult organisms and they act as a repair system for the body. They replenish special cells, but also maintain the blood, skin and intestinal tissues. They can also be found in developing embryonic pancreatic tissue. The majority of progenitor cells lie dormant or possess little activity in the tissue in which they reside. They exhibit slow growth and
17059710
Lipase inhibitors


remain attached to the lipase. Studies have shown that lipase inhibitors work optimally when 40% of an individual's daily caloric intake is obtained from fat. Orlistat tends to block absorption of 30% of total fat intake from a meal, as orlistat passes out of the digestive tract more rapidly than fat does. Lipase inhibitors can be found naturally in plants and can also be produced as pharmaceutical drugs. Some lipase inhibitors have been identified in "Panax ginseng". Lipase inhibitors can cause side effects, including oily spotting, fecal
10661329
Lipase inhibitors


Lipase inhibitors are substances used to reduce the activity of lipases found in the intestine. Lipases are secreted by the pancreas when fat is present. The primary role of lipase inhibitors is to decrease the gastrointestinal absorption of fats. Fats then tend to be excreted in feces rather than being absorbed to be used as a source of caloric energy, and this can result in weight loss in individuals. These inhibitors could be used for the treatment of obesity, which can subsequently lead to Type II diabetes and cardiovascular diseases if not managed.
10661327
Ketogenesis


critical enzyme, succinyl CoA transferase, to process ketone bodies, and therefore cannot undergo ketolysis. The result is that the liver only produces ketone bodies, but does not use a significant amount of them. Ketogenesis may or may not occur, depending on levels of available carbohydrates in the cell or body. This is closely related to the paths of acetyl-CoA: Insulin and glucagon are key regulating hormones of ketogenesis. Both hormones regulate hormone-sensitive lipase and acetyl-CoA carboxylase. Hormone-sensitive lipase produces diglycerides
7260995
Lipase


, which is the main enzyme that breaks down dietary fats in the human digestive system, converts triglyceride substrates found in ingested oils to monoglycerides and two fatty acids. Several other types of lipase activities exist in nature, such as phospholipases and sphingomyelinases; however, these are usually treated separately from "conventional" lipases. Some lipases are expressed and secreted by pathogenic organisms during an infection. In particular, "Candida albicans" has a large number of different lipases, possibly reflecting broad-lipolytic activity, which may contribute to the
7317287
Human digestive system


and proteins. Some of these are released in response to the production of CKK in the duodenum. (The enzymes that digest polysaccharides, by contrast, are primarily produced by the walls of the intestines.) The cells are filled with secretory granules containing the precursor digestive enzymes. The major proteases, the pancreatic enzymes which work on proteins, are trypsinogen and chymotrypsinogen. Elastase is also produced. Smaller amounts of lipase and amylase are secreted. The pancreas also secretes phospholipase A2, lysophospholipase, and cholesterol esterase. The precursor zymogens
11200379
Aspergillus wentii


media supplemented with glucose of pH 6.0 at a temperature of 30 °C. "Aspergillus wentii" grown in mannitol media produces the second largest lipase yield (with 84% lipase activity). Lipase activity for "Aspergillus wentii" grown on fructose media produces just under 50% lipase activity while media supplemented with galactose, sucrose, lactose or maltose all yielded moderate lipase activity (20–37%). "Aspergillus wentii" strain NRRL 2001 spores were found to naturally produce glucose from hydrolyzing soluble starch. Of all "Aspergilli"
6385850
Pancreatic disease


insufficiency (EPI) is the inability to properly digest food due to a lack of digestive enzymes made by the pancreas. EPI is found in humans afflicted with cystic fibrosis and Shwachman–Diamond syndrome. It is caused by a progressive loss of the pancreatic cells that make digestive enzymes. Chronic pancreatitis is the most common cause of EPI in humans. Loss of digestive enzymes leads to maldigestion and malabsorption of nutrients. Cystic fibrosis, is a hereditary disease that affects the entire body, causing progressive disability and early death. It is
8830327
Pancreatic fistula


also assist in diagnosis, with the latter an essential component of treatment. An external pancreatic fistula is an abnormal communication between the pancreas (actually pancreatic duct) and the exterior of the body via the abdominal wall. Loss of bicarbonate-rich pancreatic fluid via a pancreatic fistula can result in a hyperchloraemic or normal anion gap metabolic acidosis. Loss of a small volume of fluid will not cause a problem but an acidosis is common if the volume of pancreatic fluid lost from the body is large. First described by Smith (1953
18753159
Triglyceride


acids are identical. Their names indicate the fatty acid: stearin derived from stearic acid, palmitin derived from palmitic acid, etc. These compounds can be obtained in three crystalline forms (polymorphs): α, β, and β′, the three forms differing in their melting points. If the first and third chain R and R″ are different, then the central carbon atom is a chiral center, and as a result the triglyceride is chiral. The pancreatic lipase acts at the ester bond, hydrolyzing the bond and "releasing
11702334
Secretin-cholecystokinin test


The secretin-cholecystokinin test (aka Secretin-CCK test, Secretin-Pancreozymin test) is a combination of the secretin test and the cholecystokinin test and is used to assess the function of both the pancreas and gall bladder. Cholecystokinin, a hormone secreted by the APUD cells located in the proximal mucosa of the small intestine is administered intravenously, this stimulates the pancreatic secretion of the digestive enzymes amylase, trypsin, and lipase. These are measured by a catheter placed in the duodenum. Cholecystokinin also stimulates the flow of bile and
19513266
Gallbladder


cell count suggestive of inflammation or infection. Tests such as bilirubin and liver function tests may reveal if there is inflammation linked to the biliary tree or gallbladder, and whether this is associated with inflammation of the liver, and a lipase or amylase may be elevated if there is pancreatitis. Bilirubin may rise when there is obstruction of the flow of bile. A CA 19-9 level may be taken to investigate for cholangiocarcinoma. Ultrasound is often the first medical imaging test performed when gallbladder disease such as gallstones are suspected. An
19520522
Secretin


the ductal cells of the pancreas. It also stimulates bile production by the liver; the bile emulsifies dietary fats in the duodenum so that pancreatic lipase can act upon them. Meanwhile, in concert with secretin's actions, the other main hormone simultaneously issued by the duodenum, cholecystokinin, is stimulating the gallbladder to contract, delivering its stored bile for the same reason. Prosecretin is a precursor to secretin, which is present in digestion. Secretin is stored in this unusable form, and is activated by gastric acid in the lower
5266015
Human digestive system


the jejunum. It starts at the duodenal bulb and ends at the suspensory muscle of duodenum. The attachment of the suspensory muscle to the diaphragm is thought to help the passage of food by making a wider angle at its attachment. Most food digestion takes place in the small intestine. Segmentation contractions act to mix and move the chyme more slowly in the small intestine allowing more time for absorption (and these continue in the large intestine). In the duodenum, pancreatic lipase is secreted together with a co-enzyme, colipase
11200384
Diabetic ketoacidosis


imprecise. In addition to the above, blood samples are usually taken to measure urea and creatinine (measures of kidney function, which may be impaired in DKA as a result of dehydration) and electrolytes. Furthermore, markers of infection (complete blood count, C-reactive protein) and acute pancreatitis (amylase and lipase) may be measured. Given the need to exclude infection, chest radiography and urinalysis are usually performed. If cerebral edema is suspected because of confusion, recurrent vomiting or other symptoms, computed tomography may be
11702362