Lipase and pepsin activity in the gastric mucosa of infants, children, and adults

DiPalma, Joan; Kirk, Charlotte L.; Hamosh, Margit; Colón, A. R.; Benjamin, Stanley B.; Hamosh, Paul

doi:10.1016/0016-5085(91)90467-y

Cited by 70 publications

(36 citation statements)

References 31 publications

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“…There have been a few observations of the activity of pancreatic enzymes in the epithelial cells of nonpancreatic organs [1,[3][4][5] and some ultrastructural observations of zymogen granules in these cells [6,18]. However, we find the presence of pancreatic digestive enzymes in several nonpancreatic gastrointestinal organs, albeit at much lower levels than in the pancreas, confirming that the nonpancreatic organs produce much smaller quantities of pancreatic digestive enzymes than does the pancreas.…”

Section: Discussionsupporting

confidence: 84%

“…Our recent studies have shown immunoreactive pancreatic digestive enzymes in the intrahepatic biliary system [26][27][28][29][30]32]. Although lipase activity has been noted in several tissues, including the stomach (gastric lipase) [1,3,16,17,25,34], pancreatic lipase has not been reported in non-pancreatic organs. Donaldson et al [5] reported amylase activity in the human bile, and recently Doglioni et al [4] reported that pancreatic acinar metaplasia in the stomach was positive for immunoreactive pancreatic α-amylase and lipase.…”

Section: Discussionmentioning

confidence: 98%

“…The pancreas is the major site of such digestive enzymes; it produces and secretes enzymes that digest proteins, peptides, saccharides, lipids and nucleotides [23]. These include pancreatic α-amylase (EC 3 [23]. The enzymes have been considered to be present exclusively in the pancreas [37], although lipase activity (nonpancreatic lipase) is present in several organs including the liver, adipose tissue and stomach [16,17,25,34].…”

Section: Introductionmentioning

confidence: 99%

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Expression of pancreatic digestive enzymes in normal and pathologic epithelial cells of the human gastrointestinal system

et al. 1997

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Pancreatic digestive enzymes have rarely been reported in human nonpancreatic organs. We examined their expression in the epithelial cells of the nonpancreatic gastrointestinal organs, looking for pancreatic alpha-amylase, trypsin, chymotrypsin and pancreatic lipase. Western blotting, enzyme assay and pancreatic alpha-amylase mRNA were also used in selected specimens. In normal tissues, immunoreactivity of one or more of these enzymes was frequently noted in cells of the salivary glands, stomach, duodenum, large pancreatic ducts, extrahepatic bile ducts and gall bladder. The epithelium of the normal oesophagus, small intestine and colon were consistently negative for these enzymes. In pathologic tissues, immunoreactivity for one or more enzymes was present in epithelial cells of pleomorphic adenomas of the salivary glands, oesophageal squamous cell carcinoma, gastric adenoma and adenocarcinoma, pancreatic adenocarcinoma, cholecystitis, adenocarcinoma of the gall bladder and extrahepatic bile duct, and colon adenoma and adenocarcinoma. Western blotting showed a specific band of each enzyme in some specimens of normal stomach. In situ hybridization for pancreatic alpha-amylase mRNA showed specific signals in the normal stomach, but not in the normal colon. Reverse transcriptase polymerase chain reaction analysis for pancreatic alpha-amylase mRNA revealed specific signals in the normal stomach. Enzyme assay revealed that the stomach and gall bladder showed these activities. The data suggest that pancreatic digestive enzymes are produced by several epithelial cell types of the nonpancreatic gastrointestinal organs, that the organs positive for pancreatic enzyme have a common cell lineage, and that neoplasms continue to express or neoexpress these enzymes after neoplastic transformation.

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Section: Discussionsupporting

confidence: 84%

Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Expression of pancreatic digestive enzymes in normal and pathologic epithelial cells of the human gastrointestinal system

et al. 1997

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“…much lower activity in premature infants than in CF, with 183 Ϯ 16 U/mL at baseline and 92 Ϯ 4 U/mL after feeding. This may be related to the low pepsinogen secretion in premature infants compared with fullterm infants (58,59). Gastric enzyme activity expressed as units per milliliter is dependent on the volume of gastric secretions and on dilution by the test meal; therefore, comparison of enzyme output (expressed as total units per kilogram body weight) is more pertinent (Table 5).…”

Section: Discussionmentioning

confidence: 99%

Gastric Function in Children with Cystic Fibrosis: Effect of Diet on Gastric Lipase Levels and Fat Digestion

et al. 2004

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The effect of diet, usual (44 Ϯ 4% energy as fat), high-fat (49 Ϯ 4% energy as fat), and moderate-fat (33 Ϯ 2% energy as fat), on gastric function (lipase and pepsin activities, pH, emptying rate) and intragastric digestion of fat were assessed in six children with cystic fibrosis. Fasting and postprandial activity of digestive enzymes, gastric pH, and gastric volume measured before, during, and after 120 min of feeding did not differ significantly as a function of fat intake. Postprandial gastric lipase output (units per kilogram of body weight) during usual, moderate-fat, and high-fat diets was close to or higher than (38.8 Ϯ 7.2, 44.9 Ϯ 8.6, and 54.8 Ϯ 5.5 U/kg per 20 min) gastric lipase output of premature infants (22.5 Ϯ 6.4 to 28.3 Ϯ 6.6 U/kg per 20 min) or of healthy adults (5.4 Ϯ 0.4 U/kg per 15 min) fed a high-fat diet. Postprandial pepsin output was higher (4749 Ϯ 797, 6117 Ϯ 925, and 5444 Ϯ 819 U/kg per 20 min) than in premature infants (597 Ϯ 77 to 743 Ϯ 97 U/kg per 20 min) or healthy adults (781 Ϯ 56 U/kg per 15 min). Eighty minutes after feeding gastric lipolysis reached 20 to 36%. This study shows that gastric lipase activity is high in cystic fibrosis patients maintained on diets providing 32% to 49% energy as fat, and that gastric lipase level did not increase over the ranges of dietary fat intake tested. CF is the most common autosomal recessive disorder in Caucasians and results in pulmonary, gastrointestinal, metabolic and nutritional disturbances (1-3). The basic defect in CF involves faulty regulation of the epithelial cell chloride channel caused by mutations in the CFTR gene (4). Deletion of phenylalanine at amino acid position 508 (⌬F508) in the CFTR protein accounts for 70% of CF gene abnormalities in patients of Northern European ancestry (5). The ⌬F508 mutation leads to defective maturation of CFTR and absence of the protein at the apical membrane (6). Greater than 98% of ⌬F508 homozygotes have PI.PI, resulting in fat malabsorption, is found in at least 85% of CF patients (7-9). Lacking pancreatic enzymes, CF patients are dependent on pancreatic enzyme supplements (10 -12). However, the degree to which fat is absorbed by these patients varies, and even when pancreatic lipase activity is completely absent, dietary fat is absorbed. Indeed, Ross (13) reported fat absorption of 26 to 81% in a group of children with CF, although most of them did not have detectable pancreatic lipase activity. Lapey et al. (14) reported greater than 50% fat absorption in 15 patients with exocrine PI secondary to CF, without any oral enzyme supplementation. Ross and Sammons (15) have therefore postulated the presence of compensatory lipolytic activity in PI. It was shown subsequently that this compensation is provided by gastric lipase, the enzyme that initiates fat digestion in the stomach (16,17

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“…The data, however, suggest that the pepsin-catalyzed cleavage of FA and the subsequent release of PVP chains from the gel surface was quite rapid, and hence no transition from surface degradation to bulk degradation was observed in the range of concentrations studied. In the development of albumin-crosslinked hydrogels for oral drug delivery, this consistency in the degradation mechanism would be helpful when one considers the variations in the levels of pepsin found in the stomach [37,38]. By utilizing a system which can undergo surface or bulk degradation over a wide range of enzyme concentrations, the rate of drug release from the system can be effectively controlled.…”

Section: Effect Of Enzyme Concentration On Hydrogel Degradationmentioning

confidence: 98%

A Mechanistic Assessment of Enzyme-Induced Degradation of Albumin-Crosslinked Hydrogels

Shalaby

Chen

Park

1992

Journal of Bioactive and Compatible Polymers

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Pepsin-induced degradation of albumin-crosslinked hydrogels was studied as a function of the degree of albumin incorporation in the network and the concentration of pepsin. The degree of albumin incorporation, which represents the sum of chemical crosslinks and physical entanglements in the network, was controlled by changing the concentration of initiator in the monomer solution and the degree of vinylic functionality on albumin. Swelling characterization studies showed that the degree of hydrogel swelling decreased as the concentration of chemical initiator for the polymerization increased or as the degree of vinylic functionality on albumin increased. This indicated that the degree of albumin incorporation in the network increased by raising either the concentration of chemical initiator or the degree of albumin functionality. The rate and mechanism of gel degradation was also dependent on the degree of albumin incorporation in the network. A low degree of albumin incorporation resulted in a predominance of surface degradation while a high degree of albumin incorporation resulted in a predominance of bulk degradation. The transition from surface degradation to bulk degradation occurred at lower concentrations of chemical initiator when the degree of vinylic functionality on albumin was high. However, when the degree of vinylic functionality on albumin was low, the transition from surface degradation to bulk degradation was observed at higher concentrations of chemical initiator. The rate of gel degradation became slower as the concentration of pepsin was reduced. The results suggest that the rate and mechanism of hydrogel degradation was dependent on the steric constraints imposed by polymer chains of the network and on the conformational constraints of the albumin crosslinker.

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Lipase and pepsin activity in the gastric mucosa of infants, children, and adults

Cited by 70 publications

References 31 publications

Expression of pancreatic digestive enzymes in normal and pathologic epithelial cells of the human gastrointestinal system

Expression of pancreatic digestive enzymes in normal and pathologic epithelial cells of the human gastrointestinal system

Gastric Function in Children with Cystic Fibrosis: Effect of Diet on Gastric Lipase Levels and Fat Digestion

A Mechanistic Assessment of Enzyme-Induced Degradation of Albumin-Crosslinked Hydrogels

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