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Nutrition in Clinical Practice :... Jun 2011Pancreatic enzyme supplementation is an important part of management for a number of gastrointestinal conditions. For patients who are unable to swallow pancreatin...
BACKGROUND
Pancreatic enzyme supplementation is an important part of management for a number of gastrointestinal conditions. For patients who are unable to swallow pancreatin capsules or granules, enteral feeding tubes can be used to administer the pancreatic enzyme. This presents challenges given the unique format of the pancreatic enzyme supplements, with common problems including tube blockage and loss of the enzyme's effect.
METHODS AND RESULTS
A novel technique is described for administration of pancreatic enzyme via feeding tubes. For gastrically placed tubes, this involves opening the pancreatin capsules and suspending the enzyme microspheres in thickened acidic fluid (such as the mildly thickened or "nectar-thick" fruit juice used for dysphagia) for delivery into the feeding tube. This technique minimizes tube blockage by preventing the enzyme from clumping in the tube. For jejunally placed tubes, enzyme microspheres can be crushed and activated with sodium bicarbonate before flushing into the tube, or the activated enzyme mixture can be added to enteral feeds.
CONCLUSIONS
Pancreatic enzyme supplementation can continue while patients receive enteral feeding. Using the described technique can help to avoid tube blockage and maintain optimal enzyme activity.
Topics: Deglutition Disorders; Dietary Supplements; Enteral Nutrition; Exocrine Pancreatic Insufficiency; Humans; Pancreas; Pancreatin
PubMed: 21508176
DOI: 10.1177/0884533611405537 -
Molecular and Cellular Biochemistry Nov 2002Enzyme load in pancreas has been considered a risk factor in the development of acute pancreatitis. In order to confirm this hypothesis our aim was to analyze the...
Enzyme load in pancreas has been considered a risk factor in the development of acute pancreatitis. In order to confirm this hypothesis our aim was to analyze the development and evolution of acute pancreatitis (AP) induced by bile-pancreatic duct obstruction (BPDO) after reducing the pancreatic enzyme content. L-364,718 - a potent CCK-receptor antagonist - was administered (0.1 mg/kg/day) for 7 days before inducing AP by BPDO. The course of AP was evaluated at different times from 1.5-48 h after BPDO. Amylase and trypsinogen contents and cytosolic calcium levels were measured by flow cytometry using specific antisera against pancreatic enzymes labelled with isothiocyanate of fluorescein and Fluo 3, respectively. The severity of the disease at the different stages was evaluated by measurements of amylase activity in ascites and plasma, percentage of pancreatic fluid and haematocrit. Electron microscopy study of the pancreas showed an increased number of zymogen granules spread through the acinar cells of control rats treated with L-364,718 for 7 days, however, total enzyme content in individual acinar cells was significantly (p < 0.01) diminished. AP significantly increased intracellular amylase and trypsinogen load from 3-12 h after BPDO, and prior L-364,718 treatment enhanced the blockade of enzyme secretion. As a result, acinar enzyme content was significantly increased from earlier stages (1.5 h after BPDO). In parallel, increased cytosolic calcium levels observed up to 24 h after BPDO appeared earlier in L-364,718-treated rats than in those not treated. The severity of AP seems to have been higher in rats previously treated with the CCK-receptor antagonist as indicated by the significantly higher pancreatic fluid and amylase activity in ascites and plasma observed at different times after BPDO. Our results indicate that there is no correlation between the severity of pancreatitis and the amount of enzymes accumulated in the pancreas before the disease is induced.
Topics: Acute Disease; Amylases; Animals; Bile Ducts; Calcium; Cholestasis, Extrahepatic; Devazepide; Disease Models, Animal; Male; Microscopy, Electron; Pancreas; Pancreatic Ducts; Pancreatitis; Rats; Rats, Wistar; Severity of Illness Index; Time Factors; Trypsinogen
PubMed: 12487374
DOI: 10.1023/a:1020603724002 -
Transplantation Proceedings Sep 2004The aim of this study was to investigate the results of 20 consecutive porcine islet isolations using a new enzyme Liberase PI. Twenty pancreata were procured for islet...
The aim of this study was to investigate the results of 20 consecutive porcine islet isolations using a new enzyme Liberase PI. Twenty pancreata were procured for islet isolation, which was performed using modified Ricordi's method with Liberase PI. Quantitation of islet viability staining, insulin stimulation assay, intracellular insulin content/DNA, and in vivo transplantability into diabetic nude mice were examined for quality control. The results were compared between a high-yield group (>2500 IEQ/g pancreas) and a low-yield group (<2500 IEQ/g pancreas). Sufficient amount of purified islets (3000 IEQ/g pancreas) were obtained using the new brand enzyme Liberase PI. These islets showed good quality in structure and functions, which were demonstrated by in vitro and in vivo standard assays. Isolation index (IEQ/number) of the low-yield group was lower than that of high-yield group (0.75 vs 0.86), which means more fragmentation of islets in the low-yield group. There were no differences in function between the two groups. In conclusion, we obtained sufficient numbers of viable, functional islets from porcine pancreas using a new brand enzyme Liberase PI and low-temperature isolation technique. However, overdigestion of islets during the isolation remains to be overcome. Advance in porcine islet isolation technique will in the future make the porcine islet xenotransplantation a reality for the cure of diabetes mellitus.
Topics: Animals; Cell Separation; Cell Survival; Collagenases; Islets of Langerhans; Models, Animal; Pancreas; Swine; Thermolysin; Transplantation, Homologous
PubMed: 15518798
DOI: 10.1016/j.transproceed.2004.08.010 -
Digestive and Liver Disease : Official... Jul 2007Benign pancreatic hyperenzymemia is a newly identified syndrome characterized by an abnormal increase in serum pancreatic enzymes in the absence of pancreatic disease.... (Review)
Review
Benign pancreatic hyperenzymemia is a newly identified syndrome characterized by an abnormal increase in serum pancreatic enzymes in the absence of pancreatic disease. The hyperenzymemia can occur sporadically or in a familial form, and all of the pancreatic enzymes show elevations. Although the condition is persistent, the enzyme elevations fluctuate considerably, even temporarily returning to normal levels at times. In this review the main characteristics of this syndrome are described.
Topics: Amylases; Humans; Lipase; Pancreas; Pancreatic Diseases; Time Factors
PubMed: 17531557
DOI: 10.1016/j.dld.2007.03.005 -
Comparative Medicine Feb 2002The aim of the study reported here was to investigate changes in the digestive enzyme content in the pancreas after food and secretagogue stimulation. Rats from which...
The aim of the study reported here was to investigate changes in the digestive enzyme content in the pancreas after food and secretagogue stimulation. Rats from which food had been withheld overnight were either fed (between 6 and 8 a.m.) or not before euthanasia and pancreatic excision (at 8 a.m.: 21 not fed and 21 fed) and at 4 (12 p.m.: six not fed and six fed) and 8 h later (4 p.m.: six not fed and six fed). Another 16 rats were anesthetized, fitted with jugular vein and pancreatic duct catheters, and infused with the secretagogues, CCK-33 and secretin, during 1.5 h of pancreatic juice collection before euthanasia and pancreatic excision. The pancreata were homogenized, and total soluble protein and individual enzyme (trypsin and amylase) tissue contents were analyzed. Results indicated lower amounts of protein and enzymes remaining in the pancreata of the fed, compared with non-fed rats. Enzyme values indicated recovery within four hours in fed rats, but non-fed rats also had increased values during daytime. High enzyme secretion during the high dose of hormonal stimulation was reflected in lower enzyme values remaining in the pancreas, compared with that in response to low-dose stimulation. Results indicated that stimulation of the pancreas, either by food ingestion or exogenous secretagogues, lowers the amounts of digestive enzymes remaining in the pancreas, and imply that stimulation and circadian rhythms influence the pancreatic enzyme content at euthanasia. This finding should be borne in mind in interpretation of data from pancreatic studies.
Topics: Amylases; Animals; Cholecystokinin; Dose-Response Relationship, Drug; Eating; Food Deprivation; Gastrointestinal Agents; Infusions, Intravenous; Male; Pancreas; Pancreatic Juice; Proteins; Rats; Rats, Sprague-Dawley; Secretin; Trypsin
PubMed: 11900410
DOI: No ID Found -
Digestion 1997
Review
Topics: Animals; Binding Sites; Calcium; Cell Membrane; Exocytosis; Humans; Intracellular Fluid; Ion Transport; Pancreas; Phosphoric Monoester Hydrolases; Protein Kinases
PubMed: 9225090
DOI: 10.1159/000201524 -
The American Journal of Physiology Nov 1980The earliest changes noted during the evolution of pancreatitis induced by feeding mice a choline-deficient ethionine-supplemented (CDE) diet are an increase in the...
The earliest changes noted during the evolution of pancreatitis induced by feeding mice a choline-deficient ethionine-supplemented (CDE) diet are an increase in the number of zymogen granules in pancreatic acinar cells and an increase in digestive enzyme content of the pancreas. We have studied the processes of protein and digestive enzyme synthesis and discharge at varying times after institution of the CDE diet, a choline-deficient diet (CD), and a diet containing ethionine but not choline-deficient (E). Both the CDE and E diets increased digestive enzyme content within 12 h of their institution. Both the CDE and E diets reduced the rate of protein and amylase synthesis and caused a marked reduction in the rate of protein and amylase discharge from the pancreas. These changes were greatest and were noted earliest in the CDE diet group. A marked reduction in secretagogue-induced in vivo and in vitro amylase discharge followed ingestion of either the CDE or E diet. These studies indicate that the increased pancreatic content of digestive enzymes noted after ingestion of the CDE and E diets results from an ethionine-induced decrease in the rat of digestive enzyme discharge. This phenomenon is enhanced by simultaneous choline deficiency. Subsequent intrapancreatic activation of zymogens may couple these changes in enzyme content to the development of hemorrhagic pancreatitis.
Topics: Amylases; Animals; Cholecystokinin; Choline; Choline Deficiency; Chymotrypsinogen; Ethionine; Female; Mice; Pancreas; Trypsinogen
PubMed: 6159794
DOI: 10.1152/ajpgi.1980.239.5.G418 -
Proteins 1991Interfacial catalysis is a necessary consequence for all enzymes that act on amphipathic substrates with a strong tendency to form aggregates in aqueous dispersions. In... (Review)
Review
Interfacial catalysis is a necessary consequence for all enzymes that act on amphipathic substrates with a strong tendency to form aggregates in aqueous dispersions. In such cases the catalytic event occurs at the interface of the aggregated substrate, the overall turnover at the interface is processive, and it is influenced the molecular organization and dynamics of the interface. Such enzymes can access the substrate only at the interface because the concentration of solitary monomers of the substrate in the aqueous phase is very low. Moreover, the microinterface between the bound enzyme and the organized substrate not only facilitates formation of the enzyme-substrate complex, but a longer residence time of the enzyme at the substrate interface also promotes high catalytic processivity. Binding of the enzyme to the substrate interface as an additional step in the overall catalytic turnover permits adaptation of the Michaelis-Menten formalism as a basis to account for the kinetics of interfacial catalysis. As shown for the action of phospholipase A2 on bilayer vesicles, binding equilibrium has two extreme kinetic consequences. During catalysis in the scooting mode the enzyme does not leave the surface of the vesicle to which it is bound. On the other hand, in the hopping mode the absorption and desorption steps are a part of the catalytic turnover. In this minireview we elaborate on the factors that control binding of pig pancreatic phospholipase A2 to the bilayer interface. Binding of PLA2 to the interface occurs through ionic interactions and is further promoted by hydrophobic interactions which probably occur along a face of the enzyme, with a hydrophobic collar and a ring of cationic residues, through which the catalytic site is accessible to substrate molecules in the bilayer. An enzyme molecule binds to the surface occupied by about 35 lipid molecules with an apparent dissociation constant of less than 0.1 pM for the enzyme on anionic vesicles compared to 10 mM on zwitterionic vesicles. Results at hand also show that aggregation or acylation of the protein is not required for the high affinity binding or catalytic interaction at the interface.
Topics: Animals; Binding Sites; Lipid Bilayers; Models, Molecular; Pancreas; Phospholipases A; Phospholipases A2; Protein Conformation; Swine
PubMed: 1866429
DOI: 10.1002/prot.340090402 -
La Nouvelle Presse Medicale Nov 1972
Review
Topics: Amylases; Animals; Cell Membrane; Cytoplasm; Cytoplasmic Granules; Dogs; Endopeptidases; Endoplasmic Reticulum; Esterases; Golgi Apparatus; Histocytochemistry; Humans; Lipase; Nucleotidyltransferases; Organoids; Pancreas; Pancreatic Juice; Peptide Hydrolases; Phospholipases
PubMed: 4565099
DOI: No ID Found -
Annual Review of Physiology 1977
Review
Topics: Amylases; Animals; Biological Transport; Carbachol; Carboxypeptidases; Cholecystokinin; Chymotrypsinogen; Cytoplasmic Granules; Enzyme Precursors; Exocytosis; Hydrolases; Kinetics; Models, Biological; Pancreas; Ribonucleases; Trypsinogen
PubMed: 322600
DOI: 10.1146/annurev.ph.39.030177.002105