Severe acute pancreatitis and normal serum amylase activity due to pancreatic isoamylase deficiency

1989 ◽  
Vol 34 (4) ◽  
pp. 644-646 ◽  
Author(s):  
A. Borgstr�m ◽  
M. Bohe
Keyword(s):  
Acute Pancreatitis ◽  
Severe Acute Pancreatitis ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Normal Serum ◽  
Pancreatic Isoamylase ◽  
Serum Amylase Activity

(Washington University case conference): acute pancreatitis, hyperlipemia, and normal amylase.

1978 ◽  
Vol 24 (5) ◽  
pp. 815-820 ◽  
Keyword(s):  
Acute Pancreatitis ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Normal Serum ◽  
Case Conference ◽  
Diagnosis And Management ◽  
Serum Amylase Activity ◽  
Washington University

Abstract This case focuses on the biochemical findings in acute pancreatitis and the role of the laboratory in the diagnosis and management of such patients. It also illustrates a major unappreciated problem in the use of amylase determinations in patients with acute pancreatitis: normal serum amylase activity in the presence of hyperlipemia.

scholarly journals The roles of Na+/H+ exchanger regulatory factor 1 and aquaporin-1 in the pathomechanism of experimental acute pancreatitis

2019 ◽  
Author(s):  
Zsolt Balla
Keyword(s):  
Acute Pancreatitis ◽  
Pancreatic Necrosis ◽  
Serum Amylase ◽  
Apical Membrane ◽  
Amylase Activity ◽  
Fluid Secretion ◽  
Leukocyte Infiltration ◽  
Regulatory Factor ◽  
Control Groups ◽  
Serum Amylase Activity

Introduction: Pancreatic ductal epithelial cells (PDEC) secrete an alkaline HCO_3^- rich isotonic fluid. The secretion of HCO_3^- across the apical membrane of PDEC is mediated by cystic fibrosis transmembrane conductance regulator Cl- channel (CFTR) and solute carrier family 26 (SLC26) anion exchangers. Na+/H+ exchanger regulatory factor isoform 1 (NHERF 1) is a cytosolic adaptor protein, which binds CFTR on the apical membrane of epithelial cells. Aquaporins (AQPs) facilitate the transepithelial water flow involved in epithelial fluid secretion in numerous tissues. Acute pancreatitis (AP) is a serious disorder in which specific treatment is still not possible. Accumulating evidence indicate that decreased pancreatic ductal fluid secretion plays an essential role in AP. The role of NHERF-1 in the pancreas has not yet been investigated despite the fact that CFTR, a key regulator of epithelial function, is controlled by this scaffolding protein Also the functions of AQPs in the pancreas are less characterized. Our aim was to characterize the function of NHERF-1 and AQP1 in AP. Methods: We used 12 16 week old WT, NHERF 1 knock-out (KO) and AQP1 KO male mice. In the AP groups, mice were injected 7 or 10 times hourly, intraperitoneally (i.p.) with 50 µg/kg cerulein. In another AP model, 4 % Na taurocholate was administered i.d. via the punctured duodenum. Control animals were injected i.p. or i.d. with PS instead of cerulein or Na taurocholate (n=6-8). Animals were sacrificed at 12 hours in case of the cerulein model or 24 hours in the Na taurocholate experiment. Laboratory [serum amylase or, pancreatic myeloperoxidase (MPO) activity, pancreatic IL 1β concentrations] and histological parameters (pancreatic necrosis, edema, inflammatory cell infiltration) were measured to evaluate disease severity. Expression of HSP 72, IκB α, and IκB β contents were determined by Western blot analysis. Our results showed that the induction of AP was successful in both models and also in both strains. The injection of mice with cerulein or Na taurocholate increased the measured laboratory and histological parameters vs. the control groups. The measured laboratory (serum amylase, HSP72) and histological parameters (necrosis, apoptosis) were significantly elevated in AP mice injected with cerulein vs. control mice. In accord with the measured pancreatic MPO , trypsinogen activity, IκB α, IκB β, or pancreatic IL 1β concentrations were not significantly altered in the NHERF 1 KO group vs. the WT AP groups. In case of the Na taurocholate-induced AP, pancreatic necrosis, hemorrhage and MPO activity were significantly increased in the NHERF 1 KO group vs. the WT AP group. However, the pancreatic edema, leukocyte infiltration, IL 1β concentrations and serum amylase activity were significantly elevated in the WT or NHERF 1 KO AP vs. respective control groups but not in the NHERF 1 KO vs WT AP groups. The pancreatic leukocyte infiltration, edema, necrosis or serum amylase activity were significantly increased in cerulein-treated vs. control groups. In accord with the histological results, only necrosis and serum amylase activity were increased significantly in the AQP1 KO vs. WT AP groups. In conclusion, after complete evaluation of the data, we can say that the AP in both NHERF 1 or AQP1 KO groups were more severe. These results may be due the reduced HCO_3^- and fluid secretion.

Severe Acute Pancreatitis, Normal Serum Amylase and Lipase

2008 ◽  
Vol 103 ◽  
pp. S86
Author(s):  
Bielose Konwe ◽  
Hector Amaya ◽  
Nolan Perez ◽  
James Hanley
Keyword(s):  
Acute Pancreatitis ◽  
Severe Acute Pancreatitis ◽  
Serum Amylase ◽  
Normal Serum

Elevated Amylase Levels as a Result of Self-Induced Hypersalivation

PEDIATRICS ◽  
1983 ◽  
Vol 71 (4) ◽  
pp. 585-587
Author(s):  
Jacques Belik ◽  
Carl Tishler ◽  
Juhling McClung
Keyword(s):  
Acute Pancreatitis ◽  
Abdominal Pain ◽  
Pediatric Patients ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Elevated Serum ◽  
Pancreatic Disease ◽  
Sensitive Indicator ◽  
Recurrent Vomiting ◽  
Serum Amylase Activity

A patient with recurrent vomiting, abdominal pain, and elevated serum amylase activity may have pancreatitis. Although elevated serum amylase levels are a sensitive indicator for acute pancreatitis, this test is not highly specific for pancreatic disease. A patient is described who illustrates the need for specific laboratory, historical, and occasional psychological evaluation in pediatric patients with elevated amylase values.

Restoration of intestinal mucosal in Euphorbia kansui-treated severe acute pancreatitis rats is based on HMGB1/MFG-E8 expression

2020 ◽  
Vol 21 ◽  
Author(s):  
Chengjiang Qiu ◽  
Kairui Liu ◽  
Xuguang Li ◽  
Weirun Chen ◽  
Sheng Zhang ◽  
...  
Keyword(s):  
Acute Pancreatitis ◽  
Severe Acute Pancreatitis ◽  
Serum Amylase ◽  
Intestinal Barrier ◽  
Enzyme Linked Immunosorbent Assay ◽  
Inflammatory Factor ◽  
Apoptotic Cells ◽  
Rat Ileum ◽  
Plasma Endotoxin ◽  
Euphorbia Kansui

Background: The pathogenesis of severe acute pancreatitis (SAP) is mediated substantially by dysfunctions in the intestinal barrier. Euphorbia kansui (EK) is a medicinal plant used widely in traditional Chinese medicine to treat inflammation; however, its efficacy and mechanism of action in SAP treatment is not yet well understood. Objective: To investigate the role of EK in intestinal barrier tissue repair and in the pathogenesis and development of SAP. Methods: The rat SAP model was established by a retrograde injection of sodium taurocholate into the pancreatic bile duct. The SAP model group and the SAP + EK treatment groups were divided into 6 subgroups according to timing: 2, 6, 12, 24, 48, or 72 h after inducing SAP. The progression of the SAP rats and of the rats receiving the EK treatment was evaluated using the ascites volume, serum amylase and plasma endotoxin levels, and histological grading of intestinal mucosal damage. In addition, serum inflammatory factor contents were measured using enzyme-linked immunosorbent assay (ELISA) tests and apoptotic cells in damaged ileum tissue were detected using TUNEL staining. Apoptosis markers and other signaling proteins in intestinal mucosal cells were detected by immunohistochemical assays and then validated by combining these data with quantitative polymerase chain reactions and western blotting. Results: Compared with the results of the SAP model rats, the results of the rats that received EK treatment demonstrated that EK could effectively reduce the ascites volume and serum amylase and plasma endotoxin levels. EK treatment also greatly reduced the abnormal intestinal morphological alterations in the rat SAP model and significantly downregulated the serum contents of interleukin (IL)-1β, IL-6, and tumor necrosis factor-α. EK treatment inhibited the elevation of capapse-3, inhibited the decrease of the Bcl-2 protein, and decreased the number of apoptotic cells in rat ileum tissue. Finally, EK treatment abrogated the increase of HMGB1 and the suppression of MFG-E8 protein expression in the SAP + EK rat ileum tissue. Conclusion: EK suppresses SAP pathogenesis by restoring intestinal barrier function and modulating the HMGB1/MFG-E8 signaling axis.

scholarly journals Secrets, puzzles and mysteries of macroamylasemia

2020 ◽  
Vol 46 (1) ◽  
pp. 12-22
Author(s):  
N. B. Gubergrits ◽  
N. V. Byelyayeva ◽  
G. M. Lukashevich ◽  
T. L. Mozhyna
Keyword(s):  
Serum Amylase ◽  
Amylase Activity ◽  
Clinical Manifestations ◽  
Specific Treatment ◽  
Normal Serum ◽  
Amylase Level ◽  
Clearance Ratio ◽  
Urine Amylase ◽  
Classical Constant

Physiological features of amylase synthesis and excretion are considered in the article, presence of other sources of amylase synthesis different from pancreas and salivary glands is emphasized. Definitions of hyperenzymemia and macroamylasemia (MAE) are given. MAE is a state characterized by presence of circulating complexes of normal serum amylase with protein or carbohydrates in blood. There are 3 types of MAE: first — classical (constant hyperamylasemia, decreased amylase level in urine, high blood concentration of macroamylase complexes); second — hyperamylasemia with slightly decreased amylase activity in urine, macroamylase/normal amylase ratio is less than in the first type; third — normal blood and urine amylase activity, low macroamylase/normal amylase ratio. Pathogenesis is explained by connection of blood amylase and acute phase protein in different inflammatory, infectious diseases, malabsorption. MAE clinical manifestations could be absent, sometimes abdominal pain is possible. Hyperamylasemia and reduced urine amylase activity are typical. MAE diagnostics means determination of macroamylase complexes in blood (chromatography, calculation of the clearance ratio of amylase and creatinine). The article presents clinical cases describing extra-pancreatic MAE in women with malignant ovarian lesions. The question of expediency of thorough diagnostic examination in asymptomatic MAE is raised, which may turn out to be a symptom of cancer. The lack of specific treatment for MAE is emphasized.

An Automated, Saccharogenic Method for Determining Serum Amylase Activity

1970 ◽  
Vol 16 (12) ◽  
pp. 985-989 ◽  
Author(s):  
Wendell R O'Neal ◽  
Nathan Gochman
Keyword(s):  
Glucose Oxidase ◽  
Blood Donors ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Serum Glucose ◽  
Normal Range ◽  
Reducing Substances ◽  
Serum Amylase Activity

Abstract An automated adaptation of the Somogyi saccharogenic determination of serum amylase is described in which conventional AutoAnalyzer modules are used. Adequate sensitivity with short incubation is achieved by incorporating glucose oxidase and catalase in the substrate to destroy serum glucose during incubation. Maltose and other dialyzable oligosaccharides are measured with the alkaline copper-neocuproine reaction. A simultaneous blank run is performed to determine reducing substances other than glucose in serum. Precision studies and correlation with a manual saccharogenic method are presented. The normal range was determined from data for 49 healthy blood donors.

A New Saccharogenic Micromethod for Measurement of Amylase Activity in Biological Fluids

1970 ◽  
Vol 16 (4) ◽  
pp. 300-304 ◽  
Author(s):  
Klaus Lorentz ◽  
Detlef Oltmanns
Keyword(s):  
Standard Deviation ◽  
Blood Donors ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Biological Fluids ◽  
Soluble Starch ◽  
Starch Digestion ◽  
Triphenyltetrazolium Chloride ◽  
Serum Amylase Activity ◽  
Apparently Healthy

Abstract To determine serum amylase activity we have quantitatively measured the glucose and maltose hydrolyzed from soluble starch by colorimetrically measuring the reduction of colorless triphenyltetrazolium chloride to a red formazan, which is dissolved in methanol. The method is suitable for use with microsamples of all biological fluids, and is specific for the final products of starch digestion. Values found for sera from 55 apparently healthy blood donors ranged from 0.15 to 1.55 (mean, 0.83; standard deviation, ±0.4) mg of glucose per ml per h, corresponding to 7.5 to 78 Somogyi units.

Effect of Cadmium Exposure on Serum Amylase Activity in Cadmium Electroplating Workers

2006 ◽  
Vol 1 (4) ◽  
pp. 260-267 ◽  
Author(s):  
R. B. Kalahasthi ◽  
Rajmohan Hirehal Raghavendra Rao ◽  
Rajan Bagalur Krishna Murthy ◽  
M. Karuna Kumar
Keyword(s):  
Serum Amylase ◽  
Amylase Activity ◽  
Cadmium Exposure ◽  
Serum Amylase Activity

Amylase, lipase, pancreatic isoamylase, and phospholipase A in diagnosis of acute pancreatitis

1995 ◽  
Vol 41 (8) ◽  
pp. 1129-1134 ◽  
Author(s):  
P Clavé ◽  
S Guillaumes ◽  
I Blanco ◽  
N Nabau ◽  
J Mercé ◽  
...  
Keyword(s):  
Acute Pancreatitis ◽  
Operating Characteristic ◽  
Serum Amylase ◽  
Acute Abdominal Pain ◽  
Characteristic Curve ◽  
Threshold Value ◽  
Phospholipase A ◽  
Diagnostic Efficiency ◽  
Pancreatic Isoamylase ◽  
Parallel Fashion

Abstract To determine the utility of serum amylase (AMY), lipase (Lp), pancreatic isoamylase (isoA), phospholipase A (PLA), and urine AMY in the diagnosis of acute pancreatitis, samples of serum and urine were obtained on admission and every day thereafter for 5 days from 384 patients with acute abdominal pain. Diagnostic accuracy, determined as the area under the receiver operating characteristic curve, was > 0.975 for serum AMY, Lp, isoA, and urine AMY. For each of these enzymes, a threshold value (twice to sixfold the upper limit of the reference values) offering diagnostic efficiency > 95% could be determined. In contrast, accuracy and efficiency of serum PLA were low. The profiles of these enzymes in acute pancreatitis decreased in a parallel fashion over 5 days except for PLA. We conclude that diagnostic utilities are similar for serum AMY, Lp, isoA, and urine AMY for acute pancreatitis, provided that an appropriate threshold is established.

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