scholarly journals The Agreement between Feline Pancreatic Lipase Immunoreactivity and DGGR-Lipase Assay in Cats—Preliminary Results

Animals ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 3172
Author(s):  
Magdalena Maria Krasztel ◽  
Michał Czopowicz ◽  
Olga Szaluś-Jordanow ◽  
Agata Moroz ◽  
Marcin Mickiewicz ◽  
...  
Keyword(s):  
Blood Sample ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Prospective Studies ◽  
Gold Standard ◽  
Glutaric Acid ◽  
Preliminary Results

The colorimetric catalytic assay based on the use of 1,2-o-dilauryl-rac-glycero-3-glutaric acid-(6′-methylresorufin) (DGGR) ester as a substrate for pancreatic lipase activity is commonly used for the diagnosis of pancreatitis in dogs and cats. Even though the assay has generally been shown to yield consistent results with feline pancreatic lipase immunoreactivity (fPLI) assay, the agreement may vary between assays of different manufacturers. In this study, the chance-corrected agreement between a DGGR-lipase assay offered by one of the biggest providers of diagnostic solutions in Poland and fPLI assay was investigated. The study was carried out on 50 cats in which DGGR-lipase activity and fPLI were tested in the same blood sample. The chance-corrected agreement was determined using Gwet’s AC1 coefficient separately for the fPLI assay’s cut-off values of >3.5 μg/L and >5.3 μg/L. The DGGR-lipase activity significantly positively correlated with fPLI (Rs = 0.665; CI 95%: 0.451, 0.807, p < 0.001). The chance-corrected agreement between the fPLI assay and DGGR-lipase assay differed considerably depending on the cut-off values of the DGGR-lipase assay. When the cut-off value reported in the literature (>26 U/L) was used, it was poor to fair. It was moderate at the cut-off value recommended by the laboratory (>45 U/L), and good at the cut-off value recommended by the assay’s manufacturer (>60 U/L). The highest agreement was obtained between the fPLI assay at the cut-off value of 3.5 μg/L and the DGGR-lipase assay at the cut-off value of 55 U/L (AC1 = 0.725; CI 95%: 0.537, 0.914) and between the fPLI assay at the cut-off value of 5.3 μg/L and the DGGR-lipase assay at the cut-off value of 70 U/L (AC1 = 0.749; CI 95%: 0.577, 0.921). The study confirms that the chance-corrected agreement between the two assays is good. Prospective studies comparing both assays to a diagnostic gold standard are needed to determine which of them is more accurate.

Evaluation of 1,2-O-dilauryl-rac-glycero glutaric acid-(6′-methylresorufin) ester (DGGR) and 1,2-diglyceride lipase assays in dogs with naturally occurring hypercortisolism

2021 ◽  
pp. 104063872110213
Author(s):  
Guido Linari ◽  
Francesco Dondi ◽  
Sofia Segatore ◽  
Kateryna Vasylyeva ◽  
Nikolina Linta ◽  
...  
Keyword(s):  
Acute Pancreatitis ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Glutaric Acid ◽  
Clinical Signs ◽  
The Other ◽  
Naturally Occurring ◽  
Specific Serum ◽  
Serum Test ◽  
Healthy Dogs

1,2-O-dilauryl-rac-glycero glutaric acid-(6′-methylresorufin) ester (DGGR) lipase activity has been proposed as a faster and less expensive test used in the diagnosis of acute pancreatitis (AP) compared to canine pancreatic lipase immunoreactivity (cPLI), which is considered the most sensitive and specific serum test available for dogs. Elevations in lipase activity have been observed in dogs with naturally occurring hypercortisolism (HC) and in those treated with exogenous steroids, which complicates the diagnosis of AP in dogs with HC. We compared lipase activity measured by DGGR and 1,2-diglyceride (1,2-DiG) assays in 22 dogs with HC, 22 with AP, and 22 healthy dogs. The dogs with HC had no clinical signs or ultrasonographic findings consistent with AP. DGGR lipase activity was elevated in 64% and 73% of the dogs with HC and AP, respectively, and in 18% of healthy dogs. 1,2-DiG lipase activity was high in 23% and 36% of the dogs with HC and AP, respectively, and in 5% of the healthy dogs. Both DGGR and 1,2-DiG lipase activities were significantly different between the healthy dogs and the other 2 groups, whereas no differences were detected between the dogs with HC and those with AP. Our results support a lack of specificity for both DGGR and 1,2-DiG lipase activity assays in aiding the diagnosis of AP in dogs with HC.

scholarly journals Increased canine pancreatic lipase immunoreactivity (cPLI) and 1,2-o-dilauryl-rac-glycero-3-glutaric acid-(6′-methylresorufin) ester (DGGR) lipase in dogs with evidence of portal hypertension and normal pancreatic histology: a pilot study

2021 ◽  
pp. 104063872110039
Author(s):  
Gonçalo Serrano ◽  
Dominique Paepe ◽  
Tim Williams ◽  
Penny Watson
Keyword(s):  
Portal Hypertension ◽  
Liver Disease ◽  
Pilot Study ◽  
Pancreatic Lipase ◽  
Glutaric Acid ◽  
Inclusion Criteria ◽  
Reference Limit ◽  
Clinical Presentations ◽  
Upper Reference Limit

The clinical presentations of both liver disease and pancreatitis are nonspecific and overlapping, which may cause difficulty in diagnosis. In our retrospective pilot study, we assessed whether dogs with evidence of portal hypertension and absence of pancreatitis on pancreatic histology have increases in canine pancreatic lipase immunoreactivity (cPLI) and 1,2-o-dilauryl-rac-glycero-3-glutaric acid-(6′-methylresorufin) ester (DGGR) lipase. We included dogs that had been presented between 2008 and 2019 if they had normal pancreatic histology, histologically confirmed hepatopathy, and if canine pancreas-specific lipase (Spec cPL; Idexx) or DGGR lipase had been measured. Only dogs with portal hypertension were included. Six dogs fulfilled the inclusion criteria. Four of 6 and 2 of 6 dogs had Spec cPL and DGGR lipase exceeding the upper reference limit, respectively. From the 4 dogs with increased Spec cPL, 2 had concentrations of 200–400 µg/L and 2 had concentrations ≥ 400 µg/L. Our results suggest that canine portal hypertension might lead to increased Spec cPL and DGGR lipase values in the absence of pancreatitis on histology. Until more evidence in a larger number of dogs with portal hypertension is available, both tests should be interpreted cautiously in the presence of portal hypertension.

scholarly journals Modification of a phospholipid stabilized emulsion interface by bile salt: effect on pancreatic lipase activity

1998 ◽  
Vol 39 (3) ◽  
pp. 623-632 ◽  
Author(s):  
Martin Wickham ◽  
Martin Garrood ◽  
John Leney ◽  
Peter D.G. Wilson ◽  
Annette Fillery-Travis
Keyword(s):  
Bile Salt ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Salt Effect

scholarly journals Studies on the detergent inhibition of pancreatic lipase activity.

1983 ◽  
Vol 24 (10) ◽  
pp. 1336-1342
Author(s):  
Y Gargouri ◽  
R Julien ◽  
A G Bois ◽  
R Verger ◽  
L Sarda
Keyword(s):  
Pancreatic Lipase ◽  
Lipase Activity

scholarly journals Kinetic studies on pancreatic lipase activity in micellar systems. II. Effect of fatty acid chain length of substrates.

1983 ◽  
Vol 31 (12) ◽  
pp. 4213-4219 ◽  
Author(s):  
HIROSHI NAKAHARA ◽  
SATOSHI OKADA ◽  
KENSHU MOCHIDA ◽  
HIDENOBU OHMORI ◽  
MASAICHIRO MASU
Keyword(s):  
Fatty Acid ◽  
Chain Length ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Kinetic Studies ◽  
Fatty Acid Chain Length ◽  
Fatty Acid Chain ◽  
Micellar Systems

scholarly journals Physiological parameters governing the action of pancreatic lipase

2010 ◽  
Vol 23 (1) ◽  
pp. 146-154 ◽  
Author(s):  
Iain A. Brownlee ◽  
Deborah J. Forster ◽  
Matthew D. Wilcox ◽  
Peter W. Dettmar ◽  
Chris J. Seal ◽  
...  
Keyword(s):  
Weight Management ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Dietary Lipid ◽  
Ion Concentration ◽  
Lipid Absorption ◽  
Energy Yield ◽  
Body Of Knowledge ◽  
Lipid Ester ◽  
Duodenal Lumen

The most widely used pharmacological therapies for obesity and weight management are based on inhibition of gastrointestinal lipases, resulting in a reduced energy yield of ingested foods by reducing dietary lipid absorption. Colipase-dependent pancreatic lipase is believed to be the major gastrointestinal enzyme involved in catalysis of lipid ester bonds. There is scant literature on the action of pancreatic lipase under the range of physiological conditions that occur within the human small intestine, and the literature that does exist is often contradictory. Due to the importance of pancreatic lipase activity to nutrition and weight management, the present review aims to assess the current body of knowledge with regards to the physiology behind the action of this unique gastrointestinal enzyme system. Existing data would suggest that pancreatic lipase activity is affected by intestinal pH, the presence of colipase and bile salts, but not by the physiological range of Ca ion concentration (as is commonly assumed). The control of secretion of pancreatic lipase and its associated factors appears to be driven by gastrointestinal luminal content, particularly the presence of acid or digested proteins and fats in the duodenal lumen. Secretion of colipase, bile acids and pancreatic lipase is driven by cholecystokinin and secretin release.

scholarly journals Prognostic value of canine pancreatic lipase immunoreactivity and lipase activity in dogs with gastric dilatation-volvulus

PLoS ONE ◽  
2018 ◽  
Vol 13 (9) ◽  
pp. e0204216 ◽  
Author(s):  
Giuseppe Spinella ◽  
Francesco Dondi ◽  
Lisa Grassato ◽  
Luca Magna ◽  
Veronica Cola ◽  
...  
Keyword(s):  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Prognostic Value ◽  
Gastric Dilatation

Evaluation of lipase activity in serum by radial enzyme diffusion.

1976 ◽  
Vol 22 (5) ◽  
pp. 633-637 ◽  
Author(s):  
J M Goldberg ◽  
P Pagast
Keyword(s):  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Reference Method ◽  
Pancreatic Disease ◽  
Serum Lipase ◽  
Normal Limits ◽  
Diffusion Assay

Abstract Results of determination of serum lipase by radial enzyme diffusion correlate well with those by a titrimetric reference method in the abnormal range. The specificity of the diffusion assay allows the differentiation of patients with pancreatic disease, even when the lipase activity of the serum is within the normal limits of the tritrimetric assay. Pancreatic lipase is not detectable by the diffusion assay in the serum of individuals who are free from pancreatic disease.

scholarly journals Caffeic Acid Derivatives from Bacopa monniera Plants as Inhibitors of Pancreatic Lipase Activity and their Structural Requirements

2016 ◽  
Vol 11 (12) ◽  
pp. 1934578X1601101
Author(s):  
Souichi Nakashima ◽  
Tomoe Ohta ◽  
Seikou Nakamura ◽  
Yoshimi Oda ◽  
Mari Koumoto ◽  
...  
Keyword(s):  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Methanol Extract ◽  
Bacopa Monniera ◽  
Inhibitory Effects ◽  
Active Constituent ◽  
Structural Requirements ◽  
Phenylpropanoid Glycosides ◽  
First Time

The methanol extract of whole Bacopa monniera plants inhibited pancreatic lipase activity in vitro. From this extract we have reported the isolation of 11 triterpene glycosides and 5 phenylethanoid- and/or phenylpropanoid- glycosides. In this paper, we describe the effects of the methanol extract and/or its constituents on pancreatic lipase activity and the isolation of an active constituent, desrhamnosyl isoacteoside. In addition, the structural requirements for its inhibitory effects were examined. We also examined the effects on the elevation of plasma triglyceride (TG) levels in olive oil loaded mice. The major active constituents, desrhamnosyl isoacteoside and plantainoside B, reduced plasma TG levels in the mice. The inhibitory effects of B. monniera and its constituents on pancreatic lipase activity and plasma TG level are reported for the first time.

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