Objective—To determine cellular immunolocalization
of canine gastric lipase (cGL) and canine pancreatic
lipase (cPL) in various tissues obtained from clinically
Sample Population—Samples of 38 tissues collected
from 2 climically healthy dogs.
Procedures—The cGL and cPL were purified from gastric
and pancreatic tissue, respectively, obtained from
dogs. Antisera against both proteins were developed,
using rabbits, and polyclonal antibodies were purified by
use of affinity chromatography. Various tissues were collected
from 2 healthy dogs. Primary antibodies were
used to evaluate histologic specificity. Replicate sections
from the collected tissues were immunolabeled for cGL
and cPL and examined by use of light microscopy.
Results—Mucous neck cells and mucous pit cells
of gastric glands had positive labeling for cGL,
whereas other tissues did not immunoreact with
cGL. Pancreatic acinar cells had positive labeling for
cPL, whereas other tissues did not immunoreact
Conclusions and Clinical Relevance—We concluded
that cGL and cPL are exclusively expressed in gastric
glands and pancreatic acinar cells, respectively. Also,
evidence for cross-immunoreactivity with other lipases
or related proteins expressed by other tissues was not
found for either protein. Analysis of these data suggests
that gastric lipase is a specific marker for gastric
glands and that pancreatic lipase is a specific marker
for pancreatic acinar cells. These markers may have
clinical use in the diagnosis of gastric and exocrine
pancreatic disorders, respectively. (Am J Vet Res
(1) Determine if a relationship exists between ionized calcium (iCa) and pancreatic lipase (cPLI) concentration in dogs, and (2) assess for correlation between resolving hypercalcemia and cPLI concentrations in dogs after treatment for primary hyperparathyroidism (PHPT).
Phase I, 44 residual serum samples (collected April 2023) from client-owned dogs with a clinical indication for cPLI quantification. Phase II, 24 residual serum samples (collected August 2022 through February 2023) from client-owned dogs with PHPT pre- and postcorrection of hypercalcemia.
Serum cPLI and iCa concentrations were measured via the Spec cPL assay and a spectrophotometric method respectively. Spearman’s rank correlation coefficients were used to investigate if there was a correlation between serum calcium and cPLI concentrations. A paired t-test was used to investigate the effect of the resolution of hypercalcemia on serum cPLI concentrations.
Phase I, serum cPLI concentrations were negatively correlated with serum iCa concentrations (r = −.429, 95% CI [−.64, −.14], P = .005) in dogs with a clinical indication for cPLI quantification. Phase II, median serum cPLI concentrations were higher before (median: 228.5 μg/L, IQR: 351.3 μg/L) than after (median: 141.0 μg/L, interquartile ranges (IQR): 279.5 μg/L) management of hypercalcemia (PHPT model). However, the decrease in cPLI concentration was not statistically significant (P = .70).
Calcium depletion may result in an inverse relationship between serum cPLI and iCa concentrations in dogs with a clinical indication for cPLI quantification. Hypercalcemia may be associated with an above reference interval cPLI concentration in some dogs.
not amenable to complete resection; however, a biopsy sample (approx 1 X 1 X 1 cm) was obtained.
Histopathologic diagnosis of the mass was pancreaticacinarcell cystadenoma. Because resection was not a viable option, ongoing patient monitoring every
AP at hospital admission (ie, > 400 µg/L). Serum concentrations of cPL may not have any relation to the magnitude of either pancreatic impairment or AUS findings because serum cPL concentration only reflects pancreaticacinarcell injury. 12 In
Immunohistochemistry has demonstrated that pancreatic lipase is found exclusively in zymogen granules of pancreaticacinarcells and is thus pancreatic specific. 24 Pancreatic lipase and its cofactor, colipase, together with other pancreatic
. Clinical procedures . In: Biology and medicine of rabbits and rodents . 5th ed. Ames, Iowa : Wiley-Blackwell , 2007 ; 128 – 129 .
2. Sigler RE Gough AW Iglesia FA . Pancreaticacinarcell neoplasia in male Wistar rats following 2 years of
dogs and cats, including PAA, CP, pancreatic duct obstruction, and pancreatic neoplasia. In dogs, PAA is considered the most common cause of EPI. PAA is characterized by selective destruction of pancreaticacinarcells and their replacement with adipose
reliable indicator of disease severity. 4 , 13 , 25 , 26 Pancreatic lipase is released into the systemic circulation within minutes of damage to pancreaticacinarcells but has a short half-life (approx 2 hours). 27 If the trigger for pancreatic
The human SPINK1 gene encodes for a protein with a molecular mass of 6.5 kDa. This protein, pancreatic secretory typsin inhibitor, is produced, stored, and secreted by pancreaticacinarcells. 1 The gene has a length of approximately 7
catalytic assays, such as those used to measure lipase activity in serum.
Recently, a new assay for measurement of PLI was developed and validated. 9 An immunolocalization study 10 revealed that only pancreaticacinarcells stain for pancreatic lipase