A new test for the diagnosis of exocrine pancreatic insufficiency in the dog

Batt, R. M.; Bush, B. M.; Peters, T J

doi:10.1111/j.1748-5827.1979.tb07029.x

Cited by 24 publications

(7 citation statements)

References 9 publications

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“…An accurate diagnosis can be made by the assay of pancreatic enzymes in the lumen of the proximal small intestine. In order to avoid duodenal intubation this has been achieved in viva for chymotrypsin by the oral administration of a synthetic peptide (Freudiger & Bigler, 1977;Batt, Bush & Peters, 1979b). Small intestinal damage can also result in the malabsorption of many nutrients (Table 1).…”

Section: Discussionmentioning

confidence: 99%

The molecular basis of malabsorption

Batt¹

1980

J of Small Animal Practice

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Section: Discussionmentioning

confidence: 99%

The molecular basis of malabsorption

Batt¹

1980

J of Small Animal Practice

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“…The diagnosis was confirmed by the oral administration of N-benzoyl-L-tyrosyl-p-aminobenzoic acid, a substrate specific for chymotrypsin, and the subsequent estimation of plasma and urine p-aminobenzoic acid (PABA) (Batt et al, 1979b). The results (Table 1) show that at two hours normal animals achieve a plasma PABA concentration approximately 10 times greater than that of the animals with pancreatic insufficiency.…”

Section: Groups Of Animalsmentioning

confidence: 92%

“…The clinical details and results of the screening tests (Batt et al, 1979b) are shown in Table 1. The diagnosis was confirmed by the oral administration of N-benzoyl-L-tyrosyl-p-aminobenzoic acid, a substrate specific for chymotrypsin, and the subsequent estimation of plasma and urine p-aminobenzoic acid (PABA) (Batt et al, 1979b).…”

Section: Groups Of Animalsmentioning

confidence: 99%

Biochemical changes in the jejunal mucosa of dogs with naturally occurring exocrine pancreatic insufficiency

Batt¹,

Bush²

1979

Gut

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SUMMARY The roles of extracellular and intracellular mechanisms in the degradation of brush border proteins have been investigated by studying the small intestinal mucosa of dogs with naturally occurring exocrine pancreatic insufficiency. Peroral jejunal biopsies were homogenised and the organelles separated by isopycnic centrifugation on continuous sucrose density gradients. The distributions of marker enzymes for the principal subcellular organelles were determined in the gradients and related to the specific activities in the homogenates. There were increased activities of the brush border carbohydrases zinc-resistant x-glucosidase, maltase and sucrase in the pancreatic insufficient animals, but no change in lactase activity. The activity of y-glutamyl transferase was also higher in the affected group; the activities of two other brush border enzymes, alkaline phosphatase and leucyl-3-naphthylamidase, however, were unaltered. These findings with an increase in the modal density of the brush border from 1 20 to 1'22 are consistent with an enhanced glycoprotein content of the microvillus membrane. There were also rises in the activities of lysosomal enzymes. N-Acetyl-3-glucosaminidase activity was increased in the soluble fractions and the percentage latent enzyme activity was reduced, findings indicative of an increased fragility of the lysosomal membrane. There were no marked alterations in the activities or density gradient distributions of marker enzymes for the other organelles, stressing the specificity of the changes in the brush borders and lysosomes. These findings are compatible with the degradation of certain exposed brush border proteins by pancreatic proteases and suggest that when this is defective, intracellular degradative mechanisms may be stimulated.The enterocyte is a highly specialised cell involved in the terminal processing of nutrients and their transference from the lumen of the small intestine. Although the life span of this cell is relatively short, the protein content of the enterocyte is not static, proteins turning over at heterogeneous rates by a continuous process of synthesis and degradation (Alpers and Kinzie, 1973). A balance between these processes maintains the steady state level of individual proteins. Free ribosomes are responsible for the synthesis of intracellular proteins, whereas those destined for export or insertion into membranes are synthesised on the rough endoplasmic reticulum (Dallner et al., 1966).

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“…Bacterial proteolytic activity may 0022-45 10/84/1200-0707%02.00 0 1984 BSAVA 707 add a further complication by falsely elevating the results in dogs with EPI. The oral N-benzoyl-L-tyrosyl-P-aminobenzoic acid test has helped to overcome these difficulties (Freudiger & Bigler, 1977;Strombeck, 1978;Batt, Bush & Peters, 1979;Rogers et al, 1980;Batt & Mann, 1981), however, practical constraints are likely to limit the widespread application of this procedure. As an alternative approach a radioimmunoassay has been developed for the accurate detection of EPI by the analysis of a single blood sample (Williams & Batt, 1983).…”

Section: Introductionmentioning

confidence: 99%