Regulation of proteolytic enzyme activities and mRNA concentrations in rat pancreas by food content

Giorgi, Dominique; Renaud, Wanda; Bernard, Jean‐Paul; Dagorn, Jean–Charles

doi:10.1016/s0006-291x(85)80034-6

Cited by 53 publications

(17 citation statements)

References 22 publications

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“…Twenty micrograms of insect protein was loaded in each well. et al, 1977;Schick et al, 1984;Giorgi et al, 1985;Graf and Briegel, 1989;Corring et al, 1989;Barillas-Mury et al, 1991;Lhoste et al, 1993), the insect seems to adjust its digestive proteolytic system to the diet, both quantitatively and qualitatively. As shown on gelatin-containing gels, CPB larvae use a complex set of proteinase forms present in varying amounts depending on the diet.…”

Section: Discussionmentioning

confidence: 99%

“…Previous studies carried out on mammals (Johnson et al, 1977;Schick et al, 1984;Giorgi et al, 1985;Lhoste et al, 1993) or insects (Gooding, 1973;Briegel and Lea, 1975;Noriega et al, 1994) clearly demonstrated that both the size and the nature of the diet influence the amount of specific proteolytic enzymes available for dietary protein di-*Abbreviations used: BSA, bovine serum albumin; CPB, Colorado potato beetle; E-64, transepoxysuccinyl-L-leucylamido (4-guanidino) butane; PAGE, polyacrylamide gel electrophoresis.…”

Section: Introductionmentioning

confidence: 99%

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Diet-related plasticity of the digestive proteolytic system in larvae of the Colorado potato beetle (Leptinotarsa decemlineata Say)

Overney

Fawe

Yelle

et al. 1997

Arch. Insect Biochem. Physiol.

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Quantitative and qualitative changes in digestive proteolytic activities were monitored in fourth‐instar larvae of the Colorado potato beetle (Leptinotarsa decemlineata Say) subjected to three different leaf diets. Depending on the diet, the larvae exhibited variable growth rates, similar for potato (Solanum tuberosum) and eggplant (Solanum melongena) diets but lower for the tomato (Lycopersicon esculentum) diet. Interestingly, these growth rates were not associated with total protease activity in the midgut. While growth of tomato‐fed insects was negligible, midgut protease activity in these insects was 1.5 and 4.2 times higher than that measured for potato‐ and eggplant‐fed insects, respectively. As seen on gelatin‐containing polyacrylamide gels, midgut extracts from insects that ingested eggplant leaves contained only a few proteinase forms, while numerous forms were observed in extracts of potato‐ and tomato‐fed larvae. Although several forms were common to the three diets, their relative importance in the insect midgut varied. This diet‐related plasticity of the digestive proteolytic system in Colorado potato beetle larvae leads one to question the potential for control approaches based on the inhibition of digestive proteases. Arch. Insect Biochem. Physiol. 36:241–250, 1997. © 1997 Wiley‐Liss, Inc.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Diet-related plasticity of the digestive proteolytic system in larvae of the Colorado potato beetle (Leptinotarsa decemlineata Say)

Overney

Fawe

Yelle

et al. 1997

Arch. Insect Biochem. Physiol.

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“…Similar modulations occur in the pancreas of rats whose diet is enriched in protein (Reboud et al, 1966), and CCK-PZ has been proposed as one of the effectors of pancreatic adaptation to a protein-rich diet . In previous experiments, we have demonstrated that the diet-induced changes in pancreatic enzyme production were accompanied by changes in the concentrations of the corresponding mRNAs (Giorgi et al, 1984(Giorgi et al, , 1985. The present study examined the influence of long-term treatment with CCK-PZ, caerulein and pilocarpine, acholinergic agonistwith potent secretagogue properties, on the pancreatic concentrations of mRNAs encoding amylase, trypsinogen I and chymotrypsinogen B.…”

Section: Introductionmentioning

confidence: 86%

“…Amylase was assayed as described by Noelting & Bernfeld (1948). Chymotrypsinogen and trypsinogen were activated and assayed by the method of Hummel (1959), as previously described (Giorgi et al, 1985). Quantifiction of mRNA by filter hybridization has been previously described (Giorgi et al, 1984).…”

Section: Methodsmentioning

confidence: 99%

Regulation of concentrations of mRNA for amylase, trypsinogen I and chymotrypsinogen B in rat pancreas by secretagogues

Renaud¹,

Giorgi²,

Iovanna³

et al. 1986

Biochemical Journal

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Regulation of pancreatic gene expression by the secretory stimulants cholecystokinin-pancreozymin, caerulein and pilocarpine was studied in the rat, by using cloned cDNA probes to quantify concentrations of specific mRNAs (amylase, trypsinogen I and chymotrypsinogen B). It is concluded that long-term pancreatic stimulation results in pre-translational regulation of secretory-protein gene expression, with a preferential accumulation of RNA transcripts encoding serine proteinases, compared with that for amylase.

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“…Chymotrypsinogen content and synthesis is highest with an 82% casein diet, while trypsinogen is highest with a 45% casein diet (24). However, the mRNAs coding for these proteases increase 76 DIETARY ADAPTATION, PANCREAS, AND RESERPINE 177 3.6-to 3.9-fold with a high protein diet (25). The adaptive " response of these hydrolytic enzymes to their respective substrates begins within 24 h and reaches a maximum in 5-7 days (18,(26)(27)(28)(29)(30).…”

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confidence: 99%

Effects of Reserpine Treatment on Dietary Adaptation of the Rat Exocrine Pancreas

Hazlett

Brannon

1988

Pediatr Res

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ABSTRACT. Chronic reserpine treatment (500 pg/kg) of the rat results in generalized exocrinopathy, impaired pancreatic secretion, and decreased pancreatic amylase. These characteristics are similar to those in cystic fibrosis and are the basis for use of this experimental model for cystic fibrosis. Pancreatic enzymes adapt to diet, but it is not known whether chronic reserpine treatment affects this response. Due to the malnutrition induced by this treatment, another dose of reserpine was required that would alter pancreatic function but not induce malnutrition in order to evaluate dietary adaptation. Male rats (100-120 g) were injected subcutaneously daily for 7 days with 1) no injection (control); 2) 1.0 ml/kg vehicle or sham (pair fedsham); or 3) reserpine: 500,50, or 5 pglkg. Food consumption was comparable among control and reserpine-treated (50 and 5 pg/kg) rats and significantly greater (200%) than pair fed-sham and 500 pg/kg reserpine-treated rats. Pancreatic amylase, however, was significantly lower in all reserpine-treated rats (500 pg/kg, 74%; 50 pg/kg, 56%; 5 pglkg, 52%) than in control rats. To evaluate dietary adaptation, control and reserpine-treated (5 pg/kg) rats were fed high carbohydrate, high fat or high protein diets. Both groups adapted to these diets with the greatest amylase, lipase, and trypsin activities in high carbohydrate-, high fat-, and high protein-fed rats, respectively. Reserpine-treated rats fed high carbohydrate, however, had significantly lower (64%) amylase activity than high carbohydrate-fed control rats. Although reserpine-treated rats can adapt pancreatic enzymes to diet, the adaptation of amylase to carbohydrate is impaired. (Pediatr Res 23: 176-180,1988) Abbreviations PFS, pair-fed sham C, control R500, reserpine-treated with 500 pglkg R50, reserpine-treated with 50 pg/kg R5, reserpine-treated with 5 pg/kg HC, high carbohydrate HF, high fat HP, high protein ANOVA, analysis of variance LSD, least significant difference

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Regulation of proteolytic enzyme activities and mRNA concentrations in rat pancreas by food content

Cited by 53 publications

References 22 publications

Diet-related plasticity of the digestive proteolytic system in larvae of the Colorado potato beetle (Leptinotarsa decemlineata Say)

Diet-related plasticity of the digestive proteolytic system in larvae of the Colorado potato beetle (Leptinotarsa decemlineata Say)

Regulation of concentrations of mRNA for amylase, trypsinogen I and chymotrypsinogen B in rat pancreas by secretagogues

Effects of Reserpine Treatment on Dietary Adaptation of the Rat Exocrine Pancreas

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