Increase of Trypsin Activity

1964 ◽  
pp. 246-254 ◽  
Author(s):  
Elton S. Cook ◽  
Sister M. Justa Smith
Keyword(s):  
Trypsin Activity

Digestive processes of haematophagous insects. XII. Secretion of trypsin and carboxypeptidase B by Glossina morsitans morsitans Westwood (Diptera: Glossinidae)

1977 ◽  
Vol 55 (1) ◽  
pp. 215-222 ◽  
Author(s):  
R. H. Gooding
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Content ◽  
Bovine Serum ◽  
Significant Positive Correlation ◽  
Glossina Morsitans Morsitans ◽  
Trypsin Activity ◽  
Glossina Morsitans ◽  
Carboxypeptidase B ◽  
Positive Correlation

There was a significant positive correlation between protein content and the amounts of trypsin and carboxypeptidase B (CPB) in the digestive portion of the midgut of Glossina morsitans morsitans, 24, 48, 72, and 96 h after feeding on a rabbit. CPB and trypsin activity were also positively correlated. Trypsin and CPB production were stimulated, to varying degrees, by bovine serum albumin (BSA), α-globulin, β-globulin, γ-globulin, and haemoglobin; the greatest response was to BSA. Peptides derived from BSA by trypsin cleavage also stimulated production of trypsin and CPB.

scholarly journals SPINK1-induced amelioration of impaired autophagy contributes to suppression of trypsinogen activation in a model of acute pancreatitis

2020 ◽  
Author(s):  
Yuxiao Zhao ◽  
Jianlong Jia ◽  
Abdullah Shopit ◽  
Yang Liu ◽  
Jun Wang
Keyword(s):  
Acute Pancreatitis ◽  
In Vitro Model ◽  
Autophagic Flux ◽  
Trypsin Activity ◽  
Autophagy Flux ◽  
Trypsinogen Activation ◽  
Vitro Model ◽  
First Time ◽  
Induced Amelioration

AbstractSPINK1 has been regarded as a reversible trypsinogen inhibitor for the inappropriate activation of trypsin, a key step in the initiation of acute pancreatitis (AP). However, the mechanisms of its action remains largely unclear and controversial. Here, we reported an unexpected effects of SPINK1 on inhibiting trypsinogen activation through the regulation of impaired autophagy in cerulein-stimulated AR42J cells, a well-established in vitro model of acute pancreatitis. Firstly, we found that the impaired autophagic flux was induced and trypsinogen activity enhanced in the above setting. Then, we showed that SPINK1 overexpression could inhibit the level of increased autophagic activity, improving the hindered autophagy flux, and significantly decreased the trypsinogen activity, whereas shRNA-caused downregulation of SPINK1 exacerbated the impairment of autophagic flux and trypsin activity, in the same cerulein-processed cells. More importantly, the trypsinogen activation in this model could be ameliorated by 3-Methyladenine(3-MA), an autophagy inhibitor. Thus, this study revealed, possibly for the first time, that SPINK1 greatly blocked the trypsinogen activation possibly through the modulation of impaired autophagy in cerulein-induced in vitro model of acute pancreatitis.

Anterior midgut proteinase inhibitor from Glossina morsitans morsitans Westwood (Diptera: Glossinidae) and its effects upon tsetse digestive enzymes

1980 ◽  
Vol 58 (1) ◽  
pp. 79-87 ◽  
Author(s):  
Jon G. Houseman
Keyword(s):  
Proteinase Inhibitor ◽  
Periplaneta Americana ◽  
Specific Activity ◽  
Glossina Morsitans Morsitans ◽  
Tsetse Flies ◽  
Trypsin Activity ◽  
Glossina Morsitans ◽  
Trypsin Hydrolysis ◽  
Hydrolysis Of ◽  
Anterior Midgut

The anterior midgut of Glossina morsitans morsitans Westwood contains a proteinase inhibitor, molecular weight 5000 ± 2000daltons, stable to 1 M HCl, heat, and dialysis, but unstable to 1% trichloroacetic acid. Inhibitor activity is not associated with anticoagulant in the anterior midgut. The specific activity of the proteinase inhibitor is similar in mated and unmated females and greater than in male tsetse flies. Proteinase inhibitor inhibits proteinase VI and trypsin hydrolysis of N-benzoyl-L-arginine ethyl ester (BAEE) and benzoyl-DL-arginine-p-nitroanilide (BAPNA) but has no effect on proteinase VI hydrolysis of haemoglobin. Inhibition of trypsin hydrolysis of haemoglobin is noncompetitive. Proteinase inhibitor levels in the anterior midgut decreased immediately after feeding and then increased, reaching a maximum 60–100 h after ingestion of the bloodmeal. Postteneral flies contained higher levels of proteinase inhibitor than teneral individuals. Trypsin activity in gut homogenates of Phormia regina and Aedes aegypti was inhibited by the tsetse inhibitor. There was no detectable inhibition of bovine or Pterostichus adstrictus trypsin activity. Inhibition of Periplaneta americana trypsin occurred but was less than fly trypsin inhibition. The possible role of the inhibitor in terminating proteinase production is discussed.

Low-molecular-weight proteinase inhibitor of human epidermis inhibiting papain and trypsin activity

1986 ◽  
Vol 278 (3) ◽  
pp. 194-198 ◽  
Author(s):  
I. Takiuchi ◽  
H. Takagi ◽  
H. Goi ◽  
M. Kawamura ◽  
D. Higuchi
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Human Epidermis ◽  
Low Molecular Weight ◽  
Trypsin Activity

Toxic effect of melanoidins from glucose–asparagine on trypsin activity

2009 ◽  
Vol 47 (8) ◽  
pp. 2071-2075 ◽  
Author(s):  
Albert Ibarz ◽  
Alfonso Garvín ◽  
Salvador Garza ◽  
Jordi Pagán
Keyword(s):  
Toxic Effect ◽  
Trypsin Activity

scholarly journals Effect of extruded full-fat soybeans on performance, amino acids digestibility, trypsin activity, and intestinal morphology in broilers

2013 ◽  
Vol 58 (No. 10) ◽  
pp. 470-478 ◽  
Author(s):  
M. Foltyn ◽  
V. Rada ◽  
M. Lichovníková ◽  
I. Šafařík ◽  
A. Lohniský ◽  
...  
Keyword(s):  
Amino Acids ◽  
Body Weight ◽  
Growth Performance ◽  
Intestinal Morphology ◽  
Trypsin Activity ◽  
Villus Height ◽  
Isoleucine Leucine ◽  
Final Body Weight ◽  
Dietary Treatments ◽  
Different Levels

The influence of different levels of extruded full-fat soybean (EFFSB) in the diet on growth performance, apparent ileal amino acids digestibility (AIAAD), intestinal morphology, and trypsin activity in digesta of broilers was determined. In the first experiment, two-hundred sixty ROSS 308 male chickens were used to investigate the effect of EFFSB on growth performance, intestinal morphology, and trypsin activity in the digesta and AIAAD. Five dietary treatments were used, containing 0, 40, 80, 120, and 160 g/kg of EFFSB. The experiment lasted from day 10 till day 38 of age. The inclusion of EFFSB at the level of 160 g/kg in the diet significantly (P < 0.05) decreased final body weight (2443 g in 0 group vs. 2093 in 160 group) and worsened feed efficiency. AIAAD was lower when diet contained more than 40 g/kg EFFSB. But at the level of 160 g/kg AIAAD increased in several amino acids (threonine, isoleucine, leucine, histidine). Trypsin activity increased with increasing EFFSB in the diets. There were no significant (P > 0.05) differences in AIAAD between groups 80, 120, and 160. Villus height (groups 0: 966.2; 4: 852.1; 8: 792.6; 12: 836.3; 16: 926.7 µm) and crypt depth (groups 0: 160.1; 4: 134.8; 8: 122.9; 12: 129.5; 16: 134.6 µm) of ileum decreased with inclusion of EFFSB in the diet, but villi/crypt ratio increased. In the second experiment, male chickens ROSS 308 were divided into 4 groups with 2 replicates per 100 chicks each. The groups were fed 0, 40, 80, and 120 g/kg of EFFSB. The experiment lasted from day 10 till day 38 of age. Final body weight (2594 g in 0 group vs. 2624 g in 120 group) was not significantly (P > 0.05) affected by the diet. The study showed that EFFSB at the level of 120 g/kg in grower broiler diet had no adverse effect on performance.  

Effects of a high-protein, low-carbohydrate diet on degradation of sucrase-isomaltase in rat jejunoileum

1988 ◽  
Vol 254 (6) ◽  
pp. G907-G912 ◽  
Author(s):  
T. Goda ◽  
F. Raul ◽  
F. Gosse ◽  
O. Koldovsky
Keyword(s):  
Active Site ◽  
Degradation Product ◽  
High Protein ◽  
Standard Diet ◽  
Trypsin Activity ◽  
Sucrase Activity ◽  
Carbohydrate Diet ◽  
Low Carbohydrate Diet ◽  
Entire Height ◽  
Low Carbohydrate

During the degradation of intestinal sucrase-isomaltase by pancreatic proteinases, degradation of sucrase-active site precedes that of the isomaltase-active site in rats. In the present paper, we demonstrate that the extent of degradation of sucrase-isomaltase is altered by dietary manipulation in vivo. Adult rats were starved for 24 h and received either a standard diet (20 cal% protein, 55% carbohydrate) or an isocaloric high-protein, low-carbohydrate diet (70 cal% protein, 5% carbohydrate). Animals were killed 15 h after the refeeding. In rats fed a high-protein, low-carbohydrate diet, luminal trypsin activity was three times higher than controls, and sucrase activity in proximal ileum was significantly lower (P less than 0.001) than controls, whereas isomaltase activity was similar in both groups. In proximal jejunum, luminal trypsin activity was remarkably lower (P less than 0.01) than in proximal ileum in both groups; sucrase and isomaltase activity was similar in both groups. Crossed immunoelectrophoresis demonstrated that a degradation product of sucrase-isomaltase, i.e., isomaltase monomer, was present in a larger amount in rats fed a high-protein, low-carbohydrate diet. In rats with bypassed pancreatic ducts, the amount of this degradation product was decreased and effect of a high-protein, low-carbohydrate diet was abolished. Experiments with a sequential isolation of epithelial cells of proximal ileum revealed that sucrase activity was decreased along the entire height of the villus in animals fed a high-protein, low-carbohydrate diet.(ABSTRACT TRUNCATED AT 250 WORDS)

Trypsin activity

1994 ◽  
Vol 39 (12) ◽  
pp. 2634-2638 ◽  
Author(s):  
Olivier Le Moine ◽  
Jeanne-Marie Devaster ◽  
Jacques Devière ◽  
Philippe Thiry ◽  
Michel Cremer ◽  
...  
Keyword(s):  
Trypsin Activity
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