Inhibitory effects of estrogens on digestive enzymes, insulin deficiency, and pancreas toxicity in diabetic rats

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Diabetes mellitus, with its attendant disorders and dysfunctional behaviors, constitutes a growing concern to the population of the world. With this concern in mind, the present study investigated the anti-diabetic and hypolipedimic potential of 17â-estradiol (called E2), particularly in terms of its inhibitory effects on maltase, sucrase, lactase, and lipase activities in the intestine of surviving diabetic rats. The findings revealed that this supplement helped protect the â cells of the rats from death and damage. Interestingly, E2 induced considerable decreases of 29%, 46%, 42%, and 84% in the activities of intestinal maltase, lactase, sucrase, and lipase, respectively. The E2 extract also decreased the glucose, triglyceride, and total cholesterol rates in the plasma of diabetic rats by 39%, 27%, and 53%, respectively, and increased the HDL–cholesterol level by 74%, which helped maintain the homeostasis of blood lipid. When compared to those of the untreated diabetic rats, the superoxide dismutase, catalase, and glutathione peroxidase levels in the pancreas of the rats treated with this supplement were also enhanced by 330%, 170%, and 301%, respectively. A significant decrease was also observed in the lipid peroxidation level and lactate dehydrogenase activity in the pancreas of diabetic rats after E2 administration. Overall, the findings presented in this study demonstrate that E2 has both a promising potential with regard to the inhibition of intestinal maltase, sucrase, lactase, and lipase activities, and a valuable hypoglycemic and hypolipidemic function, which make it a potential strong candidate for industrial application as apharmacological agent for the treatment and prevention of hyperlipidemia, obesity, and cardiovascular diseases (AU)

Inhibitory effects of estrogens on digestive enzymes, insulin deficiency, and pancreas toxicity in diabetic rats.

Diabetes mellitus, with its attendant disorders and dysfunctional behaviors, constitutes a growing concern to the population of the world. With this concern in mind, the present study investigated the anti-diabetic and hypolipedimic potential of 17ß-estradiol (called E2), particularly in terms of its inhibitory effects on maltase, sucrase, lactase, and lipase activities in the intestine of surviving diabetic rats. The findings revealed that this supplement helped protect the ß cells of the rats from death and damage. Interestingly, E2 induced considerable decreases of 29%, 46%, 42%, and 84% in the activities of intestinal maltase, lactase, sucrase, and lipase, respectively. The E2 extract also decreased the glucose, triglyceride, and total cholesterol rates in the plasma of diabetic rats by 39%, 27%, and 53%, respectively, and increased the HDL-cholesterol level by 74%, which helped maintain the homeostasis of blood lipid. When compared to those of the untreated diabetic rats, the superoxide dismutase, catalase, and glutathione peroxidase levels in the pancreas of the rats treated with this supplement were also enhanced by 330%, 170%, and 301%, respectively. A significant decrease was also observed in the lipid peroxidation level and lactate dehydrogenase activity in the pancreas of diabetic rats after E2 administration. Overall, the findings presented in this study demonstrate that E2 has both a promising potential with regard to the inhibition of intestinal maltase, sucrase, lactase, and lipase activities, and a valuable hypoglycemic and hypolipidemic function, which make it a potential strong candidate for industrial application as apharmacological agent for the treatment and prevention of hyperlipidemia, obesity, and cardiovascular diseases.

Purification and characterization of a thermostable keratinolytic serine alkaline proteinase from Streptomyces sp. strain AB1 with high stability in organic solvents.

A keratinolytic alkaline proteinase (KERAB) was isolated from Streptomyces sp. strain AB1. Based on MALDI-TOF mass spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 29850.17Da. The NH(2)-terminal sequence of the enzyme was determined to be TQANPPSWGLDDIDQTAL. This keratinase was completely inhibited by phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DIFP), which suggests that it belongs to the serine protease family. Using keratin azure as a substrate, the optimum pH and temperature values for keratinase activity were pH 11.5 and 75 degrees C, respectively. This keratinase was stable between 30 and 60 degrees C and pH 4 and 11 for 4 and 96 h, respectively, and thermoactivity and thermostability were enhanced in the presence of 5 mM Mg(2+). Its catalytic efficiency was higher than those of SAPB-L31I/T33S/N99Y, nattokinase and subtilisin Carlsberg. KERAB exhibited stability to detergents and high resistance against organic solvents and was able to degrade feathers completely. These properties make KERAB a potential candidate for future applications in detergent formulations, dehairing during leather processing, and non-aqueous peptide biocatalysis.