title: Effect of heat-stable and heat-labile enterotoxins of Escherichia coli on intestinal brush border membrane enzymes of mice.
abstract: The activities of intestinal brush border membrane (BBM) enzymes alkaline phosphatase, maltase, lactase, sucrase, gamma-glutamyl transpeptidase and leucine aminopeptidase were determined in intestinal homogenates and purified BBMs from control, heat-stable and heat-labile enterotoxin treated mice. The activities of all the enzymes except lactase were decreased significantly (p less than 0.01) in homogenates while increased significantly (p less than 0.001) in BBMs of experimental groups as compared to controls. Calmodulin activities were increased significantly (p less than 0.01) as compared to control in heat-stable enterotoxin treated mice but remained unaltered in heat-labile enterotoxin treated mice. DNA contents of intestinal homogenates were decreased in experimental groups demonstrating the decrease in cell number in these groups. The altered BBM enzyme activities could not be attributed to changes in calmodulin activities. The increase in enzyme activities in BBMs may reflect a compensatory phenomenon in the remaining cells.
authors.affiliation: Department of Pediatrics, Postgraduate Institute of Medical Education and Research, Chandigarh, India.
authors.forename: M
authors.initials: M
authors.lastname: Kohli
authors.forename: N K
authors.initials: NK
authors.lastname: Ganguly
authors.forename: U C
authors.initials: UC
authors.lastname: Garg
authors.forename: J
authors.initials: J
authors.lastname: Goyal
authors.forename: S
authors.initials: S
authors.lastname: Majumdar
authors.forename: B N
authors.initials: BN
authors.lastname: Walia
mesh_terms: D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism; D000818:Animals; D001427:Bacterial Toxins / Q000494:pharmacology*; D002147:Calmodulin / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D004768:Enterotoxins / Q000494:pharmacology*; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D065089:Glycoside Hydrolase Inhibitors; D007422:Intestines / Q000201:enzymology* / Q000648:ultrastructure; D007931:Leucyl Aminopeptidase / Q000037:antagonists & inhibitors / Q000378:metabolism; D051379:Mice; D008871:Microvilli / Q000201:enzymology*; D013393:Sucrase / Q000037:antagonists & inhibitors / Q000378:metabolism; D000520:alpha-Glucosidases / Q000378:metabolism; D001616:beta-Galactosidase / Q000037:antagonists & inhibitors / Q000378:metabolism; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors / Q000378:metabolism
chemical_list: D001427:Bacterial Toxins; D002147:Calmodulin; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D065089:Glycoside Hydrolase Inhibitors; C034151:heat stable toxin (E coli); D004247:DNA; C027538:heat-labile enterotoxin, E coli; D005723:gamma-Glutamyltransferase; D000469:Alkaline Phosphatase; D000520:alpha-Glucosidases; D001616:beta-Galactosidase; D013393:Sucrase; D007931:Leucyl Aminopeptidase