Intestinal enzyme profiles in normal and rotavirus-infected mice.
To investigate further the pathophysiology of rotavirus-induced diarrhea, changes in specific activities of eight relevant intestinal enzymes [alkaline phosphatase, thymidine kinase, lactase, maltase, sucrase, Na+,K+-adenosine triphosphatase (ATPase), adenylate and guanylate cyclases] were measured following infection of suckling mice with murine rotavirus (epizootic diarrhea of infant mouse strain) and compared with age-matched control mice. The concentration of lactose within the lumen of the gastrointestinal tract during infection was also measured. During the course of infection, activities of alkaline phosphatase and lactase decreased, whilst the activity of thymidine kinase increased. Precocious maturation profiles of sucrase and maltase enzymes were observed. No significant changes were detected in the activities of Na+,K+-ATPase or the adenylate and guanylate cyclases. These results are discussed in relation to existing and novel hypotheses on the pathogenesis of rotavirus-induced diarrhea.
D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D000833:Animals, Suckling; D003967:Diarrhea / Q000209:etiology*; D006162:Guanylate Cyclase / Q000378:metabolism; D007410:Intestinal Diseases / Q000201:enzymology* / Q000209:etiology; D007421:Intestine, Small / Q000201:enzymology*; D051379:Mice; D012400:Rotavirus Infections / Q000201:enzymology*; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism; D013393:Sucrase / Q000378:metabolism; D013937:Thymidine Kinase / Q000378:metabolism; D000520:alpha-Glucosidases / Q000378:metabolism; D001616:beta-Galactosidase / Q000378:metabolism
D013937:Thymidine Kinase; D000469:Alkaline Phosphatase; D000520:alpha-Glucosidases; D001616:beta-Galactosidase; D013393:Sucrase; D006162:Guanylate Cyclase; D000254:Sodium-Potassium-Exchanging ATPase