title: Matched regulation of gastrointestinal performance in the Burmese python, Python molurus.
abstract: In Burmese pythons fasting and feeding cause dramatic regulation of gastric acid production and intestinal nutrient uptake. Predictably, other components of their gastrointestinal tract are similarly regulated with each meal. We therefore assessed the matched regulation of gastrointestinal performance by comparing the postprandial activities and capacities of gastric (pepsin), pancreatic (amylase and trypsin) and intestinal (aminopeptidase-N and maltase) enzymes, and intestinal nutrient uptake. Tissue samples were collected from pythons fasted and at 0.25, 0.5, 1, 2, 3, 4, 6, 10 and 15 days following their consumption of rodent meals equaling 25% of snake body mass. With feeding, pythons experience no significant change in stomach mass, whereas both the pancreas and small intestine doubled in mass. Feeding also triggered a depletion of gastric mucosal pepsinogen, a respective 5.7- and 20-fold increase in the peak activities of pancreatic trypsin and amylase, and a respective 2.3- and 5.5-fold increase in the peak activities of intestinal maltase and aminopeptidase-N. Enzyme activities peaked between 2 and 4 days postfeeding and returned to fasting levels by day 10. Independent of digestive stage, python intestine exhibited a proximal to distal decline in enzyme activity. For both sugars and proteins, intestinal capacities for enzyme activity were significantly correlated with nutrient uptake capacities. The concomitant postprandial upregulation of tissue morphology, intestinal nutrient transport rates and enzyme activities illustrate, for the python, the matched regulation of their gastrointestinal performance with each meal.
authors.affiliation: Department of Biological Sciences, The University of Alabama, Tuscaloosa, AL 35487-0344, USA. clcox@uta.edu
authors.forename: Christian L
authors.initials: CL
authors.lastname: Cox
authors.forename: Stephen M
authors.initials: SM
authors.lastname: Secor
mesh_terms: D000626:Aminopeptidases; D000681:Amylases / Q000378:metabolism; D000818:Animals; D001692:Biological Transport; D017821:Boidae / Q000502:physiology*; D005247:Feeding Behavior; D005753:Gastric Mucosa / Q000033:anatomy & histology / Q000648:ultrastructure; D041981:Gastrointestinal Tract / Q000502:physiology*; D005947:Glucose / Q000378:metabolism; D007422:Intestines / Q000033:anatomy & histology / Q000201:enzymology; D007930:Leucine / Q000378:metabolism; D002052:Myanmar; D009929:Organ Size; D010179:Pancreas / Q000201:enzymology / Q000648:ultrastructure; D010434:Pepsin A / Q000378:metabolism; D011392:Proline / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism; D000520:alpha-Glucosidases / Q000378:metabolism
chemical_list: D011392:Proline; D000681:Amylases; D000520:alpha-Glucosidases; D000626:Aminopeptidases; D014357:Trypsin; D010434:Pepsin A; D007930:Leucine; D005947:Glucose