title: Exocrine pancreatic function in critically ill patients: septic shock versus non-septic patients.
abstract: OBJECTIVE
  To determine the exocrine pancreatic function in critically ill patients.
  
  
  METHODS
  Prospective cohort study.
  
  
  METHODS
  Medical intensive care unit.
  
  
  METHODS
  A total of 18 critically ill patients (11 patients with septic shock according to the criteria of the American College of Chest Physicians/Society of Critical Care Medicine, 7 nonseptic patients). The results obtained in these subjects were compared with the data obtained in seven healthy volunteers.
  
  
  METHODS
  Examination of exocrine pancreatic function was done by means of a cholecystokinin-secretin test. Intravenous stimulation of the exocrine pancreas with cholecystokinin and secretin (1 unit/kg body weight/hr each) and aspiration of duodenal fluid by a gastroscopically inserted oroduodenal tube was done during a period of 1 hr.
  
  
  RESULTS
  The content of amylase, chymotrypsin, and trypsin in aspirated duodenal fluid was significantly reduced in patients with septic shock compared with nonseptic patients as well as healthy subjects (p < .01). The volume of aspirated fluid was significantly reduced in patients with septic shock compared with healthy controls (p = .03), but not in nonseptic patients. The content of bicarbonate was not statistically different in the three groups. No significant correlation was to find between variables of exocrine pancreatic function and Acute Physiology and Chronic Health Evaluation III score, sepsis-related organ failure assessment score, systolic arterial pressure and mean arterial pressure in septic shock patients. Positive end-expiratory pressure was significantly correlated with the content of trypsin (r2 = 0.52; p = .02). Postmortem examinations of five septic patients who died during the intensive care stay did not reveal gross morphologic alterations of pancreatic tissue.
  
  
  CONCLUSIONS
  The study shows two pancreatic enzyme systems, namely, amylase as a carbohydrate splitting enzyme and the proteolytic enzymes trypsin and chymotrypsin, strongly affected in critically ill patients with septic shock.
authors.affiliation: Clinic of Internal Medicine IV--Department of Gastroenterology and Hepatology, University of Vienna, Austria.
authors.forename: B
authors.initials: B
authors.lastname: Tribl
authors.forename: C
authors.initials: C
authors.lastname: Madl
authors.forename: P R
authors.initials: PR
authors.lastname: Mazal
authors.forename: B
authors.initials: B
authors.lastname: Schneider
authors.forename: S
authors.initials: S
authors.lastname: Spitzauer
authors.forename: H
authors.initials: H
authors.lastname: Vogelsang
authors.forename: A
authors.initials: A
authors.lastname: Gangl
mesh_terms: D000368:Aged; D000681:Amylases / Q000378:metabolism; D002766:Cholecystokinin; D002918:Chymotrypsin / Q000378:metabolism; D015331:Cohort Studies; D003422:Critical Care; D010188:Exocrine Pancreatic Insufficiency / Q000175:diagnosis* / Q000503:physiopathology; D005260:Female; D006801:Humans; D008297:Male; D008875:Middle Aged; D010179:Pancreas / Q000503:physiopathology; D010186:Pancreatic Function Tests; D011446:Prospective Studies; D012633:Secretin; D012772:Shock, Septic / Q000175:diagnosis* / Q000503:physiopathology; D014357:Trypsin / Q000378:metabolism
chemical_list: D012633:Secretin; D002766:Cholecystokinin; D000681:Amylases; D002918:Chymotrypsin; D014357:Trypsin