The lysosomal hydrolases in the rat pancreas after maximal or supramaximal stimulation with cerulein.
The decompartmentation of lysosomal compartment in pancreatic acinar cells with consecutive activation of zymogens might play an important role as a "trigger mechanism" in acute pancreatitis. The admixture of lysosomal hydrolases to secretory enzymes in pancreatic juice was found, but their role in pancreatic secretion remains obscure. The aim of the present study was to assess the fragility of pancreatic lysosomal structure after maximal (optimal) or supramaximal stimulation of rats with cerulein during 3, 6, 12 h, and after recovery. In the mitochondrial-lysosomal (M-L) and in the supernatant (S) of pancreases free (F) total (T), and fractional free (%F/T) activities of beta-glucuronidase (beta G), acid phosphatase (AcP), cathepsins (Cs), and beta-N-acetyl-hexosaminidase (NAH) were estimated. In edematous pancreatitis following supramaximal stimulation with cerulein, a significant increase of %F/T of beta G in whole homogenate began at 6 h of hyperstimulation in comparison to the control (93 vs 42% p < 0.01). This increment persisted until 12 h of hyperstimulation and declined after 24 and 48 h of recovery to 67-69%. The changes of %F/T of beta G in M-L followed those in whole homogenate, and additionally the increase free activity in S after 6 h of hyperstimulation and after 24 h recovery occurred. The respective activities of other hydrolases showed a similar pattern of changes. It is of interest that fragility of lysosomal membranes increases significantly also after maximal stimulation when inflammatory changes were absent. Our results suggest that the increase of lysosomal fragility of the pancreas is most unlikely pathological in itself, but also occurs during stimulated pancreatic secretion.(ABSTRACT TRUNCATED AT 250 WORDS)
Baniukiewicz
A A
AA
Gastroenterology Department, Medical Academy, Bialystok, Poland.
Dlugosz
J W
JW
Gabryelewicz
A
A
D000208:Acute Disease; D000818:Animals; D002108:Ceruletide / Q000494:pharmacology*; D005966:Glucuronidase / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism*; D008247:Lysosomes / Q000201:enzymology*; D008297:Male; D010179:Pancreas / Q000201:enzymology*; D010195:Pancreatitis / Q000209:etiology; D051381:Rats; D017208:Rats, Wistar
D002108:Ceruletide; D006867:Hydrolases; D005966:Glucuronidase