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Apical Secretion of Lysosomal Enzymes in Rabbit Pancreas Occurs Via a Secretagogue Regulated Pathway and Is Increased After Pancreatic Duct Obstruction

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Apical Secretion of Lysosomal Enzymes in Rabbit Pancreas Occurs Via a Secretagogue Regulated Pathway and Is Increased After Pancreatic Duct Obstruction Apical secretion of lysosomal enzymes in rabbit pancreas occurs via a secretagogue regulated pathway and is increased after pancreatic duct obstruction. T Hirano, … , M Saluja, M L Steer J Clin Invest. 1991;87(3):865-869. https://doi.org/10.1172/JCI115091. Research Article Lysosomal hydrolases such as cathepsin B are apically secreted from rabbit pancreatic acinar cells via a regulated as opposed to a constitutive pathway. Intravenous infusion of the cholecystokinin analogue caerulein results in highly correlated apical secretion of digestive and lysosomal enzymes, suggesting that they are discharged from the same presecretory compartment (zymogen granules). Lysosomal enzymes appear to enter that compartment as a result of missorting. After 7 h of duct obstruction is relieved, caerulein-stimulated apical secretion of cathepsin B and amylase is increased, but the ratio of cathepsin B to amylase secretion is not different than that following caerulein stimulation of animals never obstructed. These findings indicate that duct obstruction causes an increased amount of both lysosomal and digestive enzymes to accumulate within the secretagogue releasable compartment but that duct obstruction does not increase the degree of lysosomal enzyme missorting into that compartment. Pancreatic duct obstruction causes lysosomal hydrolases to become colocalized with digestive enzymes in organelles that, in size and distribution, resemble zymogen granules but that are not subject to secretion in response to secretagogue stimulation. These organelles may be of importance in the development of pancreatitis. Find the latest version: https://jci.me/115091/pdf Apical Secretion of Lysosomal Enzymes in Rabbit Pancreas Occurs Via a Secretagogue Regulated Pathway and Is Increased after Pancreatic Duct Obstruction T. Hirano, A. Saluja, P. Ramarao, M. M. Lerch, M. Saluja and M. L. Steer Department ofSurgery and Harvard Digestive Diseases Center Beth Israel Hospital and Harvard Medical School, Boston, Massachusetts 02215 Abstract can be stimulated by the digestive enzyme secretagogue chole- cystokinin (CCK).' We have reported the results ofa large num- Lysosomal hydrolases such as cathepsin B are apically se- ber of studies that suggest that lysosomal hydrolases may play creted from rabbit pancreatic acinar cells via a regulated as an important role in the pathogenesis ofacute pancreatitis. In a opposed to a constitutive pathway. Intravenous infusion of the recent communication, we noted that obstruction of the rabbit cholecystokinin analogue caerulein results in highly correlated pancreatic duct for 7 h causes subcellular redistribution of lyso- apical secretion of digestive and lysosomal enzymes, suggesting somal hydrolases and the appearance of lysosomal hydrolases that they are discharged from the same presecretory compart- in organelles that, by their size and distribution, resemble zy- ment (zymogen granules). Lysosomal enzymes appear to enter mogen granules (3). These observations led us to suspect that that compartment as a result of missorting. After 7 h of duct pancreatic duct obstruction might have an important effect on obstruction is relieved, caerulein-stimulated apical secretion of lysosomal enzyme secretion. cathepsin B and amylase is increased, but the ratio of cathepsin Surprisingly, little is known of the mechanisms responsible B to amylase secretion is not different than that following cae- for lysosomal enzyme secretion. Most of the studies evaluating rulein stimulation of animals never obstructed. These findings this phenomenon have been performed using nonpolarized cell indicate that duct obstruction causes an increased amount of types, and the results of those studies have indicated that, both lysosomal and digestive enzymes to accumulate within the under most conditions, lysosomal enzymes are secreted in a secretagogue releasable compartment but that duct obstruction constitutive manner (4, 5). In this paper, we report the results does not increase the degree of lysosomal enzyme missorting of studies that have characterized lysosomal enzyme secretion into that compartment. Pancreatic duct obstruction causes lyso- from the exocrine pancreas. Pancreatic acinar cells are believed somal hydrolases to become colocalized with digestive enzymes to secrete digestive enzymes exclusively at the apical surface of in organelles that, in size and distribution, resemble zymogen the cell, and in these cells, digestive enzyme secretion occurs granules but that are not subject to secretion in response to primarily via a well-characterized regulated pathway. We re- secretagogue stimulation. These organelles may be of impor- port that a small fraction ofthe pancreatic content oflysosomal tance in the development of pancreatitis. (J. Clin. Invest. 1991. hydrolases is released from the apical surface of pancreatic cells 87:865-869.) Key words: pancreatitis * cathepsin B - digestive under resting conditions and that intravenous infusion of the enzymes * intracellular trafficking - cell polarity cholecystokinin analogue caerulein increases the rate of lyso- somal enzyme secretion from the apical cell surface. This in- Introduction creased rate of lysosomal enzyme secretion closely parallels the enhanced rate of digestive enzyme secretion stimulated by Lysosomal hydrolases are synthesized on the endoplasmic retic- caerulein infusion. These observations indicate that the apical ulum, and along with other newly synthesized proteins includ- secretion of lysosomal hydrolases from the exocrine pancreas ing structural proteins and digestive zymogens, are transported occurs primarily via the regulated rather than via the constitu- to the Golgi complex. During transit through the Golgi com- tive pathway. Relief of pancreatic duct obstruction was found plex, lysosomal hydrolases are glycosylated, 6-mannose phos- to increase the magnitude of secretagogue-stimulated lyso- phorylated, and bound by 6-mannose phosphate-specific re- somal as well as digestive enzyme secretion. Since the lyso- ceptors (1). As a result, the bound lysosomal hydrolases are somal hydrolase cathepsin B can activate trypsinogen (6, 7) and diverted towards the lysosomal compartment and away from trypsin can activate the remaining digestive zymogens, these the pathway(s) by which proteins such as digestive zymogens observations may help to further elucidate events that underlie are exported from the cell. the development of pancreatitis. Rinderknecht and colleagues (2) have reported that lyso- somal enzymes can be detected in human pancreatic juice and Methods that the secretion of some, but not all, lysosomal hydrolases All experiments were performed using New Zealand rabbits of either sex, weighing 2.2-3.0 kg, purchased from Pine Acre Rabbitary (West Address correspondence to Dr. Michael L. Steer, Beth Israel Hospital, Brattleboro, VT). They were housed in light/dark cycle-regulated, air- MA Department of Surgery, 330 Brookline Ave., Boston, 02215. and 16 h 1990 in 17 conditioned (23±3°C) quarters fasted for before each experi- Receivedfor publication 25 June and revisedform Sep- ment. Caerulein and secretin were purchased from Sigma Chemical tember 1990. Co. (St. Louis, MO). CBZ-arginyl-arginine /3-naphthylamide was from Bachem Biosciences (Philadelphia, PA) and ,B-naphthylamide from J. Clin. Invest. Sigma Chemical Co. Leucine-2-naphthylamide, 4-methylumbelliferyl ©3 The American Society for Clinical Investigation, Inc. 0021-9738/91/03/0865/05 $2.00 Volume 87, March 1991, 865-869 1. Abbreviation used in this paper: CCK, cholecystolcinin. Pancreatic Secretion ofLysosomal Enzymes 865 sulfate, 4-methylumbelliferyl N-acetyl 3-D-galactosaminide, and 4- close correlation (P < 0.01) between the output of amylase and methylumbelliferyl N-acetyl f3-D-glucosaminide were purchased from ofcathepsin B that occurred in the presence ofeach ofthe doses Sigma Chemical Co. All other reagents were of the highest purity com- of caerulein tested (0.2-2.0 ,ug/kg/h, Fig. 2). The relationship mercially available. between amylase and cathepsin B output in response to each of Animal preparation. Rabbits were anesthetized with intravenously the doses was similar, i.e., when analyzed individually, the re- administered pentobarbitol (35 mg/kg initially, supplemented by peri- line was not odic doses of 10 mg/kg as needed) and a cannula (PE 50) was intro- gression obtained for each dose significantly differ- duced into the inferior vena cava via the femoral vein. After upper ent from that obtained by combining the results for the remain- abdominal midline laparotomy, the pylorus was ligated and a drainage ing secretagogue doses. Caerulein was also noted to stimulate gastrostomy cannula (PE 70) was placed. The pancreatic duct was can- the secretion of a number of other lysosomal hydrolases into nulated (PE 10) extraduodenally. After placement and exteriorization the pancreatic duct (Table I). In each instance, secretin alone ofthe various cannulas, the abdominal wound was closed. Core temper- caused only mild degrees of lysosomal enzyme secretion, while ature was maintained using a heating pad and overhead lamp. To stim- addition of caerulein (0.5 ,Ag/kg/h) caused a roughly threefold ulate and maintain pancreatic fluid secretion, secretin was infused stimulation of secretion for each ofthe four lysosomal enzymes through the venous catheter at a rate calculated to deliver 2.0 U/kg/h. studied. When indicated, pancreatic ductal obstruction was produced, after an Fractional output ofamylase and cathepsin B. Preliminary
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