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S S Rothman

Publications and source records attributed to S S Rothman.

At least 73 records · Page 4Linked to original sources

Enzyme secretion in the absense of zymogen granules.

Pure pancreatic juice was collected from the cannulated common bile duct of anesthetized rats after an overnight fast. Digestive enzyme secretion was followed in these animals during and after the progressive degranulation of acinar cells produced by sequentially applied cholinergic stimuli. The kinetics of degranulation, a progressive decrease in the number of zymogen granules in acinar cells, was estimated from the relative cell volume occupied by electron-opaque granules at various times using a random pointcount stereological technique to examine tissue sections. Three hourly injections of methacholine chloride were sufficient to produce the almost complete disappearance of electron-opaque granules from secretory cells. Greatly augmented enzyme secretion was still observed in their absence, 7-25 times greater than control values: 10-fold for protein output overall, 7-fold for trypsinogen, and 25-fold for chymotrypsinogen. Secretion in the absence of zymogen granules is discussed relativeto exocytosis and three-compartment (intracellular storage, cytoplasm, and duct lumen)secretory models.

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Chymodenin, a duodenal peptide: specific stimulation of chymotrypsinogen secretion.

Chymodenin, a basic porcine duodenal peptide, was administered to anesthetized rabbits intravenously or added to the medium bathing the isolated pancreas. In the 10(-8)M range, chymodenin rapidly increased chymotrypsinogen (ChTg) secretion, did not increase lipase secretion, and modestly enhanced protein secretion (which could be attributed primarily to augmented ChTg secretion). The increased ChTg output was too rapid to be the result of increased rates of protein synthesis and could not be attributed to the exocytosis os zymogen granule contents because of the enzyme-;pecific nature of the response. In contrast to shymodenin, cholinergic stimulation in vitro produced a relatively lipase-rich, chymotrypsinogen-poor secretion. Lipase and ChTg outputs, which varied relatively independently under unstimulated conditions, covaried in the presence of chymodenin. The existence of a duodenal peptide that produces an enzyme-specific response supports the hypothesis that the secretion of digestive enzymes during digestion is a highly regulated process in which the enzyme content of pancreatic secretion varies with differences in the composition of intestinal substrates.

Animals↗

Selective pancreatic enzyme secretion due to a new peptide called chymodenin.

Chymodenin, a peptide newly isolated from porcine duodenum, elicited a rapid threefold increase in secretion of chymotrypsinogen while increasing secrelion of total protein by only, about 40 percent; lipase secretion was unaffected. The pancreas appears able, under chymodenin stimulation, to rapidly alter the transport of an individual enzyme as opposed to producing en masse secretion of enzyme.

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