Carbamylcholine stimulation of protein secretion in pancreatic acinar carcinoma of rat

John R. Warren*, Michael J. Trump, Janardan K Reddy, Michael J. Becich

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Pancreatic acinar carcinoma fragments, pulse-chase labeled with [ 3 H]-leucine, responded to carbamylcholine chloride by increased secretion of [ 3 H]leucine-labeled protein into external buffer medium. Secretion of labeled protein by the carcinoma fragments increased in concentration-dependent fashion between 10 -8 -10 -5 M carbamylcholine, was completely inhibited at 4°C, and was accompanied by an equivalent increase in the secretion of preformed amylase. A maximally effective carbamylcholine concentration of 10 -5 M was observed for both carcinoma fragments and normal pancreas lobules. However, the maximal rate of protein secretion by the carcinoma fragments was only approximately one-fifth the rate determined for the normal pancreas lobules. This modest secretory response indicates a population of partially differentiated cells in the pancreatic acinar carcinoma which secrete less enzyme than fully differentiated adult pancreatic acinar cells. Secretory responsiveness can be utilized as a quantitative acinar cell response in studies on differentiation in pancreatic carcinoma.

Original languageEnglish (US)
Pages (from-to)245-253
Number of pages9
JournalCancer Letters
Volume15
Issue number3
DOIs
StatePublished - Jan 1 1982

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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