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 [3H]-leucine, responded to carbamylcholine chloride by increased secretion of [3H]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 - 1982

Funding

This work was supported by PHS grants CA 27443 and CA 23055, award ed by the National Cancer Institute, Department of Health and Human Services. We gratefully acknowledge the excellent technical assistance of Rosetta Young Kale. We also thank Lola River0 for secretarial help in preparation of this manuscript.

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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