Insulin receptors in isolated mouse pancreatic acini

Murray Korc, Hariharan Sankaran, K. Y. Wong, John A. Williams, Ira D. Goldfine

Research output: Contribution to journalArticle

53 Scopus citations


Specific insulin receptors were measured in isolated mouse pancreatic acini. Scatchard analyses revealed a high affinity binding site with a Kd of 1.67 nM and a lower affinity site with a Kd of 83 nM. Binding of insulin to these receptors was rapid, one-half maximal binding occurring at 2 min and maximal binding at 30 min. Insulin stimulated the uptake of the glucose analogue 2-deoxy-D-glucose; maximum effects were detected at 1.67 μM. Insulin, in contrast, had no direct effects on alpha-aminoisobutyric acid uptake. The finding of high affinity insulin receptors in pancreatic acinar cells supports the hypothesis that insulin may directly regulate specific functions in the exocrine pancreas.

Original languageEnglish (US)
Pages (from-to)293-299
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Sep 29 1978

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Insulin receptors in isolated mouse pancreatic acini'. Together they form a unique fingerprint.

  • Cite this

    Korc, M., Sankaran, H., Wong, K. Y., Williams, J. A., & Goldfine, I. D. (1978). Insulin receptors in isolated mouse pancreatic acini. Biochemical and Biophysical Research Communications, 84(2), 293-299.