Insulin receptors in isolated mouse pancreatic acini

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

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51 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

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.