Activation of the ATP-sensitive K+ channel by long chain acyl-CoA. A role in modulation of pancreatic beta-cell glucose sensitivity

J Biol Chem. 1996 May 3;271(18):10623-6. doi: 10.1074/jbc.271.18.10623.

Abstract

Long-term exposure to elevated levels of long chain free fatty acids decreases glucose-induced insulin secretion from pancreatic islets and clonal pancreatic beta-cells. The mechanism for this loss of glucose sensitivity is at present not known. In this study, we evaluated the possibility that increases in long chain acyl-CoA esters (LC-CoA), the metabolically active form of free fatty acids, might mediate the loss of glucose sensitivity. We observed that cellular levels of LC-CoA increased more than 100% in response to overnight incubation with 0.5 mM palmitic acid complexed to albumin. In the same studies, the total CoA pool increased by about 40%. Patch-clamp studies demonstrated that saturated and unsaturated LC-CoA, but not malonyl-CoA or free CoASH, induced a rapid and slowly reversible opening of ATP-sensitive K+ channels. The effect was concentration-dependent between 10 nM and 1 microM. These findings indicate that the ATP-regulated K/ channels is a sensitive target for LC-CoA and suggest that high levels of LC-CoA, which accumulate in response to hyperglycemia or prolonged exposure to free fatty acids, may prevent channel closure and contribute to the development of beta-cell glucose insensitivity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acyl Coenzyme A / metabolism*
  • Adenosine Triphosphate / metabolism*
  • Animals
  • Cells, Cultured
  • Female
  • Glucose / metabolism
  • Hyperglycemia / metabolism
  • Islets of Langerhans / metabolism*
  • Male
  • Mice
  • Potassium Channels / metabolism*

Substances

  • Acyl Coenzyme A
  • Potassium Channels
  • Adenosine Triphosphate
  • Glucose