Low-affinity sulfonylurea binding sites reside on neuronal cell bodies in the brain

Brain Res. 1997 Jan 16;745(1-2):1-9. doi: 10.1016/s0006-8993(96)01006-2.

Abstract

The antidiabetic sulfonylurea drugs bind to sites associated with an ATP-sensitive potassium (Katp) channel on cell bodies and terminals of neurons which increase their firing rates or transmitter release when glucose concentrations rise or sulfonylureas are present. High-affinity sulfonylurea binding sites are concentrated in areas such as the substantia nigra (SN) where glucose and sulfonylureas increase transmitter release from GABA neurons. But there is a paucity of high-affinity sites in areas such as the hypothalamic ventromedial nucleus (VMN) where many neurons increase their activity when glucose rises. Here we assessed both high- and low--affinity sulfonylurea binding autoradiographically with 20 nM [3H]glyburide in the presence of absence of Gpp(NH)p. Neurotoxin lesions with 6-hydroxydopamine (6-OHDA), 5,7-dihydroxytryptamine (5,7-DHT) and ibotenic acid were used to elucidate the cellular location of the two sites in the VMN, SN and locus coeruleus (LC). In the VMN, 25% of the sites were of low affinity. Neither 6-OHDA nor 5,7-DHT affected [3H]glyburide binding, while ibotenic acid reduced the number of VMN neurons and abolished low-affinity without changing high-affinity binding. In cell-attached patches of isolated VMN neurons, both 10 mM glucose and 100 microM glyburide decreased the open probability of the Katp channel suggesting that the low-affinity binding site resides on these neurons. In the SN pars reticulata, ibotenic acid reduced the number of neurons and high-affinity [3H]glyburide binding was decreased by 20%, while 6-OHDA had no effect. In the SN pars compacta, both 6-OHDA and ibotenic acid destroyed endogenous dopamine neurons and selectivity ablated low-affinity binding. In the LC, 6-OHDA destroyed norepinephrine neurons and abolished low-affinity binding. These data suggest that low-affinity sulfonylurea binding sites reside on cell bodies on VMN, SN dopamine and LC norepinephrine neuron cell bodies and that high-affinity sites may be on axon terminals of GABA neurons in the SN.

Publication types

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

MeSH terms

  • 5,7-Dihydroxytryptamine / toxicity
  • Animals
  • Binding Sites
  • Brain / cytology
  • Brain / metabolism*
  • Electrophysiology
  • Glyburide / metabolism
  • Hypoglycemic Agents / pharmacology
  • Immunohistochemistry
  • Male
  • Neurons / metabolism*
  • Oxidopamine / toxicity
  • Potassium Channels / drug effects
  • Potassium Channels / metabolism
  • Rats
  • Rats, Sprague-Dawley
  • Serotonin Agents / toxicity
  • Sulfonylurea Compounds / metabolism*
  • Sympatholytics / toxicity

Substances

  • Hypoglycemic Agents
  • Potassium Channels
  • Serotonin Agents
  • Sulfonylurea Compounds
  • Sympatholytics
  • 5,7-Dihydroxytryptamine
  • Oxidopamine
  • Glyburide