[125I]Tyr-bradykinin binding in primary rat brain cultures

Robert E. Lewis, Steven R. Childers, M. Ian Phillips

Research output: Contribution to journalArticlepeer-review

41 Scopus citations


Kinins bind to specific, high affinity recognition sites in rat brain cell culture. Studies in these cultures minimize non-specific binding and degradation of the ligand. Binding of [125I]Tyr-bradykinin to intact cultured brain cells from neonatal rats was time- and pH-dependent. Scatchard analysis of saturation experiments yielded two affinity components with dissociation constant and maximum binding site concentration averaging 1 nM and 100 fmol/mg protein, and 16 M and 1000 fmol/mg protein, respectively. The binding sites were specific for kinins and kinin analogues, and the order of potency in competing for [125I]Tyr-bradykinin binding was Lys-bradykinin > bradykinin > Tyr-bradykinin > Tyr-8-bradykinin ⋙ Des-Arg9-bradykinin. Monovalent and divalent cations inhibited kinin binding. Comparison of competition curves performed in glial-enriched vs neuron-enriched cultures suggested that the kinin binding sites resided primarily on neurons. These data enhance the existing evidence suggesting kinins as neurotransmitters or neuromodulators.

Original languageEnglish (US)
Pages (from-to)263-272
Number of pages10
JournalBrain Research
Issue number2
StatePublished - Nov 4 1985
Externally publishedYes


  • binding
  • bradykinin
  • brain
  • cell culture
  • kinin
  • receptor

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Clinical Neurology
  • Developmental Biology


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