The so-called prion diseases are probably caused by the conformational conversion of the cellular prion protein (PrPc) into an abnormal, pathological form (PrPsc). PrPc is widely expressed in neuronal tissues, but its function is not known. From electrophysiological measurements in prion-less mice it was proposed that PrPc may contribute to the structural integrity of central synapses containing gamma-aminobutyric acid type A (GABAA) receptors. We tried to substantiate this hypothesis by obtaining evidence for a structural link between the GABAA receptor and PrPc. Preparations of PrPc and GABAA receptors, respectively, from cow brain were analysed for PrPc-GABAA receptor complexes. No evidence for such complexes could be obtained in our experiments, although the protein purification schemes used should favour the preservation of intermolecular linkages. We conclude that further data concerning interactions of PrPc with other proteins are needed to obtain insight into its normal functional role.