Hosli_1997_J.Chem.Neuroanat_13_95

The cellular localization of binding sites for [125I]galanin was studied in explant cultures of rat neocortex, cerebellum, locus coeruleus and spinal cord by means by of autoradiography. Binding sites for the peptide were observed on a great number of astrocytes in all CNS regions studied. In addition to astrocytes, many neurones were intensely labelled by [125I]galanin. Binding of [125I]galanin (10(-8) M) to both astrocytes and neurones was markedly reduced or inhibited by the unlabelled peptide at high concentration (10(-6) M), suggesting 'specific' binding of the radioligand. Evidence for the colocalization of galanin and cholinergic receptors on astrocytes was provided by combined autoradiographic and immunohistochemical studies. Many astrocytes were labelled by [125I]galanin and immunostained with antibodies to either muscarinic or nicotinic receptors. Electrophysiological studies revealed that addition of galanin (10(-9) to 10(-7) M) to the bathing fluid caused a dose-dependent hyperpolarization of the majority of astrocytes studied. When galanin (10(-8) M) and the cholinergic agonists muscarine and nicotine (10(-6) M) were tested on the same astrocyte, all three compounds induced a hyperpolarization, suggesting a colocalization of functional galanin and cholinergic receptors on the glial membrane.