Journal Cover: 1990

Ryanodine binding proteins of the CNS have been identified using monoclonal antibodies against avian skeletal muscle ryanodine binding proteins. These proteins were localized to intracellular membranes of the dendrites, perikarya, and axons of cerebellar Purkinje neurons using laser confocal microscopy and immunoelectron microscopy. Ryanodine binding proteins were not found in dendritic spines. Immunoprecipitation and [3H]epiryanodine binding experiments revealed that the cerebellar ryanodine binding proteins have a native molecular weight of ~2000 kd and are composed of two high molecular weight (~500 kd) polypeptide subunits. A comparable protein having a single high molecular weight polypeptide subunit was observed in the remainder of the brain. If the ryanodine binding proteins in muscle and nerve are similar in function, then the neuronal proteins may participate in the release of calcium from intracellular stores that are mechanistically and spatially distinct from those gated by inositol triphosphate receptors.

Ellisman MH, Deerinck TJ, Ouyang Y, Beck CF, Tanksley SJ, Walton PD, Airey JA, Sutko JL (1990) Identification and Localizatoin of Ryanodine Binding Proteins in the Avian Central Nervous System. Neuron, Vol 5, pp 135-146 PubMed