Synapsin I is associated with cholinergic nerve terminals in the electric organs of Torpedo, Electrophorus, and Malapterurus and copurifies with Torpedo synaptic vesicles.
Using an affinity-purified monospecific polyclonal antibody against bovine brain synapsin I, the distribution of antigenically related proteins was investigated in the electric organs of the three strongly electric fish Torpedo marmorata, Electrophorus electricus, Malapterurus electricus and in the rat diaphragm. On application of indirect fluorescein isothiocyanate-immunofluorescence and using alpha-bungarotoxin for identification of synaptic sites, intense and very selective staining of nerve terminals was found in all of these tissues. Immunotransfer blots of tissue homogenates revealed specific bands whose molecular weights are similar to those of synapsin Ia and synapsin Ib. Moreover, synapsin I-like proteins are still attached to the synaptic vesicles that were isolated in isotonic glycine solution from Torpedo electric organ by density gradient centrifugation and chromatography on Sephacryl-1000. Our results suggest that synapsin I-like proteins are also associated with cholinergic synaptic vesicles of electric organs and that the electric organ may be an ideal source for studying further the functional and molecular properties of synapsin.
D000818:Animals; D000906:Antibodies; D003964:Diaphragm / Q000166:cytology; D004557:Electric Organ / Q000166:cytology*; D004593:Electrophorus; D005399:Fishes; D005455:Fluorescent Antibody Technique; D009419:Nerve Tissue Proteins / Q000032:analysis*; D010750:Phosphoproteins / Q000032:analysis*; D051381:Rats; D016704:Synapsins; D013572:Synaptic Vesicles / Q000648:ultrastructure*; D014101:Torpedo
D000906:Antibodies; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D016704:Synapsins