Differentiation-dependent changes of nicotinic synapse-associated proteins.
Developmentally regulated changes were followed by analyzing the protein composition in vivo of the electric organ of Torpedo marmorata. A 45 000-Mr component, most likely a form of actin, is found to decrease during synaptogenesis, whereas a 43 000-Mr component increases significantly at later embryonic stages, to become the most abundant protein of electric organ. The 43 000-Mr polypeptides are heterogeneous in their solubilization properties and isoelectric points. Translation in vitro of mRNA isolated from embryonic electric organ shows that the appearance of these proteins during development is regulated by the amount of translatable mRNA available. The close correlation between the translatable amounts of mRNA in vitro and the protein synthesis observed in vivo during synaptogenesis suggests that the functional maturation of the electric organ is linked to the appearance of 43 000-Mr polypeptides.
D000199:Actins / Q000096:biosynthesis; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004557:Electric Organ / Q000196:embryology / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007120:Immunochemistry; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D012333:RNA, Messenger / Q000302:isolation & purification*; D011950:Receptors, Cholinergic / Q000378:metabolism*; D011978:Receptors, Nicotinic / Q000378:metabolism*; D014101:Torpedo / Q000378:metabolism
D000199:Actins; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger; D011950:Receptors, Cholinergic; D011978:Receptors, Nicotinic