Protein cross-linking by transglutaminase induced in long-term potentiation in the Ca1 region of hippocampal slices.
Long-term potentiation induced by high-frequency stimulation of Schaffer collaterals in slices of rat hippocampus is accompanied by protein cross-linking by the Ca(2+)-dependent enzyme transglutaminase. This conclusion was drawn from the accumulation of the "isodipeptide" epsilon(gamma-glutamyl)lysine in the proteolytic digests of tetanized, but not of control, slices. The isopeptide bond is formed by transglutaminase between glutamyl-gamma-CONH2 and lysyl-epsilon-NH2 groups of proteins. It is suggested that the Ca(2+-induced covalent cross-linking of neuronal, probably dendritic, proteins may be part of the mechanism of long-term plastic changes via stabilization of newly formed supramolecular protein assemblies at the synapse.
Institute of Enzymology, Hungarian Academy of Sciences, Budapest.
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Friedrich
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Fesus
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Tarcsa
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Czéh
D000200:Action Potentials; D000818:Animals; D004151:Dipeptides / Q000378:metabolism; D004558:Electric Stimulation; D004594:Electrophysiology; D005260:Female; D006624:Hippocampus / Q000378:metabolism / Q000502:physiology*; D066298:In Vitro Techniques; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D011503:Transglutaminases / Q000378:metabolism*
D004151:Dipeptides; D009419:Nerve Tissue Proteins; D011503:Transglutaminases