PROTEIN CROSS-LINKING BY TRANSGLUTAMINASE INDUCED IN LONG-TERM POTENTIATION IN THE CA1 REGION OF HIPPOCAMPAL SLICES

被引：26
|
作者：
FRIEDRICH, P
FESUS, L
TARCSA, E
CZEH, G
机构：
[1] DEBRECEN UNIV MED,SCH MED,DEPT BIOCHEM,H-4012 DEBRECEN,HUNGARY
[2] UNIV PECS,SCH MED,INST PHYSIOL,H-7643 PECS,HUNGARY
来源：
NEUROSCIENCE | 1991年 / 43卷 / 2-3期
关键词：
D O I：
10.1016/0306-4522(91)90297-2
中图分类号：
Q189 [神经科学];
学科分类号：
071006 ;
摘要：
Long-term potentiation induced by high-frequency stimulation of Schaffer collaterals in slices of rat hippocampus is accompanied by protein cross-linking by the Ca2+-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 Ca2+-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.
引用
收藏
页码：331 / 334
页数：4
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