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Protein cross-linking by transglutaminase induced in long-term potentiation in the CA1 region of hippocampal slices
| Content Provider | Semantic Scholar |
|---|---|
| Author | Friedrich, Péter Fesus, Làszlò Tarcsa, Edit Czéh, Gábor |
| Copyright Year | 1991 |
| Abstract | 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. |
| Starting Page | 331 |
| Ending Page | 334 |
| Page Count | 4 |
| File Format | PDF HTM / HTML |
| DOI | 10.1016/0306-4522(91)90297-2 |
| PubMed reference number | 1681463 |
| Journal | Medline |
| Volume Number | 43 |
| Alternate Webpage(s) | https://api.elsevier.com/content/article/pii/0306452291902972 |
| Alternate Webpage(s) | https://www.sciencedirect.com/science/article/pii/0306452291902972?dgcid=api_sd_search-api-endpoint |
| Alternate Webpage(s) | https://doi.org/10.1016/0306-4522%2891%2990297-2 |
| Journal | Neuroscience |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |