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Beta-actin is a target for transglutaminase activity at synaptic endings in chicken telencephalic cell cultures.
- Source :
-
Journal of molecular neuroscience : MN [J Mol Neurosci] 2012 Feb; Vol. 46 (2), pp. 410-9. Date of Electronic Publication: 2011 Jul 26. - Publication Year :
- 2012
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Abstract
- Transglutaminases are Ca(2+)-dependent enzymes that catalyse the covalent cross-linking of protein-bound glutamine and lysine residues, which can stabilise proteins or protein aggregates. In the brain, elevated expression levels and activity of transglutaminases are known to be linked with several neurodegenerative diseases. However, little is known about the physiological functions of transglutaminases in the central nervous system. In this study, we examined the expression and activity of transglutaminase 1 in chicken telencephalic cell cultures. We observed a cytosolic expression of transglutaminase 1 in telencephalic neurons. However, transglutaminase 1 activity was restricted to synaptic endings. Transglutaminase targets in the cultured cells were characterised via a biotinylation assay and β-actin was identified as a substrate. Furthermore, we were able to show that β-actin is a target for the activity of recombinant human transglutaminase 1 in vitro. We propose a mechanism where neuronal transglutaminase 1 is activated by synaptic activity-dependent influx of calcium ions and thereupon catalyse the formation of an intramolecular cross-link in β-actin, thereby stabilising the actin cytoskeleton against depolymerising effects. In this way, transglutaminase 1 could modulate actin-dependent plasticity events at synaptic endings.
- Subjects :
- Actins chemistry
Actins drug effects
Amines pharmacology
Animals
Biotin analogs & derivatives
Biotin pharmacology
Biotinylation
Cell Membrane enzymology
Cell Nucleus enzymology
Cells, Cultured ultrastructure
Chick Embryo
Cross-Linking Reagents pharmacology
Cytoskeleton ultrastructure
Cytosol enzymology
Genetic Vectors genetics
Humans
Microscopy, Fluorescence
Nucleopolyhedroviruses genetics
Presynaptic Terminals enzymology
Recombinant Fusion Proteins isolation & purification
Recombinant Fusion Proteins pharmacology
Recombinant Fusion Proteins physiology
Species Specificity
Spodoptera
Substrate Specificity
Telencephalon embryology
Telencephalon metabolism
Transglutaminases genetics
Transglutaminases isolation & purification
Actins metabolism
Nerve Tissue Proteins physiology
Neurons enzymology
Telencephalon cytology
Transglutaminases physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1559-1166
- Volume :
- 46
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Journal of molecular neuroscience : MN
- Publication Type :
- Academic Journal
- Accession number :
- 21789544
- Full Text :
- https://doi.org/10.1007/s12031-011-9601-8