Brevican isoforms associate with neural membranes
Article first published online: 17 OCT 2002
Journal of Neurochemistry
Volume 83, Issue 3, pages 738–746, November 2002
How to Cite
Seidenbecher, C. I., Smalla, K.-H., Fischer, N., Gundelfinger, E. D. and Kreutz, M. R. (2002), Brevican isoforms associate with neural membranes. Journal of Neurochemistry, 83: 738–746. doi: 10.1046/j.1471-4159.2002.01183.x
- Issue published online: 17 OCT 2002
- Article first published online: 17 OCT 2002
- Received June 14, 2002; revised manuscript received July 24, 2002; accepted August 20, 2002.
- chondroitinase ABC;
- extracellular matrix;
- glycosylphosphatidylinositol anchor;
- hippocampal primary culture;
- perineuronal nets;
Brevican is a neural-specific proteoglycan of the brain extracellular matrix, which is particularly abundant in the terminally differentiated CNS. It is expressed by neuronal and glial cells, and as a component of the perineuronal nets it decorates the surface of large neuronal somata and primary dendrites. One brevican isoform harbors a glycosylphosphatidylinositol anchor attachment site and, as shown by ethanolamine incorporation studies, is indeed glypiated in stably transfected HEK293 cells as well as in oligodendrocyte precursor Oli-neu cells. The major isoform is secreted into the extracellular space, although a significant amount appears to be tightly attached to the cell membrane, as it floats up in sucrose gradients. Flotation is sensitive to detergent treatment. Brevican is most prominent in the microsomal, light membrane and synaptosomal fractions of rat brain membrane preparations. The association with the particulate fraction is in part sensitive to chondroitinase ABC and phosphatidylinositol-specific phospholipase C treatment. Furthermore, brevican staining on the surface of hippocampal neurons in culture is diminished after hyaluronidase or chondroitinase ABC treatment. Taken together, this could provide a mechanism by which perineuronal nets are anchored on neuronal surfaces.