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Spectrins in developing rat hippocampal cells
We studied the spectrins in developing hippocampal tissue in vivo and in vitro to learn how they contribute to the organization of synaptic and extrasynaptic regions of the neuronal plasma membrane. β-Spectrin, but not β-fodrin or α-fodrin, increased substantially during postnatal development in the...
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Published in: | Brain research. Developmental brain research 2001-07, Vol.129 (1), p.81-93 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | We studied the spectrins in developing hippocampal tissue in vivo and in vitro to learn how they contribute to the organization of synaptic and extrasynaptic regions of the neuronal plasma membrane. β-Spectrin, but not β-fodrin or α-fodrin, increased substantially during postnatal development in the hippocampus, where it was localized in neurons but not in astrocytes. Immunoprecipitations from neonatal and adult hippocampal extracts suggest that while both β-spectrin and β-fodrin form heteromers with α-fodrin, oligomers containing all three subunits are also present. At the subcellular level, β-fodrin and α-fodrin were present in the cell bodies, dendrites, and axons of pyramidal-like neurons in culture, as well as in astrocytes. β-Spectrin, by contrast, was absent from axons but present in cell bodies and dendrites, where it was organized in a loose, membrane-associated meshwork that lacked α-fodrin. A similar meshwork was also apparent in pyramidal neurons in vivo. At some dendritic spines, α-fodrin was present in the necks but not in the heads, whereas β-spectrin was present at significant levels in the spine heads. The presence of significant amounts of β-spectrin without an accompanying α-fodrin subunit was confirmed by immunoprecipitations from extracts of adult hippocampus. Our results suggest that the spectrins in hippocampal neurons can assemble to form different membrane-associated structures in distinct membrane domains, including those at synapses. |
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ISSN: | 0165-3806 |
DOI: | 10.1016/S0165-3806(01)00160-2 |