期刊
JOURNAL OF NEUROSCIENCE
卷 32, 期 3, 页码 946-952出版社
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.3830-11.2012
关键词
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资金
- Deutsche Forschungsgemeinschaft [KFO177, SFB704, FOR1336]
- Hertie Foundation
- University of California
- NIH [AG 00538]
- Walter-und-Ilse-Rose-Foundation
Microglial cells are professional phagocytes of the CNS responsible for clearance of unwanted structures. Neuronal processes are marked by complement C1 before they are removed in development or during disease processes. Target molecules involved in C1 binding and mechanisms of clearance are still unclear. Here we show that the terminal sugar residue sialic acid of the mouse neuronal glycocalyx determines complement C1 binding and microglial-mediated clearance function. Several early components of the classical complement cascade including C1q, C1r, C1s, and C3 were produced by cultured mouse microglia. The opsonin C1q was binding to neurites after enzymatic removal of sialic acid residues from the neuronal glycocalyx. Desialylated neurites, but not neurites with intact sialic acid caps, were cleared and taken up by cocultured microglial cells. The removal of the desialylated neurites was mediated via the complement receptor-3 (CR3;CD11b/CD18). Data demonstrate that mouse microglial cells via CR3 recognize and remove neuronal structures with an altered neuronal glycocalyx lacking terminal sialic acid.
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