Sialylated human apolipoprotein E (apoE(s)) is preferentially associated with neuron-enriched cultures from APOE transgenic mice

Pu Ting Xu, Donald Schmechel, Hui Ling Qiu, Michael Herbstreith, Tracie Rothrock-Christian, Michele Eyster, Allen D. Roses, John R. Gilbert

Research output: Contribution to journalArticle

35 Scopus citations

Abstract

Mice transgenic for human APOE2, E3, and E4 alleles express native 34- kDa human apoE and two sialylated apoE isoproteins with approximate molecular weights of 37 kDa (apoE(s)) and 39 kDa (apoE(s2)) in brain. These multiple apoE/apoE(s)/apoE(s2) band patterns on Western blot are also observed in human brain, but are not seen in wild-type mouse brain. Both the 37-kDa apoE(s) and 39-kDa apoE(s2) are coprecipitated with native 34-kDa apoE by antibody to human apoE. Neuraminidase digestion eliminates the 37- and 39- kDa forms and results in a downward shift in the bands to the position of the 34-kDa native form. These sialylated apoE isoproteins are found preferentially associated with neurons and contribute significantly (50-60%) to the total neuronal apoE in neuronal cultures from transgenic mice, while only 5-10% of total apoE is sialylated in cultures enriched in glial cells. In situ hybridization and immunocytochemistry demonstrate apoE mRNA and apoE immunoreactivity are predominantly located in cell soma of neurons, not in neuronal processes.

Original languageEnglish (US)
Pages (from-to)63-75
Number of pages13
JournalNeurobiology of Disease
Volume6
Issue number1
DOIs
StatePublished - Feb 1999

ASJC Scopus subject areas

  • Neurology

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    Xu, P. T., Schmechel, D., Qiu, H. L., Herbstreith, M., Rothrock-Christian, T., Eyster, M., Roses, A. D., & Gilbert, J. R. (1999). Sialylated human apolipoprotein E (apoE(s)) is preferentially associated with neuron-enriched cultures from APOE transgenic mice. Neurobiology of Disease, 6(1), 63-75. https://doi.org/10.1006/nbdi.1998.0213