Key result
ApoE4-derived 22 kDa thrombin fragment causes greater primary neuronal toxicity than the apoE3 fragment.
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A 22 kDa fragment of apoE containing a putative cytotoxi domain was identified in postmortem human brain tissue and fresh CSF. This fragment is apparently equivalent to the major apoE thrombin cleavage product. In vitro toxicity assays demonstrate that the corresponding fragment derived from recombinantly expressed human apoE is toxic to primary neurons in culture and that the E4-derived fragment is significantly more toxic than the fragment derived from the E3 isoform. These results suggest that proteolytic fragments of apoE may play a direct role in the pathology associated with AD and other diseases in which apoE has been implicated.
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Marques et al. (1996) studied Alzheimer's disease. 22 kDa thrombin cleavage fragment of apolipoprotein E (E4 isoform) vs. 22 kDa thrombin cleavage fragment of apolipoprotein E (E3 isoform) was evaluated on In vitro neurotoxicity to primary neurons in culture. A 22 kDa thrombin cleavage fragment of human apoE is toxic to primary neurons in culture, with the E4-derived fragment exhibiting significantly greater toxicity than the E3-derived fragment.
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