A thrombin cleavage fragment of apolipoprotein E exhibits isoform-specific neurotoxicity

Abstract

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.

Keywords

Apolipoprotein EGene isoformCleavage (geology)ThrombinNeurotoxicityMolecular biologyFragment (logic)BiologyIn vitroBiochemistryToxicityChemistryImmunologyMedicineGeneInternal medicinePlatelet

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Publication Info

Year: 1996
Type: article
Volume: 7
Issue: 15
Pages: 2529-2532
Citations: 97
Access: Closed

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APA Style

                            
                                
                                    M Marques, 
                                
                                    Martin Tolar, 
                                
                                    Judith A.K. Harmony
                                
                                et al.
                            
                            (1996). 
                            A thrombin cleavage fragment of apolipoprotein E exhibits isoform-specific neurotoxicity. 
                            Neuroreport
                            , 7
                            (15)
                            , 2529-2532.
                            https://doi.org/10.1097/00001756-199611040-00025
                        

Identifiers

DOI: 10.1097/00001756-199611040-00025