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Synaptojanin 1 (SYNJ1) is a brain-enriched lipid phosphatase critically involved in autophagosomal/endosomal trafficking, synaptic vesicle recycling and metabolism of phosphoinositides. Previous studies suggest that  SYNJ1  polymorphisms have significant impact on the age of onset of Alzheimer’s disease (AD) and that SYNJ1 is involved in amyloid-induced toxicity. Yet SYNJ1 protein level and cellular localization in  post-mortem  human AD brain tissues have remained elusive. This study aimed to examine whether SYNJ1 localization and expression are altered in  post-mortem  AD brains. We found that SYNJ1 is accumulated in Hirano bodies, plaque-associated dystrophic neurites and some neurofibrillary tangles (NFTs). SYNJ1 immunoreactivity was higher in neurons and in the senile plaques in AD patients carrying one or two  ApolipoproteinE (APOE) ε4  allele(s). In two large cohorts of  APOE -genotyped controls and AD patients,  SYNJ1  transcripts were significantly increased in AD temporal isocortex compared to control. There was a significant increase in  SYNJ1  transcript in  APOEε4  carriers compared to non-carriers in AD cohort. SYNJ1 was systematically co-enriched with PHF-tau in the sarkosyl-insoluble fraction of AD brain. In the RIPA-insoluble fraction containing protein aggregates, SYNJ1 proteins were significantly increased and observed as a smear containing full-length and cleaved fragments in AD brains. In vitro cleavage assay showed that SYNJ1 is a substrate of calpain, which is highly activated in AD brains. Our study provides evidence of alterations in  SYNJ1  mRNA level and SYNJ1 protein degradation, solubility and localization in AD brains.

acta neuropathologica communications

The lipid phosphatase Synaptojanin 1 undergoes a significant alteration in expression and solubility and is associated with brain lesions in Alzheimer’s disease