| First Author | Odfalk KF | Year | 2024 |
| Journal | Hippocampus | Volume | 34 |
| Issue | 1 | Pages | 29-35 |
| PubMed ID | 37961834 | Mgi Jnum | J:350115 |
| Mgi Id | MGI:7661208 | Doi | 10.1002/hipo.23586 |
| Citation | Odfalk KF, et al. (2024) Hippocampal TMEM55B overexpression in the 5XFAD mouse model of Alzheimer's disease. Hippocampus 34(1):29-35 |
| abstractText | Dysfunction of the endosomal-lysosomal network is a notable feature of Alzheimer's disease (AD) pathology. Dysfunctional endo-lysosomal vacuoles accumulate in dystrophic neurites surrounding amyloid beta (Abeta) plaques and may be involved in the pathogenesis and progression of Abeta aggregates. Trafficking and thus maturation of these dysfunctional vacuoles is disrupted in the vicinity of Abeta plaques. Transmembrane protein 55B (TMEM55B), also known as phosphatidylinositol-4,5-bisphosphate 4-phosphatase 1 (PIP4P1) is an endo-lysosomal membrane protein that is necessary for appropriate trafficking of endo-lysosomes. The present study tested whether overexpression of TMEM55B in the hippocampus could prevent plaque-associated axonal accumulation of dysfunctional endo-lysosomes, reduce Abeta plaque load, and prevent hippocampal-dependent learning and memory deficits in the 5XFAD mouse models of Abeta plaque pathology. Immunohistochemical analyses revealed a modest but significant reduction in the accumulation of endo-lysosomes in dystrophic neurites surrounding Abeta plaques, but there was no change in hippocampal-dependent memory or plaque load. Overall, these data indicate a potential role for TMEM55B in reducing endo-lysosomal dysfunction during AD-like Abeta pathology. |
