Molecular dissection of domains in mutant presenilin 2 that mediate overproduction of amyloidogenic forms of amyloid beta peptides. Inability of truncated forms of PS2 with familial Alzheimer's disease mutation to increase secretion of Abeta42.

@article{Tomita1998MolecularDO,
  title={Molecular dissection of domains in mutant presenilin 2 that mediate overproduction of amyloidogenic forms of amyloid beta peptides. Inability of truncated forms of PS2 with familial Alzheimer's disease mutation to increase secretion of Abeta42.},
  author={Taisuke Tomita and Shinya Tokuhiro and Tadafumi Hashimoto and Keiko Aiba and Takaomi C Saido and Kei Maruyama and Takeshi Iwatsubo},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 33},
  pages={21153-60}
}
Mutations in presenilin (PS) 1 or PS2 genes account for the majority of early-onset familial Alzheimer's disease, and these mutations have been shown to increase production of species of amyloid beta peptide (Abeta) ending at residue 42, i.e. the most amyloidogenic form of Abeta. To gain insight into the molecular mechanisms whereby mutant PS induces overproduction of Abeta42, we constructed cDNAs encoding mutant and/or truncated forms of PS2 and examined the secretion of Abeta42 from COS or… CONTINUE READING

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