IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v389y1997i6652d10.1038_39522.html
   My bibliography  Save this article

An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease

Author

Listed:
  • Shi Du Yan

    (Surgery and Physiology, and Cellular Biophysics, Columbia Unversity, College of Physicians and Surgeons)

  • Jin Fu

    (Surgery and Physiology, and Cellular Biophysics, Columbia Unversity, College of Physicians and Surgeons)

  • Claudio Soto

    (New York University Medical Center)

  • Xi Chen

    (Surgery and Physiology, and Cellular Biophysics, Columbia Unversity, College of Physicians and Surgeons)

  • Huaijie Zhu

    (Surgery and Physiology, and Cellular Biophysics, Columbia Unversity, College of Physicians and Surgeons)

  • Futwan Al-Mohanna

    (Biological and Medical Research, King Faisal Specialist Hospital and Research Centre)

  • Kate Collison

    (Biological and Medical Research, King Faisal Specialist Hospital and Research Centre)

  • Aiping Zhu

    (Surgery and Physiology, and Cellular Biophysics, Columbia Unversity, College of Physicians and Surgeons)

  • Eric Stern

    (Surgery and Physiology, and Cellular Biophysics, Columbia Unversity, College of Physicians and Surgeons)

  • Takaomi Saido

    (Tokyo Metropolitan Institute of Medical Science)

  • Masaya Tohyama

    (Osaka University Medical School)

  • Satoshi Ogawa

    (Osaka University Medical School)

  • Alex Roher

    (Haldeman Laboratory for Alzheimer's Disease Research, Sun Health Research Institute)

  • David Stern

    (Surgery and Physiology, and Cellular Biophysics, Columbia Unversity, College of Physicians and Surgeons)

Abstract

Amyloid-β is a neurotoxic peptide which is implicated in the pathogenesis of Alzheimer's disease. It binds an intracellular polypeptide known as ERAB, thought to be a hydroxysteroid dehydrogenase enzyme, which is expressed in normal tissues, but is overexpressed in neurons affected in Alzheimer's disease. ERAB immunoprecipitates with amyloid-β, and when cell cultures are exposed to amyloid-β, ERAB inside the cell is rapidly redistributed to the plasma membrane. The toxic effect of amyloid-β on these cells is prevented by blocking ERAB and is enhanced by overexpression of ERAB. By interacting with intracellular amyloid-β, ERAB may therefore contribute to the neuronal dysfunction associated with Alzheimer's disease.

Suggested Citation

  • Shi Du Yan & Jin Fu & Claudio Soto & Xi Chen & Huaijie Zhu & Futwan Al-Mohanna & Kate Collison & Aiping Zhu & Eric Stern & Takaomi Saido & Masaya Tohyama & Satoshi Ogawa & Alex Roher & David Stern, 1997. "An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease," Nature, Nature, vol. 389(6652), pages 689-695, October.
    • Handle: RePEc:nat:nature:v:389:y:1997:i:6652:d:10.1038_39522
    DOI: 10.1038/39522
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/39522
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/39522?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:389:y:1997:i:6652:d:10.1038_39522. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.