Skip to main content

Main menu

  • HOME
  • CONTENT
    • Early Release
    • Featured
    • Current Issue
    • Issue Archive
    • Collections
    • Podcast
  • ALERTS
  • FOR AUTHORS
    • Information for Authors
    • Fees
    • Journal Clubs
    • eLetters
    • Submit
  • EDITORIAL BOARD
  • ABOUT
    • Overview
    • Advertise
    • For the Media
    • Rights and Permissions
    • Privacy Policy
    • Feedback
  • SUBSCRIBE

User menu

  • Log in
  • My Cart

Search

  • Advanced search
Journal of Neuroscience
  • Log in
  • My Cart
Journal of Neuroscience

Advanced Search

Submit a Manuscript
  • HOME
  • CONTENT
    • Early Release
    • Featured
    • Current Issue
    • Issue Archive
    • Collections
    • Podcast
  • ALERTS
  • FOR AUTHORS
    • Information for Authors
    • Fees
    • Journal Clubs
    • eLetters
    • Submit
  • EDITORIAL BOARD
  • ABOUT
    • Overview
    • Advertise
    • For the Media
    • Rights and Permissions
    • Privacy Policy
    • Feedback
  • SUBSCRIBE
PreviousNext
Articles

Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension

LW Jin, H Ninomiya, JM Roch, D Schubert, E Masliah, DA Otero and T Saitoh
Journal of Neuroscience 1 September 1994, 14 (9) 5461-5470; DOI: https://doi.org/10.1523/JNEUROSCI.14-09-05461.1994
LW Jin
Department of Neurosciences, School of Medicine, University of California, San Diego, La Jolla 92093–0624.
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
H Ninomiya
Department of Neurosciences, School of Medicine, University of California, San Diego, La Jolla 92093–0624.
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
JM Roch
Department of Neurosciences, School of Medicine, University of California, San Diego, La Jolla 92093–0624.
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
D Schubert
Department of Neurosciences, School of Medicine, University of California, San Diego, La Jolla 92093–0624.
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
E Masliah
Department of Neurosciences, School of Medicine, University of California, San Diego, La Jolla 92093–0624.
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
DA Otero
Department of Neurosciences, School of Medicine, University of California, San Diego, La Jolla 92093–0624.
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
T Saitoh
Department of Neurosciences, School of Medicine, University of California, San Diego, La Jolla 92093–0624.
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • Article
  • Info & Metrics
  • eLetters
  • PDF
Loading

Abstract

Amyloid beta/A4 protein precursor (APP) is secreted into medium by most cultured cells and can function as an autocrine factor. To study the biological function of secreted forms of APP (sAPP) on neurons, we used a clonal CNS neuronal line, B103, which does not synthesize detectable levels of APP. B103 cells transfected with APP construct developed neurites faster than the parent B103 cells when plated in a serum-free defined medium. Neurite outgrowth of B103 cells was promoted by the conditioned medium of APP-695-over-producing cells or by the bacteria- produced sAPP-695 (named KB75). A series of peptides having sequences between Ala-319 and Met-335 of APP-695 also stimulated neurite outgrowth of B103 cells. The sequence of five amino acids, RERMS (APP 328–332), within this stretch of sequence, was the shortest active peptide, although the concentration required for the neuritotropic activity was higher than that of KB75. Binding assay using 125I-labeled APP 17-mer peptide corresponding to Ala-319 to Met-335 of APP-695 as a ligand demonstrated specific and saturable cell-surface binding sites. The predicted KD value was 20 +/- 5 nM and the Bmax value was 80 +/- 8 fmol/10(6) cells. The binding could be displaced with KB75. A 17-mer peptide with reverse sequence neither induced neurite outgrowth nor competed for the binding. A bacteria-produced sAPP fragment lacking the active 17-mer sequence (named KB75 delta) did not compete with 125I- labeled 17-mer for binding or stimulate neurite extension. A peptide of sequence RMSQ (APP 330–333), which partially overlaps the active sequence RERMS, could block the neuritotropic effects of both KB75 and the 17-mer at higher concentrations. APP 17-mer was also found to induce the accumulation of inositol polyphosphates, suggesting that the APP 17-mer effects involve activation of inositol phospholipid signal transduction systems. These data indicate that sAPP induces neurite extension through cell-surface binding and that the domain containing the RERMS sequence (APP 328–332) represents the active site responsible for this function.

Back to top

In this issue

The Journal of Neuroscience: 14 (9)
Journal of Neuroscience
Vol. 14, Issue 9
1 Sep 1994
  • Table of Contents
  • Table of Contents (PDF)
  • Index by author
Email

Thank you for sharing this Journal of Neuroscience article.

NOTE: We request your email address only to inform the recipient that it was you who recommended this article, and that it is not junk mail. We do not retain these email addresses.

Enter multiple addresses on separate lines or separate them with commas.
Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension
(Your Name) has forwarded a page to you from Journal of Neuroscience
(Your Name) thought you would be interested in this article in Journal of Neuroscience.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
View Full Page PDF
Citation Tools
Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension
LW Jin, H Ninomiya, JM Roch, D Schubert, E Masliah, DA Otero, T Saitoh
Journal of Neuroscience 1 September 1994, 14 (9) 5461-5470; DOI: 10.1523/JNEUROSCI.14-09-05461.1994

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
Respond to this article
Request Permissions
Share
Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension
LW Jin, H Ninomiya, JM Roch, D Schubert, E Masliah, DA Otero, T Saitoh
Journal of Neuroscience 1 September 1994, 14 (9) 5461-5470; DOI: 10.1523/JNEUROSCI.14-09-05461.1994
del.icio.us logo Digg logo Reddit logo Twitter logo Facebook logo Google logo Mendeley logo
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Jump to section

  • Article
  • Info & Metrics
  • eLetters
  • PDF

Responses to this article

Respond to this article

Jump to comment:

No eLetters have been published for this article.

Related Articles

Cited By...

More in this TOC Section

  • Choice Behavior Guided by Learned, But Not Innate, Taste Aversion Recruits the Orbitofrontal Cortex
  • Maturation of Spontaneous Firing Properties after Hearing Onset in Rat Auditory Nerve Fibers: Spontaneous Rates, Refractoriness, and Interfiber Correlations
  • Insulin Treatment Prevents Neuroinflammation and Neuronal Injury with Restored Neurobehavioral Function in Models of HIV/AIDS Neurodegeneration
Show more Articles
  • Home
  • Alerts
  • Visit Society for Neuroscience on Facebook
  • Follow Society for Neuroscience on Twitter
  • Follow Society for Neuroscience on LinkedIn
  • Visit Society for Neuroscience on Youtube
  • Follow our RSS feeds

Content

  • Early Release
  • Current Issue
  • Issue Archive
  • Collections

Information

  • For Authors
  • For Advertisers
  • For the Media
  • For Subscribers

About

  • About the Journal
  • Editorial Board
  • Privacy Policy
  • Contact
(JNeurosci logo)
(SfN logo)

Copyright © 2022 by the Society for Neuroscience.
JNeurosci Online ISSN: 1529-2401

The ideas and opinions expressed in JNeurosci do not necessarily reflect those of SfN or the JNeurosci Editorial Board. Publication of an advertisement or other product mention in JNeurosci should not be construed as an endorsement of the manufacturer’s claims. SfN does not assume any responsibility for any injury and/or damage to persons or property arising from or related to any use of any material contained in JNeurosci.