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
    • Special Collections
  • EDITORIAL BOARD
    • Editorial Board
    • ECR Advisory Board
    • Journal Staff
  • ABOUT
    • Overview
    • Advertise
    • For the Media
    • Rights and Permissions
    • Privacy Policy
    • Feedback
    • Accessibility
  • SUBSCRIBE

User menu

  • Log out
  • Log in
  • My Cart

Search

  • Advanced search
Journal of Neuroscience
  • Log out
  • 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
    • Special Collections
  • EDITORIAL BOARD
    • Editorial Board
    • ECR Advisory Board
    • Journal Staff
  • ABOUT
    • Overview
    • Advertise
    • For the Media
    • Rights and Permissions
    • Privacy Policy
    • Feedback
    • Accessibility
  • SUBSCRIBE
PreviousNext
Articles

The major 35S-methionine-labeled rapidly transported protein (superprotein) is identical to SNAP-25, a protein of synaptic terminals

A Loewy, WS Liu, C Baitinger and MB Willard
Journal of Neuroscience 1 November 1991, 11 (11) 3412-3421; https://doi.org/10.1523/JNEUROSCI.11-11-03412.1991
A Loewy
Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110.
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
WS Liu
Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110.
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
C Baitinger
Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110.
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
MB Willard
Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110.
  • 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

Superprotein is a rapidly axonally transported protein that is conspicuously labeled with 35S-methionine supplied to the cell bodies of retinal ganglion cells. Superprotein candidates are apparent among the rapidly transported proteins of many neurons from the CNS and PNS, including cranial, sympathetic, sensory, and motor neurons from mammals, fish, and amphibians. To determine the identity of Superprotein, we purified it from rabbit visual system and spinal cord and determined the amino acid sequence of seven of its tryptic peptides. The sequence shows that Superprotein is SNAP-25, a protein recently predicted from a cDNA sequence; SNAP-25 has been reported to be concentrated in the synaptic terminals of a selected population of CNS neurons. We measured the amount of radioactivity associated with Superprotein in tissue containing axons (optic tract) and synaptic terminals (superior collicules) of rabbit retinal ganglion cells. Labeled Superprotein disappeared from the superior colliculus more rapidly than another protein (synapsin I-like protein) that is concentrated in synaptic terminals. These results serve to unite the observations on the synthesis, distribution, metabolism, and axonal transport of Superprotein with observations of SNAP-25 and its mRNA.

Back to top

In this issue

The Journal of Neuroscience: 11 (11)
Journal of Neuroscience
Vol. 11, Issue 11
1 Nov 1991
  • 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.
The major 35S-methionine-labeled rapidly transported protein (superprotein) is identical to SNAP-25, a protein of synaptic terminals
(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
The major 35S-methionine-labeled rapidly transported protein (superprotein) is identical to SNAP-25, a protein of synaptic terminals
A Loewy, WS Liu, C Baitinger, MB Willard
Journal of Neuroscience 1 November 1991, 11 (11) 3412-3421; DOI: 10.1523/JNEUROSCI.11-11-03412.1991

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
The major 35S-methionine-labeled rapidly transported protein (superprotein) is identical to SNAP-25, a protein of synaptic terminals
A Loewy, WS Liu, C Baitinger, MB Willard
Journal of Neuroscience 1 November 1991, 11 (11) 3412-3421; DOI: 10.1523/JNEUROSCI.11-11-03412.1991
Twitter logo Facebook 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

  • Memory Retrieval Has a Dynamic Influence on the Maintenance Mechanisms That Are Sensitive to ζ-Inhibitory Peptide (ZIP)
  • Neurophysiological Evidence for a Cortical Contribution to the Wakefulness-Related Drive to Breathe Explaining Hypocapnia-Resistant Ventilation in Humans
  • Monomeric Alpha-Synuclein Exerts a Physiological Role on Brain ATP Synthase
Show more Articles
  • Home
  • Alerts
  • Follow SFN on BlueSky
  • 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 Notice
  • Contact
  • Accessibility
(JNeurosci logo)
(SfN logo)

Copyright © 2025 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.