JCB logo
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 598K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dicou, E.
Right arrow Articles by Harvie, D.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Dicou, E.
Right arrow Articles by Harvie, D.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/1997//389 $5.00
The Journal of Cell Biology, Volume 136, Number 2, , 1997 389-398

Article

Two Peptides Derived from the Nerve Growth Factor Precursor Are Biologically Active



Eleni Dicou*, Beth Pflug{ddagger}, Marilyn Magazin§, Thérèse Lehy||, Daniel Djakiew{ddagger}, Pascual Ferrara§, Véronique Nerrière*, and Douglas Harvie*

* Institut National de la Santé et de la Recherche Médicale U298, Centre Hospitalier Universitaire, Angers 49033, France; {ddagger} Department of Cell Biology, Georgetown University Medical Center, Washington DC, 20007; § Sanofi Recherche, 31676 Labège, France; and || Institut National de la Santé et de la Recherche Médicale U10, Hôpital Bichat, 75877 Paris, Cedex 18, France

This report provides evidence that the proregion of the NGF precursor protein contains two novel bioactive peptides. The presence of pairs of basic amino acid (aa) residues in the NGF proregion suggests that two or three peptides other than NGF may be generated by proteolytic cleavage. Synthetic peptides of 29 aa (LIP1) and 38aa (LIP2) corresponding to the sequences –71 to –43 and –40 to –3 of the proNGF, respectively, were used in this study. ELISA specific for these two peptides revealed their presence in the rat intestine. LIP1 was localized by immunohistochemistry in endocrine cells of the intestinal epithelium, and LIP2 was immunoprecipitated from an intestinal extract. We also provide evidence for the presence of specific receptors for LIP2 in several cell lines. Scatchard analysis indicated the presence of a low affinity binding site with a Kd of ~10–7 M and a high affinity binding site of 10–9 M. Cross-linking studies revealed receptor forms of about 140 kD and 93 kD in a prostatic adenocarcinoma cell line.

LIP1 and LIP2 induced rapid F-actin redistribution in PC12 cells within 2 min of incubation, which suggests a role of LIP1 and LIP2 in the process of neurite outgrowth. Furthermore, both propeptides induced rapid tyrosine phosphorylation of the Trk protein in both prostatic adenocarcinoma cells and PC12 cells, thus implicating trk in their mechanism of action. These results support our hypothesis that two peptides within the NGF precursor protein are biologically active.

Abbreviations used in this paper: aa, amino acid; ChAT, choline acetyltransferase; DRG, dorsal root ganglia; F-actin, filamentous actin; MSG, mouse submaxillary gland; NT, neurotrophin; PS, proteolytic site.

Please address all correspondence to Eleni Dicou, INSERM U10, Hopital Bichat, 170 Boulevard Ney, 75877 Paris, Cedex 18, France. Tel.: 33-1-4025-83-09. Fax.: 33-1-46-27-85-36.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents