help button home button Endocrine Society Molecular Endocrinology ENDO 08 Sessions Library
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Perez, F.
Right arrow Articles by Ayala, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Perez, F.
Right arrow Articles by Ayala, J.

Molecular Endocrinology, Vol 8, 1278-1287, Copyright © 1994 by Endocrine Society

ARTICLES

Rab3A and Rab3B carboxy-terminal peptides are both potent and specific inhibitors of prolactin release by rat cultured anterior pituitary cells

F Perez, PM Lledo, D Karagogeos, JD Vincent, A Prochiantz and J Ayala
CNRS URA 1414, Ecole Normale Superieure, Paris, France.

Chimeric polypeptides composed of the homeodomain of Antennapedia and of the C-terminus of several low molecular weight GTP-binding proteins of the rab family have been found to translocate through the membrane of cells in culture and to accumulate in the cytoplasm and nucleus. We have used these chimeric peptides to study, in intact endocrine cells, a putative role for the C-terminal domain of rab proteins in the exocytotic process. We show that the internalization of 33- and 32- amino acid polypeptides corresponding to the C-terminal domains of rab3A and rab3B blocks calcium-triggered PRL release from adult rat anterior pituitary cells maintained in primary culture. This effect is specific to rab3 since it is not observed after internalization of either rab1 or rab2 C-terminal peptides. In addition, we demonstrate that this inhibition does not require the geranylgeranylation of the internalized C-termini. As rab3B normally shows a permissive effect on exocytosis in PRL-secreting cells, we suggest that the C-terminal domains of rab3A and rab3B contain structural elements that compete with endogenous rab3 necessary for calcium-induced exocytosis.


This article has been cited by other articles:


Home page
 J. Immunol.Home page
G. G. Chikh, S. Kong, M. B. Bally, J.-C. Meunier, and M.-P. M. Schutze-Redelmeier
Efficient Delivery of Antennapedia Homeodomain Fused to CTL Epitope with Liposomes into Dendritic Cells Results in the Activation of CD8+ T Cells
J. Immunol., December 1, 2001; 167(11): 6462 - 6470.
[Abstract] [Full Text] [PDF]

Home page
 fake Crit Rev Oral Biol MedHome page
E.L. Watson
GTP-Binding Proteins and Regulated Exocytosis
Critical Reviews in Oral Biology & Medicine, January 1, 1999; 10(3): 284 - 306.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Shibata, W. Omata, Y. Suzuki, S. Tanaka, and I. Kojima
A Synthetic Peptide Corresponding to the Rab4 Hypervariable Carboxyl-terminal Domain Inhibits Insulin Action on Glucose Transport in Rat Adipocytes
J. Biol. Chem., April 19, 1996; 271(16): 9704 - 9709.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 1994 by The Endocrine Society