Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M007557200 on September 14, 2000

J. Biol. Chem., Vol. 275, Issue 49, 38355-38362, December 8, 2000
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
275/49/38355    most recent
M007557200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Goumon, Y.
Right arrow Articles by Metz-Boutigue, M.-H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Goumon, Y.
Right arrow Articles by Metz-Boutigue, M.-H.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Processing of Proenkephalin-A in Bovine Chromaffin Cells
IDENTIFICATION OF NATURAL DERIVED FRAGMENTS BY N-TERMINAL SEQUENCING AND MATRIX-ASSISTED LASER DESORPTION IONIZATION-TIME OF FLIGHT MASS SPECTROMETRY*

Yannick GoumonDagger , Karine LugardonDagger , Patrice GadroyDagger , Jean-Marc StrubDagger , Ingeborg D. Welters§, George B. Stefano, Dominique AunisDagger , and Marie-Hélène Metz-BoutigueDagger ||

From the Dagger  INSERM Unité 338, Biologie de la Communication Cellulaire, 67084 Strasbourg, France, the § Department of Anaesthesiology and Intensive Care Medicine, Rudolf-Buchenhheim-Strasse 7, Justus-Liebig-Universitat Giessen, 35385 Giessen, Germany, and the  Neuroscience Research Institute, State University of New York, Old Westbury, New York 11568

A large variety of proenkephalin-A-derived peptides (PEAPs) are present in bovine adrenal medulla secretory granules that are cosecreted with catecholamines upon stimulation of chromaffin cells. In the present paper, after reverse phase high performance liquid chromatography of intragranular soluble material, PEAPs were immunodetected with antisera raised against specific proenkephalin-A (PEA) sequences (PEA63-70 and PEA224-237) and analyzed by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry. Thirty PEAPs were characterized in addition to enkephalins and whole PEA, indicating that preferential proteolytic attacks occurred at both N- and C-terminal regions. A similar approach was used to characterize PEA-derived fragments exocytotically released into the extracellular space that showed five additional minor PEAPs. Among all these naturally generated peptides, enkelytin, the antibacterial bisphos- phorylated C-terminal peptide (PEA209-237), was predominantly generated, as shown by MALDI-TOF mass spectrometry analysis, which constituted an efficient method for its identification. Finally, the data on PEA intragranular and extracellular processing in adrenal medulla are discussed in regard to the known enzymatic processing mechanisms. We note the high conservation of the cleavage points in evolutionarily diverse organisms, highlighting an important biological function for the released PEAPs.

* This work was supported by funds from the INSERM U.338, the Université Louis-Pasteur de Strasbourg (Pôle Neurosciences; Contrat pluriformation 97-00), the Ligue Départementale contre le Cancer (to M.-H. M.-B.), the Association Recherche et Partage (Ph.D. fellowship to K. L.), and Direction des Recherches, Etudes et Techniques Contract 96-099 (to D. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Unité INSERM U-338, 5, rue Blaise Pascal, 67084 Strasbourg Cedex, France. Tel.: 33-3-88-45-66-09; Fax: 33-3-88-60-08-06; E-mail: metz@neurochem. u-strasbg.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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 Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 FASEB J.Home page
M. C. Cerra, M. P. Gallo, T. Angelone, A. M. Quintieri, E. Pulera, E. Filice, B. Guerold, P. Shooshtarizadeh, R. Levi, R. Ramella, et al.
The homologous rat chromogranin A1-64 (rCGA1-64) modulates myocardial and coronary function in rat heart to counteract adrenergic stimulation indirectly via endothelium-derived nitric oxide
FASEB J, November 1, 2008; 22(11): 3992 - 4004.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Goumon, A. Muller, E. Glattard, C. Marban, C. Gasnier, J.-M. Strub, S. Chasserot-Golaz, O. Rohr, G. B. Stefano, I. D. Welters, et al.
Identification of Morphine-6-glucuronide in Chromaffin Cell Secretory Granules
J. Biol. Chem., March 24, 2006; 281(12): 8082 - 8089.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Goumon, T. Angelone, F. Schoentgen, S. Chasserot-Golaz, B. Almas, M. M. Fukami, K. Langley, I. D. Welters, B. Tota, D. Aunis, et al.
The Hippocampal Cholinergic Neurostimulating Peptide, the N-terminal Fragment of the Secreted Phosphatidylethanolamine-binding Protein, Possesses a New Biological Activity on Cardiac Physiology
J. Biol. Chem., March 26, 2004; 279(13): 13054 - 13064.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
S. Yasothornsrikul, D. Greenbaum, K. F. Medzihradszky, T. Toneff, R. Bundey, R. Miller, B. Schilling, I. Petermann, J. Dehnert, A. Logvinova, et al.
Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter
PNAS, August 5, 2003; 100(16): 9590 - 9595.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement