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J Biol Chem, Vol. 275, Issue 15, 10745-10753, April 14, 2000
From Vasostatin-1, the natural N-terminal 1-76
chromogranin A (CGA)-derived fragment in bovine sequence, has been
purified from chromaffin secretory granules and identified by
sequencing and matrix-assisted laser desorption time-of-flight mass
spectrometry. This peptide, which displays antibacterial activity
against Gram-positive bacteria at micromolar concentrations, is also
able to kill a large variety of filamentous fungi and yeast cells in
the 1-10 µM range. We have found that the
C-terminal moiety of vasostatin-1 is essential for the antifungal
activity, and shorter active peptides have been synthesized. In
addition, from the comparison with the activity displayed by related
peptides (human recombinant and rat synthetic fragments), we could
determine that antibacterial and antifungal activities have different
structural requirements. To assess for such activities in
vivo, CGA and CGA-derived fragments were identified in secretory
material released from human polymorphonuclear neutrophils upon
stimulation. Vasostatin-1, which is stored in a large variety of cells
(endocrine, neuroendocrine, and neurons) and which is liberated from
stimulated chromaffin and immune cells upon stress, may represent a new
component active in innate immunity.
Antibacterial and Antifungal Activities of Vasostatin-1, the
N-terminal Fragment of Chromogranin A*
,,,
,, and**
INSERM Unité 338, "Biologie de la
Communication Cellulaire," 5 Rue Blaise Pascal 67084 Strasbourg
Cedex, France, § Department of Biological and Technological
Research, San Raffaele Scientific Institute, 20132 Milan, Italy,
¶ CNRS UPR 4301, Centre de Biophysique Moléculaire, Rue
Charles Sadron, 45071 Orléans, France, and CNRS,
UPR 9022, Institut de Biologie Moléculaire et Cellulaire, 15 Rue
René Descartes, 67084 Strasbourg Cedex, France
*
This work was funded by INSERM and supported by grants from
Meiji Institute of Health Science (Odawara, Japan), the Direction des
Recherches, Etudes et Techniques Grant DRET 96-099 (to D. A.),
Université Louis-Pasteur Contrats Pluriformation 93-96 and 97-2000 (to D. A.), the Ligue Contre le Cancer (to M. H. M. B.), the Association Recherche et Partage (to K. L.), the Fondation pour la
Recherche Médicale (to K. L.), and the Région Alsace (to
Y. G.).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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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