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Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1996 Nov 08; Vol. 271 (45), pp. 28533-40. - Publication Year :
- 1996
-
Abstract
- Recently, we have isolated from bovine chromaffin granules and identified two natural peptides possessing antibacterial activity: secretolytin (chromogranin B 614-626) and enkelytin (proenkephalin-A 209-237). Here, we characterize a large natural fragment, corresponding to chromogranin A 79-431, that inhibits growth of both Gram-positive and Gram-negative bacteria. The aim of the present work was to determine the shortest active peptide located in the 79-431 chromogranin A region. Three peptides, which shared the same 173-194 chromogranin A sequence (YPGPQAKEDSEGPSQGPASREK) but differed in post-translational modifications, including O-glycosylation and tyrosine phosphorylation, were isolated. A detailed study using microsequencing and mass spectrometry allowed us to correlate their antibacterial activity with these post-translational modifications. The chromogranin A precursor fragment (79-431) and the active glycosylated and phosphorylated peptides were, respectively, named prochromacin and chromacin (P, G, and PG for phosphorylated, glycosylated, and phosphorylated-glycosylated form).
- Subjects :
- Amino Acid Sequence
Animals
Anti-Bacterial Agents pharmacology
Cattle
Chromatography, High Pressure Liquid
Chromogranin A
Chromogranins pharmacology
Glycosylation
Molecular Sequence Data
Peptide Fragments pharmacology
Phosphorylation
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Adrenal Medulla chemistry
Anti-Bacterial Agents chemistry
Chromaffin Granules chemistry
Chromogranins metabolism
Peptide Fragments metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 271
- Issue :
- 45
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 8910482
- Full Text :
- https://doi.org/10.1074/jbc.271.45.28533