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Volume 272, Number 18, Issue of May 2, 1997 pp. 11928-11936
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Phosphorylation and O-Glycosylation Sites of Bovine Chromogranin A from Adrenal Medullary Chromaffin Granules and Their Relationship with Biological Activities

(Received for publication, December 19, 1996, and in revised form, February 27, 1997)

Jean-Marc Strub , Odile Sorokine ^§ , Alain Van Dorsselaer ^§ , Dominique Aunis and Marie-Hélène Metz-Boutigue

From the  Institut National de la Santé et de la Recherche Médicale, Unité 338 de Biologie de la Communication Cellulaire, 67084 Strasbourg Cedex, France and ^§ Centre National de la Recherche Scientifique, Laboratoire de Spectrométrie de Masse Bioorganique, URA 31, Chimie Organique des Substances Naturelles, 67084 Strasbourg Cedex, France

Bovine adrenal medullary chromogranin A, the major soluble component of chromaffin granules, is a phosphorylated glycoprotein. In the present work, phosphorylation and glycosylation sites were determined using mild proteolysis, peptide separation, microsequencing, and mass analysis by electrospray and matrix-assisted laser desorption ionization time-of-flight techniques. Seven post-translational modification sites were detected. Two O-linked glycosylation sites, each consisting of the trisaccharide NeuAc2-3Gal1-3GalNAc1, were located in the middle part of the protein, on Ser¹⁸⁶ and on Thr²³¹. The former residue is present in the antibacterial peptide named chromacin. Four phosphorylation sites were located on serine residues at positions Ser⁸¹ in the N-terminal region of the protein and Ser³⁰⁷, Ser³⁷², and Ser³⁷⁶ in the C-terminal end. One additional phosphorylation site was found on the tyrosine residue at position Tyr¹⁷³, the N-terminal amino acid of chromacin. With the exception of the phosphorylation on Tyr¹⁷³, all of the other post-translational modifications are located on highly conserved chromogranin A regions, implying some biological importance.

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