Abstract |
The neuroendocrine secretory protein chromogranin A (CgA) is a precursor for various biologically active peptides. Several single and paired basic residues are present within its primary amino acid sequence comprising cleavage sites for prohormone convertases. In this study, SH-SY5Y human neuroblastoma cells were stably transfected with the prohormone convertase PC2 to analyse the proteolytic processing of endogenous chromogranin A and, in particular, the formation of the chromogranin-A-derived peptide GE-25. Our analyses revealed a significant change in the pattern of proteolytic conversion of chromogranin A in cells expressing PC2. Mock-transfected control cells contained mainly the intact chromogranin A molecule and hardly any shorter products were found. On the other hand, PC2-transfected cells showed extensive processing of chromogranin A, resulting in significantly lower amounts of the intact precursor and especially high levels of the free peptide GE-25.
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Authors | Alfred Doblinger, Alexandra Becker, Nabil G Seidah, Andrea Laslop |
Journal | Regulatory peptides
(Regul Pept)
Vol. 111
Issue 1-3
Pg. 111-6
(Mar 28 2003)
ISSN: 0167-0115 [Print] Netherlands |
PMID | 12609757
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright 2002 Elsevier Science B.V. |
Chemical References |
- CHGA protein, human
- Chromogranin A
- Chromogranins
- Neoplasm Proteins
- Peptide Fragments
- Proprotein Convertase 2
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Topics |
- Blotting, Northern
- Chromogranin A
- Chromogranins
(metabolism)
- Cloning, Molecular
- Humans
- Immunoblotting
- Neoplasm Proteins
(genetics, metabolism)
- Neuroblastoma
(metabolism)
- Peptide Fragments
(metabolism)
- Proprotein Convertase 2
(genetics, metabolism)
- Protein Processing, Post-Translational
- Radioimmunoassay
- Transfection
- Tumor Cells, Cultured
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