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Tissue-specific processing of the neuroendocrine protein VGF
E Trani1, T Ciotti, A M Rinaldi
1Departimento di Medicina Sperimentale e Scienze Biochimiche, Università di Tor Vergata, Roma, Italy.
Journal of Neurochemistry
|December 1, 1995
Summary
The VGF gene product is processed into smaller peptides in neuroendocrine tissues, particularly in nerve cells. These VGF peptides are released upon cell stimulation, suggesting a role in neuronal communication.
Area of Science:
- Neuroendocrinology
- Molecular Biology
- Cell Biology
Background:
- VGF is a neuroendocrine-specific gene product.
- Nerve growth factor (NGF) up-regulates VGF in PC12 cells.
- VGF undergoes post-translational modifications.
Purpose of the Study:
- To investigate the post-translational processing of VGF.
- To identify the biologically relevant forms of VGF.
- To explore the role of VGF in neuronal communication.
Main Methods:
- Antibody-based detection of VGF polypeptides in rat neuroendocrine tissues.
- Analysis of VGF processing in PC12 cells and primary rat cerebellar granule cells.
- Investigation of VGF secretion upon cell depolarization.
Main Results:
- Two VGF polypeptides (90 and 80 kDa) detected using N-terminal antiserum.
- Several additional VGF products, including 20, 18, and 10 kDa peptides, identified with C-terminal antiserum.
- Low-molecular-weight VGF forms accumulated during in vitro maturation of cerebellar granule cells.
- VGF processing and secretion occurred in a regulated manner, enriched in secretory vesicles.
Conclusions:
- VGF is differentially processed into various peptides in neuroendocrine tissues.
- Specific VGF cleavage occurs post-ER and is regulated by NGF.
- Secreted VGF peptides may play a role in neuronal communication.