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Expression, Processing, and Secretion of the Neuroendocrine VGF Peptides by INS-1 Cells¹

Departments of Neuroscience (R.P., A.M.R., E.T.) and Internal Medicine (P.B.), University of Tor Vergata, 00133 Rome; the Department of Cytomorphology, University of Cagliari (G.-L.F.), 09124 Cagliari; and the Institute of Neurobiology, National Research Council (R.P., A.M.R., E.T., A.L.), 00137 Rome, Italy

Address all correspondence and requests for reprints to: Dr. Roberta Possenti and Andrea Levi, Institute of Neurobiology, National Research Center, Via Carlo Marx 15, 00137 Rome, Italy. E-mail: r.possenti{at}in.rm.cnr.it alevi@in.rm.cnr.it.

The neurotropin-inducible gene vgf is expressed in neuronal and endocrine tissues. It encodes a secretory protein that is proteolytically processed in neuronal cells to low molecular mass polypeptides. In the present report, we show that vgf is expressed in different insulinoma cell lines and in normal rat pancreatic islets. In the insulinoma-derived ß-cell line INS-1, vgf messenger RNA was transcriptionally up-regulated by increased levels of intracellular cAMP, but not by the addition of glucose (20 mM) or phorbol 12-myristate 13-acetate (100 nM). Furthermore, nerve growth factor failed to stimulate vgf gene expression. In INS-1 cells, the VGF protein was shown to be processed in a post endoplasmic reticulum compartment to produce a peptide profile similar to that seen in neurons. The release of such VGF peptides occurred at a low rate in the absence of secretory stimuli (<2%/h). A 3-fold increase in the rate of release was seen after the addition of glucose (15 mM), a 4-fold increase was seen after (Bu)₂cAMP (1 mM), and a 6-fold increase was seen after phorbol 12-myristate 13-acetate (100 nM). These results indicated that insulin-containing cells produce VGF-derived peptides that are released via a regulated pathway in response to insulin secretagogues.

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