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 beta-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)(2)cAMP (1 mM), and a 6-fold increase was seen after phorbol la-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.

Possenti, R., Rinaldi, A.m., Ferri, G., Borboni, P., Trani, E., Levi, A. (1999). Expression, processing, and secretion of the neuroendocrine VGF peptides by INS-1 cells. ENDOCRINOLOGY, 140(8), 3727-3735.

Expression, processing, and secretion of the neuroendocrine VGF peptides by INS-1 cells

POSSENTI, ROBERTA;RINALDI, ANNA MARIA;BORBONI, PATRIZIA;
1999-01-01

Abstract

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 beta-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)(2)cAMP (1 mM), and a 6-fold increase was seen after phorbol la-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.
1999
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/09 - FISIOLOGIA
English
Con Impact Factor ISI
NERVE GROWTH-FACTOR; PANCREATIC BETA-CELLS; MOLECULAR-CLONING; ENDOCRINE PANCREAS; PROMOTER REGION; GENE-EXPRESSION; LINE; PROTEIN; ACID; IDENTIFICATION
Possenti, R., Rinaldi, A.m., Ferri, G., Borboni, P., Trani, E., Levi, A. (1999). Expression, processing, and secretion of the neuroendocrine VGF peptides by INS-1 cells. ENDOCRINOLOGY, 140(8), 3727-3735.
Possenti, R; Rinaldi, Am; Ferri, G; Borboni, P; Trani, E; Levi, A
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/56953
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