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VGF Metabolic-related Gene: Distribution of Its Derived Peptides in Mammalian Pancreatic Islets

Cristina Cocco, Carla Brancia, Ivo Pirisi, Filomena D'Amato, Barbara Noli, Roberta Possenti and Gian-Luca Ferri

NEF-Laboratory, Department of Cytomorphology, University of Cagliari, Monserrato, Italy (CC,CB,IP,FDA,BN,G-LF), and Department of Neuroscience, University of Tor Vergata, Rome, Italy (RP)

Correspondence to: Cristina Cocco, Dept. of Cytomorphology, Cittadella Universitaria, 09042 Monserrato (Cagliari), Italy. E-mail: cristina.cocco{at}unica.it

The vgf gene has been shown to be involved in several metabolic pathways. Because the pancreas is crucial to metabolism and food intake, we studied the VGF peptides in bovine, rat, and pig Langherans islets using antisera raised against specific sites along the primary sequence of the rat/mouse and human VGF protein precursor. Whereas almost all of the pancreatic endocrine cells expressed vgf mRNA, when using the VGF antisera a different staining pattern became apparent. VGF_556–565 and VGF_282–291 immunoreactivity were exclusively found in somatostatin-producing cells, whereas the human C-terminus antiserum selectively immunolabeled glucagon and pancreatic polypeptide cells. The same cells were decorated with the VGF_443–588 antiserum, which also weakly labeled ß insulin-secreting cells. Finally, the VGF_298–306 peptide and the rat C terminus were found in virtually all pancreatic endocrine cells. Using bovine, swine, and rat pancreatic extracts, data from chromatography and ELISA assay showed the presence of a high molecular mass form compatible with the proVGF and lower molecular mass fractions corresponding to short VGF peptides. In conclusion, selective VGF distribution may suggest a multifaceted cell type-specific processing of proVGF, resulting in different peptides probably involved in neuroendocrine regulatory metabolic mechanisms. (J Histochem Cytochem 55:619–628, 2007)

Key Words: VGF • pancreas • immunohistochemistry • hormones • insulin • glucagon • pancreatic polypeptide • somatostatin

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