BJPST: 15(2): 001-008 [July, 2017]
VGF (a non-acronymic name) a ~68 kDa neurosecretory protein, belongs to the extended granin family of proteins, initially identified as a nerve growth factor (NGF) inducible gene product, is selectively synthesised mostly in neuronal and neuroendocrine cells. Due to the presence of paired basic amino acid residues (R – Arginine, and K – Lysine), the VGF sequence undergoes endoproteolytic cleavage to produce several smaller peptides, released upon stimulation via the regulated secretory pathway both in vitro and in vivo. There are data suggesting that the VGF-derived peptides are the biologically active, stored in dense core vesicles and secreted in order to play a role in inter cellular communication, and responsible for the diverse range of biological functions associated with VGF. Several of these VGF-derived peptides have been characterised and are involved in energy balance, reproductive behaviour, pain modulation, mood order, etc. In this review the most important findings regarding the VGF derived peptides, structure, tissue distribution and functions of VGF have been summarized, mentioning its future perspective.
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