© Springer International Publishing AG 2017 229
T. Angelone et al. (eds.), Chromogranins: from Cell Biology to Physiology
and Biomedicine, UNIPA Springer Series, DOI 10.1007/978-3-319-58338-9_14
Action and Mechanisms of Action
of the Chromogranin A Derived Peptide
Pancreastatin
N.E. Evtikhova, A. Pérez-Pérez, C. Jiménez-Cortegana,
A. Carmona- Fernández, T. Vilariño-García, and V. Sánchez-Margalet
Abstract Pancreastatin (PST), is a biologically active peptide isolated from por-
cine pancreas in 1986. Soon after PST was found to be contained within the chro-
mogranin A (CGA) sequence, and therefore distributed throughout the
neuroendocrine and gastrointestinal systems. This finding started up the consider-
ation of CGA as a source of different biologically active peptides, which were then
identified.
Even though many metabolic effects, such as the modulation of secretion of dif-
ferent glands, as well as the general metabolism regulation, have been described, the
definitive picture of the physiological role of PST has not yet been established.
Nevertheless, the sum of these metabolic effects, forged the name of PST as a dys-
glycemic peptide, with conterregulatory effects on insulin action. Thus, elevated
circulating levels of PST have been found in Type 2 diabetes, gestational diabetes
and essential hypertension, suggesting that PST is a negative regulator of insulin
sensitivity and glucose homeostasis. The mechanism of action whereby PST could
modulate insulin action has been thoroughly studied in various cellular systems (rat
liver cells and adipocytes), and G coupled protein nature of the receptor has been
established. But, although the purification process is able to yield some amount of
PST binding protein, the final characterization of such PST receptor have been elu-
sive so far. On the other hand, a different kind of receptor for PST has been pro-
posed, and it may be the surface chaperone GRP78. Therefore, PST could modulate
the energy metabolism through different mechanisms, such as insulin signaling
antagonism, and as a protein folding regulator.
N.E. Evtikhova • A. Pérez-Pérez • C. Jiménez-Cortegana • A. Carmona-Fernández
T. Vilariño-García • V. Sánchez-Margalet (*)
Department of Clinical Biochemistry, Virgen Macarena University Hospital,
School of Medicine, University of Seville, Seville, Spain
e-mail: [email protected]