Catarina Rippe, et al. Effect of high-fat diet, surrounding
temperature, and enterostatin on uncoupling protein gene expression.
Am J Physiol Endocrinol Metab. 2000 Aug;279(2):E293-E300.
Lin L, et al. Enterostatin suppresses food intake in
rats after near-celiac and intracarotid arterial injection.
Am J Physiol Regul Integr Comp Physiol 2000 May;278(5):R1346-51.
Prasad C, et al. Hyperenterostatinemia in premenopausal
obese women. J Clin Endocrinol Metab 1999 Mar;84(3):937-41.
Enterostatins [Val-Pro-Asp-Pro-Arg (VPDPR), Val-Pro-Gly-Pro-Arg
(VPGPR), and Ala-Pro-Gly-Pro-Arg (APGPR)] are pentapeptides
derived from the NH2-terminus of procolipase after tryptic
cleavage and belong to the family of gut-brain peptides. Although
enterostatin-like immunoreactivities exist in blood, brain,
and gut, and exogenous enterostatins decrease fat appetite
and insulin secretion in rats, the roles of these peptides
in human obesity remain to be examined. To determine whether
VPDPR and APGPR secretion is altered in obesity, serum VPDPR
and APGPR levels were measured in 38 overnight-fasted subjects
(body mass index, 17.9-54.7 kg/m2) before and after a meal.
The mean fasting VPDPR in the serum of lean subjects was significantly
lower than that in obese subjects [lean = 603 +/- 86 nmol/L
(n = 17); obese, 1516 +/- 227 nmol/L (n = 21); P = 0.0023].
In addition, the rise in serum APGPR after a meal (postmeal/fasting
ratio) was significantly higher in lean than in obese subjects
[lean, 1.71 +/- 0.24 (n = 17); obese, 1.05 +/- 0.14 (n = 21);
P = 0.0332]. The results of these studies show hyperenterostatinemia
in obesity and a diminution in enterostatin secretion after
satiety.
Berger K, et al. Mitochondrial ATP synthase--a possible
target protein in the regulation of energy metabolism in vitro
and in vivo. Nutr Neurosci 2002 Jun;5(3):201-10
The increasing prevalence of obesity in the Western world
has stimulated an intense search for mechanisms regulating
food intake and energy balance. A number of appetite-regulating
peptides have been identified, their receptors cloned and
the intracellular events characterized. One possible energy-dissipating
mechanism is the mitochondrial uncoupling of ATP-synthesis
from respiratory chain oxidation through uncoupling proteins,
whereby energy derived from food could be dissipated as heat,
instead of stored as ATP. The exact role of the uncoupling
proteins in energy balance is, however, uncertain. We show
here that mitochondrial F1F0-ATP synthase itself is a target
protein for an anorectic peptide, enterostatin, demonstrated
both after affinity purification of rat brain membranes and
through a direct physical interaction between enterostatin
and purified F1-ATP synthase. In insulinoma cells (INS-1)
enterostatin was found to target F1F0-ATP synthase, causing
an inhibition of ATP production, an increased thermogenesis
and increased oxygen consumption. The experiments suggest
a role of mitochondrial F1F0-ATP synthase in the suppressed
insulin secretion induced by enterostatin. It could be speculated
that this targeting mechanism is involved in the decreased
energy efficiency following enterostatin treatment in rat.
RIA Assay for Enterostatin
Imamura
M, et al. Distribution and characterization of
enterostatin-like immunoreactivity in human cerebrospinal
fluid. Peptides. 1998;19(8):1385-91.
Imamura
M., et al. On the nature and distribution of enterostatin
(Val-Asp-Pro-Asp-Arg)-like immunoreactivity in rat plasma.
Peptides. 1999;20(1):133-9.
Prasad C, et al.Hyperenterostatinemia in premenopausal
obese women. J Clin Endocrinol Metab 1999 Mar;84(3):937-41
