Making Anti-de Sitter Black Holes

It is known from the work of Banados et al. that a space-time with event horizons (much like the Schwarzschild black hole) can be obtained from 2+1 dimensional anti-de Sitter space through a suitable identification of points. We point out that this can be done in 3+1 dimensions as well. In this way we obtain black holes with event horizons that are tori or Riemann surfaces of genus higher than one. They can have either one or two asymptotic regions. Locally, the space-time is isometric to anti-de Sitter space.Comment: LaTeX, 10 pages, 6 postscript figures, uses epsf.te

The blunted effect of glucose-dependent insulinotropic polypeptide in subcutaneous abdominal adipose tissue in obese subjects is partly reversed by weight loss

BACKGROUND: Glucose-dependent insulinotropic polypeptide (GIP) appears to have impaired effect on subcutaneous abdominal adipose tissue metabolism in obese subjects. The aim of the present study was to examine whether weight loss may reverse the impaired effect of GIP on subcutaneous abdominal adipose tissue in obese subjects. METHODS: Five obese males participated in a 12-week weight loss program, which consisted of caloric restriction (800 Cal day(−)(1)) followed by 4 weeks of weight-maintenance diet. Before and after weight loss, subcutaneous adipose tissue lipid metabolism was studied by conducting regional measurements of arterio-venous plasma concentrations of metabolites and blood flow (adipose tissue blood flow, ATBF) across a segment of the abdominal adipose tissue in the fasting state and during GIP infusion (1.5 pmol kg(−)(1 )min(−)(1)) in combination with a hyperinsulinemic–hyperglycemic clamp. RESULTS: After weight loss (7.5±0.8 kg), glucose tolerance and insulin sensitivity increased significantly as expected. No significant differences were seen in basal ATBF before (1.3±0.4 ml min(−1) 100 g tissue(−1)) and after weight loss (2.1±0.4 ml min(−1) 100 g tissue)(−1); however, a tendency to increase was seen. After weight loss, GIP infusion increased ATBF significantly (3.2±0.1 ml min(−1) 100 g tissue(−1)) whereas there was no increase before weight loss. Triacylglycerol (TAG) uptake did not change after weight loss. Baseline free fatty acid (FFA) and glycerol output increased significantly after weight loss, P<0.001. During the clamp period, FFA and glycerol output declined significantly, P<0.05, with no differences before and after weight loss. Weight loss increased glucose uptake and decreased FFA/glycerol ratio during the clamp period, P<0.05. CONCLUSIONS: In obese subjects, weight loss, induced by calorie restriction, improves the blunted effect of GIP on subcutaneous abdominal adipose tissue metabolism

Ghrelin receptor (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

The ghrelin receptor (nomenclature as agreed by the NC-IUPHAR Subcommittee for the Ghrelin receptor [18]) is activated by a 28 amino-acid peptide originally isolated from rat stomach, where it is cleaved from a 117 amino-acid precursor (GHRL, Q9UBU3). The human gene encoding the precursor peptide has 83% sequence homology to rat prepro-ghrelin, although the mature peptides from rat and human differ by only two amino acids [70]. Alternative splicing results in the formation of a second peptide, [des-Gln14]ghrelin with equipotent biological activity [48]. A unique post-translational modification (octanoylation of Ser3, catalysed by ghrelin &#927;-acyltransferase (MBOAT4, Q96T53) [127] occurs in both peptides, essential for full activity in binding to ghrelin receptors in the hypothalamus and pituitary, and for the release of growth hormone from the pituitary [56]. Structure activity studies showed the first five N-terminal amino acids to be the minimum required for binding [4], and receptor mutagenesis has indicated overlap of the ghrelin binding site with those for small molecule agonists and allosteric modulators of ghrelin function [43]. In cell systems, the ghrelin receptor is constitutively active [44], but this is abolished by a naturally occurring mutation (A204E) that results in decreased cell surface receptor expression and is associated with familial short stature [88]

Ghrelin receptor in GtoPdb v.2021.3

The ghrelin receptor (nomenclature as agreed by the NC-IUPHAR Subcommittee for the Ghrelin receptor [19]) is activated by a 28 amino-acid peptide originally isolated from rat stomach, where it is cleaved from a 117 amino-acid precursor (GHRL, Q9UBU3). The human gene encoding the precursor peptide has 83% sequence homology to rat prepro-ghrelin, although the mature peptides from rat and human differ by only two amino acids [74]. Alternative splicing results in the formation of a second peptide, [des-Gln14]ghrelin with equipotent biological activity [49]. A unique post-translational modification (octanoylation of Ser3, catalysed by ghrelin &#927;-acyltransferase (MBOAT4, Q96T53) [133] occurs in both peptides, essential for full activity in binding to ghrelin receptors in the hypothalamus and pituitary, and for the release of growth hormone from the pituitary [58]. Structure activity studies showed the first five N-terminal amino acids to be the minimum required for binding [4], and receptor mutagenesis has indicated overlap of the ghrelin binding site with those for small molecule agonists and allosteric modulators of ghrelin function [44]. An endogenous antagonist and inverse agonist called Liver enriched antimicrobial peptide 2 (Leap2), expressed primarily in hepatocytes and in enterocytes of the proximal intestine [35, 68] inhibits ghrelin receptor-induced GH secretion and food intake [35]. The secretion of Leap2 and ghrelin is inversely regulated under various metabolic conditions [71]. In cell systems, the ghrelin receptor is constitutively active [45], but this is abolished by a naturally occurring mutation (A204E) that results in decreased cell surface receptor expression and is associated with familial short stature [93]

Gott Time Machines, BTZ Black Hole Formation, and Choptuik Scaling

We study the formation of BTZ black holes by the collision of point particles. It is shown that the Gott time machine, originally constructed for the case of vanishing cosmological constant, provides a precise mechanism for black hole formation. As a result, one obtains an exact analytic understanding of the Choptuik scaling.Comment: 6 pages, Late

Ghrelin receptor in GtoPdb v.2023.1

The ghrelin receptor (nomenclature as agreed by the NC-IUPHAR Subcommittee for the Ghrelin receptor [19]) is activated by a 28 amino-acid peptide originally isolated from rat stomach, where it is cleaved from a 117 amino-acid precursor (GHRL, Q9UBU3). The human gene encoding the precursor peptide has 83% sequence homology to rat prepro-ghrelin, although the mature peptides from rat and human differ by only two amino acids [75]. Alternative splicing results in the formation of a second peptide, [des-Gln14]ghrelin with equipotent biological activity [50]. A unique post-translational modification (octanoylation of Ser3, catalysed by ghrelin &#927;-acyltransferase (MBOAT4, Q96T53) [134] occurs in both peptides, essential for full activity in binding to ghrelin receptors in the hypothalamus and pituitary, and for the release of growth hormone from the pituitary [59]. Structure activity studies showed the first five N-terminal amino acids to be the minimum required for binding [4], and receptor mutagenesis has indicated overlap of the ghrelin binding site with those for small molecule agonists and allosteric modulators of ghrelin function [45]. An endogenous antagonist and inverse agonist called Liver enriched antimicrobial peptide 2 (Leap2), expressed primarily in hepatocytes and in enterocytes of the proximal intestine [36, 69] inhibits ghrelin receptor-induced GH secretion and food intake [36]. The secretion of Leap2 and ghrelin is inversely regulated under various metabolic conditions [72]. In cell systems, the ghrelin receptor is constitutively active [46], but this is abolished by a naturally occurring mutation (A204E) that results in decreased cell surface receptor expression and is associated with familial short stature [94]

The 2+1 Kepler Problem and Its Quantization

We study a system of two pointlike particles coupled to three dimensional Einstein gravity. The reduced phase space can be considered as a deformed version of the phase space of two special-relativistic point particles in the centre of mass frame. When the system is quantized, we find some possibly general effects of quantum gravity, such as a minimal distances and a foaminess of the spacetime at the order of the Planck length. We also obtain a quantization of geometry, which restricts the possible asymptotic geometries of the universe.Comment: 59 pages, LaTeX2e, 9 eps figure

Lambda<0 Quantum Gravity in 2+1 Dimensions II: Black Hole Creation by Point Particles

Using the recently proposed formalism for Lambda<0 quantum gravity in 2+1 dimensions we study the process of black hole production in a collision of two point particles. The creation probability for a BH with a simplest topology inside the horizon is given by the Liouville theory 4-point function projected on an intermediate state. We analyze in detail the semi-classical limit of small AdS curvatures, in which the probability is dominated by the exponential of the classical Liouville action. The probability is found to be exponentially small. We then argue that the total probability of creating a horizon given by the sum of probabilities of all possible internal topologies is of order unity, so that there is no exponential suppression of the total production rate.Comment: v1: 30+1 pages, figures, v2: 34+1 pages, agruments straightened ou