Selected Policy Measures Against the Debt Distress in Mongolia

The objective of this report is to examine the public external debt sustainability of Mongolia, and to propose appropriate regulatory actions for ongoing debates about economic reform. Following sharp external shocks that include a drop in foreign direct investment and a depreciation of the national currency, the country is at a critical moment of determining whether to default on its external debts or correct structural policy failures. Therefore, it is important that Mongolia identify its level of debt distress and determine which structural reforms should take place

Régészeti lelőhely – Szakrális tér : A népi vallásosság és a régészeti örökség kapcsolata a mai Mongóliában

A régészeti lelőhelyek általában a tudományos kutatások helyszíneként jelennek meg, de egyre nagyobb igény van arra, hogy az álló emlékeknél, a helyreállított épületekben vagy a rekonstruált régészeti jelenségekhez kapcsolódóan bemutatóhelyek, a nagyközönség által látogatható múzeumok és régészeti parkok jöjjenek létre. Ezek ma gyakran olyan emlékhelyek is, ahol a kulturális turizmus, az oktatás, az élmény alapú megismerés helyszíneiről beszélhetünk, de sok esetben helyi vallási jelenségekhez, a népi vallásossághoz, vagy valamilyen nagy világvalláshoz kapcsolódó, vagyis szakrális helyszínek is lehetnek. Jelen tanulmányunkban e jelenség egyik érdekes megjelenési formáját, a mongóliai régészeti lelőhelyek szakralizációját szeretnénk bemutatni. Az itt közreadott példák részben a magyar-mongol tájrégészeti kutatás, a Khi-Land projekt terepmunkái során szerzett tapasztalatok, részben pedig a mai Mongólia területén található egyik legnagyobb xiongnu lelőhely, Noyon Uul (Noin-Ula) ásatásaihoz köthetők

Saussureae involucratae Herba (Snow Lotus): Review of chemical compositions and pharmacological properties

Saussureae Involucratae Herba is the dried ground part of Saussurea involucrata (Kar. et Kir.) Sch.-Bip, which is also named as “Snow lotus” and being used in traditional Uyghur and/or Chinese medicine. This rare herb can be found at 4,000 m elevation in western part of Tianshan Mountain, Xinjiang China. According to China Pharmacopoeia (2015), the major pharmaceutical values of “Snow lotus” (Xuě liánhuā in Chinese) are alleviating rheumatoid arthritis, accelerating blood circulation and mitigating other “cold” syndromes. Traditionally, the clinical application of “Snow lotus” includes the treatments in inflammation-associated disorder, blood circulation acceleration and heat and dampness elimination. Recent studies suggested that “Snow lotus” possessed therapeutic effects associating with anti-cancer, anti-oxidation, adipogenesis suppression and neuroprotection activities, which were proposed to be related with its bioactive constitutes, i.e. acacetin, hispidulin, and rutin. In the present review, we aim to summarize pharmacological effects and underlying cell signaling pathways of “Snow lotus” in treating various medical problems. Copyright © 2020 Gong, Huang, Yang, Qi, Han, Zheng, He, Chan, Tsim and Dong. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms

Data on the localization of EGFP and 20α-hydroxysteroid dehydrogenase (20α-HSD) in the placenta and testes of transgenic mice

In order to investigate the function of monkey 20α-hydroxysteroid dehydrogenase (20α-HSD), transgenic mice (tg) were produced, expressing enhanced green fluorescent protein (EGFP) under the control of the monkey 20α-HSD promoter. The expression levels and localization of EGFP and 20α-HSD were analyzed in immature testis and in placenta. In support of our recent publication, ''Characterization of transgenic mice expressing EGFP under control of monkey 20α-hydroxysteroid dehydrogenase promoter'' (Park et al., 2018) [1], it was important to characterize the function of EGFP and 20α-HSD in the ovarian luteal cells of tg mice. Here, the expression of EGFP and 20α-HSD in immature testis and placenta are presented. The expression level of EGFP and 20α-HSD were detected in the testes 1 week after birth, and increased dramatically at 8 weeks. Both of proteins strongly detected in the placenta on days 14, 16, and 18 of pregnancy. Immunohistochemical analysis revealed that EGFP was detected in the seminiferous epithelium and 20α-HSD was specifically localized in the seminiferous tubule at 8 weeks. Keywords: Transgenic mice, 20α-HSD promoter, Testis, Placent

Constitutively Activating Mutants of Equine LH/CGR Constitutively Induce Signal Transduction and Inactivating Mutations Impair Biological Activity and Cell-Surface Receptor Loss In Vitro

The signal transduction of the equine lutropin/choriogonadotropin receptor (eLH/CGR) is unclear in naturally occurring activating/inactivating mutants of this receptor, which plays an important role in reproductive physiology. We undertook the present study to determine whether conserved structurally related mutations in eLH/CGR exhibit similar mechanisms of signal transduction. We constructed four constitutively activating mutants (M398T, L457R, D564G, and D578Y) and three inactivating mutants (D405N, R464H, and Y546F); measured cyclic adenosine monophosphate (cAMP) accumulation via homogeneous time-resolved fluorescence assays in Chinese hamster ovary cells; and investigated cell-surface receptor loss using an enzyme-linked immunosorbent assay in human embryonic kidney 293 cells. The eLH/CGR-L457R-, -D564G-, and -D578Y-expressing cells exhibited 16.9-, 16.4-, and 11.2-fold increases in basal cAMP response, respectively. The eLH/CGR-D405N- and R464H-expressing cells presented a completely impaired signal transduction, whereas the Y546F-expressing cells exhibited a small increase in cAMP response. The cell-surface receptor loss was 1.4- to 2.4-fold greater in the activating-mutant-expressing cells than in wild-type eLH/CGR-expressing cells, but was completely impaired in the D405N- and Y546F-expressing cells, despite treatment with a high concentration of agonist. In summary, the state of activation of eLH/CGR influenced agonist-induced cell-surface receptor loss, which was directly related to the signal transduction of constitutively activating mutants

The N-Linked Glycosylation Site N191 Is Necessary for PKA Signal Transduction in Eel Follicle-Stimulating Hormone Receptor

The follicle-stimulating hormone receptor (FSHR) contains several N-linked glycosylation sites in its extracellular region. We conducted the present study to determine whether conserved glycosylated sites in eel FSHR are necessary for cyclic adenosine monophosphate (cAMP) signal transduction. We used site-directed mutagenesis to induce four mutations (N120Q, N191Q, N272Q, and N288Q) in the N-linked glycosylation sites of eel FSHR. In the eel FSHR wild-type (wt), the cAMP response was gradually increased in a dose-dependent manner (0.01–1500 ng/mL), displaying a high response (approximately 57.5 nM/104 cells) at the Rmax level. Three mutants (N120Q, N272Q, and N288Q) showed a considerably decreased signal transduction as a result of high-ligand treatment, whereas one mutant (N191Q) exhibited a completely impaired signal transduction. The expression level of the N191Q mutant was only 9.2% relative to that of the eel FSHR-wt, indicating a negligible expression level. The expression levels of the N120Q and N272Q mutants were approximately 35.9% and 24% of the FSHG-wt, respectively. The N288Q mutant had an expression level similar to that of the eel FSHR-wt, despite the mostly impaired cAMP responsiveness. The loss of the cell surface agonist-receptor complexes was very rapid in the cells expressing eel FSHR-wt and FSHR-N288Q mutants. Specifically, the N191Q mutant was completely impaired by the loss of cell surface receptors, despite treatment with a high concentration of the agonist. Therefore, we suggest that the N191 site is necessary for cAMP signal transduction. This finding implies that the cAMP response, mediated by G proteins, is directly related to the loss of cell surface receptors as a result of high-agonist treatment

Constitutive Activation and Inactivation of Mutations Inducing Cell Surface Loss of Receptor and Impairing of Signal Transduction of Agonist-Stimulated Eel Follicle-Stimulating Hormone Receptor

In the present study, we investigated the signal transduction of mutants of the eel follicle-stimulating hormone receptor (eelFSHR). Specifically, we examined the constitutively activating mutant D540G in the third intracellular loop, and four inactivating mutants (A193V, N195I, R546C, and A548V). To directly assess functional effects, we conducted site-directed mutagenesis to generate mutant receptors. We measured cyclic adenosine monophosphate (cAMP) accumulation via homogeneous time-resolved fluorescence assays in Chinese hamster ovary (CHO-K1) cells and investigated cell surface receptor loss using an enzyme-linked immunosorbent assay in human embryonic kidney (HEK) 293 cells. The cells expressing eelFSHR-D540G exhibited a 23-fold increase in the basal cAMP response without agonist treatment. The cells expressing A193V, N195I, and A548V mutants had completely impaired signal transduction, whereas those expressing the R546C mutant exhibited little increase in cAMP responsiveness and a small increase in signal transduction. Cell surface receptor loss in the cells expressing inactivating mutants A193V, R546C, and A548V was clearly slower than in the cell expressing the wild-type eelFSHR. However, cell surface receptor loss in the cells expressing inactivating mutant N195I decreased in a similar manner to that of the cells expressing the wild-type eelFSHR or the activating mutant D540G, despite the completely impaired cAMP response. These results provide important information regarding the structure–function relationships of G protein-coupled receptors during signal transduction