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Regarding climatic diversity in Iran and the dependence of many outdoor activities (occupational, recreational, tourism attraction, etc.) on climatic conditions, this study conducted aiming to evaluate thermal comfort fluctuations in Iran. Thermal comfort fluctuations in different climates of Iran were investigated between 1985 and 2014 using recorded meteorological data in 40 synoptic stations. The Mann-Kendall test and Sen’s Slope were used to analyse the changing trends of the Humidex and to determine the actual slope of a trend over time, respectively. In overall, the southern areas of Iran have the longest period with unfavourable and extremely unfavourable climatic conditions in this study. Conversely, in the northern half of Iran, especially in North West areas, the appropriate summer season provides the best climatic conditions for outdoor activities.

Objective: The present study aimed to determine the efficacy of EstroG-100 herbal extract on hot flashes in postmenopausal women., Material and Methods: This randomized, double-blind, placebo-controlled trial was performed on postmenopausal women recruited from two university hospitals complaining of hot flashes. The intervention group received two extract capsules (daily for 12 weeks), and the control group received two placebo capsules (daily for 12 weeks). Finally, the frequency and severity of hot flashes (F&S) were subjectively reported and compared weekly during the treatment for 12 weeks., Results: Out of 120 randomized participants, 35 entered the final analysis for each group. In the third week, participants of the control group significantly reported more moderate hot flashes than other group (MD=1.00, P = 0.004). However, in terms of mild (MD=0.74, P = 0.057) and severe (MD=0.60, P = 0.064) hot flashes, the groups did not differ. In the sixth week, mild (MD=1.51, P<0.001), moderate (MD=1.54, P<0.001), and severe (MD=1.22, P<0.001) hot flashes were significantly reported more in the control group compared with another group., Conclusion: The present study revealed that EstroG-100 herbal extract could improve hot flashes in postmenopausal women., (Copyright © 2023. Published by Elsevier Inc.)

Background: Stimulant pharmaceuticals are abused among academic students to elevate mood, improve studying, intellectual capacity, memory and concentration, and increase wakefulness. This study was designed to evaluate the current situation of stimulant use among medical students and residents of Babol University of Medical Sciences., Methods: This cross-sectional study was conducted among 560 medical students and clinical residents of Babol University of Medical Sciences during the academic year 2014-2015. A self-administered questionnaire was used for data collection., Results: Four hundred and forty-four (79.3%) students filled out the questionnaires. 49 (11%) individuals reported amphetamine and methylphenidate (ritalin) use. The mean age of the stimulant drug users was 24.6±4.8 years. The main initiator factor was to improve concentration (29 persons; 59.2%). There were significant statistical correlations between stimulant drugs abuse and male gender, living in dormitor in residence and internship and past medical history of psychiatric disorders (depression, attention deficit hyperactivity disorder and substance abuse) (p<0.05).16 (32%) students started the drug use on their friends' advice; 15 (30%) due to self-medication and 12 (24%) persons with physician´s prescription., Conclusions: Because of significant prevalence of stimulant use, regulatory governmental policies and also planning to improve essential life skills, awareness about the side effects and complications of these drugs, screening of at-risk college students and early identification of the abusers are suggested., Competing Interests: The authors declare that there are no conflicts of interest.

Amadori product is an important and stable intermediate, which is produced during glycation process. It is a marker of hyperglycemia in diabetes mellitus, and its accumulation in the body contributes to microvascular complication of diabetes including diabetic nephropathy and retinopathy. In this study, the effect of acetoacetate on the formation of Amadori products and biophysical properties of human serum albumin (HSA), after incubation with glucose, was investigated using various methods. These included circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, and UV-visible and fluorescence spectroscopy. Our results indicated that the production of Amadori products in HSA incubated with glucose (GHSA) was increased in the presence of acetoacetate. We also detected alterations in the secondary and tertiary structure of GHSA, which was increased in the presence of acetoacetate. These changes were attributed to the formation of covalent bonds between the carbonyl group of acetoacetate and the nucleophilic groups (lysine residues) of HSA. Thus, acetoacetate can enhance the production of Amadori products through formation of covalent bonds with biomaterials., (Copyright © 2016 Elsevier B.V. All rights reserved.)

P2X2 receptors are members of the ATP-gated P2X family of cation channels, and they participate in neurotransmission in sympathetic ganglia and interneurons. Here, we identified 7,7'-(carbonylbis(imino-3,1-phenylenecarbonylimino-3,1-(4-methyl-phenylene)carbonylimino))bis(1-methoxy-naphthalene-3,6-disulfonic acid) tetrasodium salt (NF770) as a nanomolar-potent competitive P2X2 receptor antagonist within a series of 139 suramin derivatives. Three structural determinants contributed to the inhibition of P2X2 receptors by NF770: 1) a "large urea" structure with two symmetric phenylenecarbonylimino groups; 2) attachment of the naphthalene moiety in position 7,7'; and 3) the specific position of two sulfonic acid groups (3,3'; 6,6') and of one methoxy group (1,1') at the naphthalene moiety. This structure-activity relationship was interpreted using a rat P2X2 homology model based on the crystal structure of the closed zebrafish P2X4 receptor. Docking of the suramin derivatives into the modeled ATP-binding pocket provides a uniform explanation for the observed differences in inhibitory potencies. Changes in the chemical structure that increase the inhibitory potency of the suramin derivatives improved the spatial orientation within the ATP-binding pocket to allow for stronger polar interactions of functional groups with Gly72, Glu167, or Arg290. Gly72 is responsible for the orientation of the methoxy group close to Arg290 or Glu167. Combined mutational and functional analysis confirmed that residues Gly72 and Glu167 are as important for ATP binding as Arg290, the ATP-binding role of which has been shown in previous studies. The in silico prediction of Gly72 and Glu167 as ATP-binding residues strongly supports the validity of our homology docking.

TMEM16A/anoctamin-1 has been identified as a protein with the classic properties of a Ca(2+)-activated chloride channel. Here, we used blue native polyacrylamide gel electrophoresis (BN-PAGE) and chemical cross-linking to assess the quaternary structure of the mouse TMEM16A(a) and TMEM16A(ac) splice variants as well as a genetically concatenated TMEM16A(a) homodimer. The constructs carried hexahistidyl (His) tags to allow for their purification using a nondenaturing metal affinity resin. Neither His-tagging nor head-to-tail concatenation of two copies of TMEM16A(a) noticeably affected Ca(2+)-induced measured macroscopic Cl(-) currents compared with the wild-type TMEM16A(a) channel. The digitonin-solubilized, nondenatured TMEM16A(a) protein migrated in the BN-PAGE gel as a homodimer, as judged by comparison with the concatenated TMEM16A(a) homodimer and channel proteins of known oligomeric structures (e.g. the voltage-gated Cl(-) channel CLC-1). Cross-linking with glutaraldehyde corroborated the homodimeric structure of TMEM16A(a). The TMEM16A(a) homodimer detected in Xenopus laevis oocytes and HEK 293 cells dissociated into monomers following denaturation with SDS, and reducing versus nonreducing SDS-PAGE provided no evidence for the presence of intersubunit disulfide bonds. Together, our data demonstrate that the Ca(2+)-activated chloride channel member TMEM16A shares an obligate homodimeric architecture with the hCLC-1 channel.

Homomeric P2X3 receptors are present in sensory ganglia and participate in pain perception. Amino acid (AA) residues were replaced in the four supposed nucleotide binding segments (NBSs) of the human (h) P2X3 receptor by alanine, and these mutants were expressed in HEK293 cells and Xenopus laevis oocytes. Patch clamp and two-electrode voltage clamp measurements as well as the Ca(2+) imaging technique were used to compare the concentration-response curves of the selective P2X1,3 agonist α,β-methylene ATP obtained at the wild-type P2X3 receptor and its NBS mutants. Within these NBSs, certain Gly (Gly-66), Lys (Lys-63, Lys-176, Lys-284, Lys-299), Asn (Asn-177, Asn-279), Arg (Arg-281, Arg-295), and Thr (Thr-172) residues were of great importance for a full agonist response. However, the replacement of further AAs in the NBSs by Ala also appeared to modify the amplitude of the current and/or [Ca(2+)](i) responses, although sometimes to a minor degree. The agonist potency decrease was additive after the simultaneous replacement of two adjacent AAs by Ala (K65A/G66A, F171A/T172A, N279A/F280A, F280A/R281A) but was not altered after Ala substitution of two non-adjacent AAs within the same NBS (F171A/N177A). SDS-PAGE in the Cy5 cell surface-labeled form demonstrated that the mutants appeared at the cell surface in oocytes. Thus, groups of AAs organized in NBSs rather than individual amino acids appear to be responsible for agonist binding at the hP2X3 receptor. These NBSs are located at the interface of the three subunits forming a functional receptor.