A novel isoform of the β subunit of thyroid stimulating hormone in the human pituitary gland, peripheral blood leukocytes and thyroid gland (2023)

Thyroid stimulating hormone (TSH), a hormone produced in the anterior pituitary gland, is used to regulate thyroid hormone secretion. It has been known for more than three decades that cells of the immune system produce TSH; however, the functional role of TSH in the immune system is unclear. We have previously shown that an alternatively spliced ​​TSHβ isoform, termed the TSHβ splice variant (TSHβv), is the major form of TSHβ produced by hematopoietic cells in mice and humans. Most studies have linked TSHβv expression to myeloid cells of the immune system; however, plasma cells in Hashimoto's thyroiditis patients have recently been shown to be a source of TSHβv for the immune system. Here we show that TSHβv is expressed in bone marrow progenitors of lymphoid cells, monocytes and granulocytes, as well as cells of the mesenteric lymph nodes (MLN). Plasma cells generated by in vitro culture with bacterial lipopolysaccharide (LPS) and MLN cells from mice infected withL. monocytogenesexpressed TSHβv. There was an increase in the intensity of intracellular TSHβv expression in MLN cells after exposure to LPS, and in the ratio of TSHβv⁺CD138⁺MLN cell trackingL. monocytogenesinfection. The number of TSHβv⁺cells were increased in MLN cells, especially in CD138⁺cells, after a bacterial infection. This was confirmed by an increase in gene expression of BLIMP-1, the transcription factor for CD138, after infection. Circulating thyroxine levels decreased significantly in mice 24 hours after infection. These findings suggest that immune system TSHβv may contribute to the host immune response during bacterial infection.

Thyroid stimulating hormone (TSH) is a glycoprotein produced by thyrotrophic cells of the anterior pituitary gland and consists of a heterodimer of two non-covalently linked subunits, α and β. Each subunit is encoded by a separate gene located on a different chromosome and is transcribed in a coordinated manner in response to primarily stimulation by thyrotropin-releasing hormone (TRH) and inhibition by thyroid hormone. The production of bioactive TSH involves a process of cotranslational glycosylation and folding that allows the combination between the nascent α and β subunits. TSH is stored in secretory granules and released into the circulation in a regulated manner, primarily in response to TRH stimulation. Circulating TSH binds to specific cell surface receptors in the thyroid gland, where it stimulates the production of thyroid hormone, which modulates many metabolic processes and inhibits TSH production. Sensitive TSH assays provide accurate measurement of circulating TSH levels. Acquired and congenital disorders of TSH production are rare causes of abnormal thyroid function, but it is important to recognize them as a possible cause of abnormal thyroid function tests.

Different effects of lamb and pork consumption on thyroid hormone levels and energy metabolism in rats were investigated. Three diets, a lamb diet (LD), a pig diet (PD) and a casein control diet (CD) were isocaloric (15.5 kJ/g dry matter). Rats in the PD group had higher serum selenium concentrations (PAG<0.05) and liver 5'-deiodinase activities (PAG<0.05), caused by a higher selenium content in pork (PM). As a result, PM consumption increased serum triiodothrionine (T3) concentrations (PAG<0.05) and decreased serum thyroxine (T4) concentrations compared to casein and lamb (LM). Compared to casein and LM powder, PM powder had higher total levels of glutamic acid, leucine, aspartic acid, serine, and alanine (48.94 vs. 44.24 vs. 44.78), leading to higher serum concentrations of TBG (PAG<0.05) in the PD group. Compared to casein, PM powder had a higher total leucine and isoleucine content (9.87 vs. 9.21; 5.12 vs. 4.74), LM powder had a lower leucine content (8.14 vs. 9.21), which led to higher serum albumin concentrations in the PD group (PAG<0.05) and lower in the LD group (PAG<0.05). Consequently, the PD group had lower serum concentrations of free T4 (FT4) and free T3 (FT3) (PAG<0.05), which significantly reduced the rats' energy expenditure, while the LD group had higher serum FT3 concentrations (PAG<0.05), which significantly increases energy consumption. These were inferred from the various changes in liver and skeletal muscle Na,K-ATPase activities (PAG<0.05), Oxygen Demand (OCR) (PAG<0.05) and rectal temperature, especially on day 13 (PAG<0.05) and body weights (PAG<0.05) in the PD or LD group. We conclude that the consumption of PM or LM, with a different amino acid composition, had different effects on rat energy metabolism through the multistep regulation of TH.

The two diets, a duck meat diet (DMD) and a control casein diet (CD), were isocaloric (15.9 kJ/g dry matter) and contained 18.3% protein, 7.4% fat and 60.0% carbohydrates. The selenium contents in casein, duck meat powder, CD and DMD were 0.061, 0.549, 0.123 and 0.225 mg/kg. Rats in the DMD group had higher serum selenium concentrations (pag<0.05) and liver 5'-deiodinase activities (pag<0.05). As a result, duck meat consumption increased serum concentrations of triiodothrionine (T3) (pag<0.05) and decreased serum thyroxine (T4) concentrations (pag<0.05). The lowest serum concentrations of T4 (pag<0.05) were also supported by the lower total tyrosine and phenylalanine content in duck meat powder compared to casein (7.72 versus 10.13). Compared to casein, duck meat powder had higher total levels of glutamic acid, leucine, aspartic acid, serine and alanine (44.68 vs. 49.21), leading to higher serum concentrations of TBG (pag<0.05) in the DMD group. Therefore, the DMD group had lower serum free T4 (FT4) concentrations (pag<0.05), and lower serum free T3 (FT3) concentrations at day 14 (pag<0.05), which significantly reduced the energy expenditure of rats in the DMD group, with lower Na, K-ATPase and Ca-ATPase activities in the liver (pag<0.05), lower OCR and rectal temperature, especially on day 13 (pag<0.05), higher body weight (pag<0.05) and weight gain (pag<0.05). We conclude that duck meat consumption decreased energy metabolism in rats by regulating TH multisteps.

European Journal of Operational Research, Volumen 239, Número 3, 2014, blz. 756-763

Three approaches are generally used to analyze decisions under uncertainty: expected utility (EU), second-degree stochastic dominance (SSD), and mean risk models (MR), with the mean standard deviation (MS) being the best-known MR. fashion model. Because MR models generally lead to different efficient sets and are therefore an ongoing source of controversy, the specific concern of this article isNeeto propose another model of MR. Instead, we show that the efficient sets of SSD and MR are identical, provided that (a) the measure of risk satisfies both positive homogeneity and consistency with respect to the Rothschild and Stiglitz definition(s) of increasing risk (1970 ) and (b) the choice set includes the risk-free asset and satisfies a general property of location and scale, which can be interpreted as a market model. Under these circumstances, there is no controversy between the RM models and they all have a theoretical basis for decisions. They also provide a useful way to compare the estimation error related to the empirical implementation of different RM models.

Pet Endocrinology, Volume 48, 2014, pp. 145-157

The development of a new enzyme-linked immunosorbent assay (ELISA) to determine luteinizing hormone (LH) in bovine plasma is described. Anti-bovine LH (bLH) monoclonal antibodies (mAb) were produced and characterized. A mAb recognizing the β subunit of bLH was used for immunoaffinity purification of substantial amounts of biologically active bLH from pituitary. Purified bLH in combination with 2 anti-bLH β subunit mAbs was used to develop a sandwich ELISA, which met all the criteria required to investigate LH secretion patterns in cattle. The ELISA standard curve was linear in the range of 0.05 to 2.5 ng/ml, and the assay proved suitable for measuring bLH in plasma without any pretreatment of the samples. Cross-reactivity and recovery tests confirmed the specificity of the method. The intra-assay and inter-assay coefficients of variation varied between 3.41% and 9.40% and 9.29% and 15.84%, respectively. The analytical specificity of the method was validated in vivo by LH challenge testing in heifers using the LH-releasing peptide, gonadotropin-releasing hormone. In conclusion, the use of mAb for this ELISA to coat the wells and label, combined with the easy one-step production of reference bLH, ensures long-term continuity in large-scale bovine LH measurements.

European Journal of Surgical Oncology (EJSO), Volumen 40, Número 11, 2014, pp. 1459-1466

Neuropeptides, Volume 59, 2016, pp. 111-116

Liquid Phase Equilibrium, Volume 367, 2014, pg. 125-1

Densities, conductivity, fluorescence and UV-vis absorption spectroscopy of glycyl dipeptide + ionic liquid (1-dodecyl-3-methylimidazolium bromide ([C₁₂Mixtures of mim]Br))+water at different temperatures have been measured. From the density data, the standard partial molar volume$(V_{2,\varphi }^0)$, standard partial molar volume of the transfer of three glycyldipeptides from water to aqueous medium [C₁₂mim]Br solutions (D_TV^O), partial molar expandability$({\mathrm{mi}}_{\varphi }^{°})$and Hepler's constant are calculated. By means of electrical conductivity measurements, the critical micellar concentration (C_cmc) and a set of thermodynamic parameters of micellization of [C₁₂mim]Br in aqueous glycyldipeptide solutions. Effects of temperature and carbohydrate chain length of glycyl dipeptides on the filling properties of the dipeptides and the critical concentration of micelles (C_cmc) dec₁₂mim]Br were examined. Pyrene fluorescence spectra were used to determine the micropolarity shift produced by [C₁₂mim]Br with glycyl dipeptides and the aggregation behavior of [C₁₂mim]Br. The results of the UV-vis absorption spectra showed the binding constant between the dipeptide and [C₁₂I]Br about itC_cmcwas determined.

Act of Analytical Chemistry, jaargang 908, 2016, pp. 150-160

Epitope mapping is crucial for the characterization of protein-specific antibodies. Typically, small overlapping peptides are chemically synthesized and immobilized to determine the specific peptide sequence. In this study, we report the use of a fast and low-cost planar microsphere chip for epitope mapping. We developed a generic strategy to express recombinant peptide libraries instead of using expensive synthetic peptide libraries. A biotin group was introducedI liveat a defined peptide position using biotin ligase. raw peptidesEscherichia coliThe lysate was coupled to streptavidin-coated microspheres by incubation, avoiding cumbersome purification procedures. For reading, we used a multiplex planar bead chip with bead populations encoded for size and fluorescence. For epitope mapping, up to 18 populations of peptide-loaded beads (at least 20 beads per peptide) displaying the primary sequence of a protein were analyzed simultaneously. If an antibody recognized an epitope, a fluorescently labeled secondary antibody generated a signal that was quantified and the average value of all granules in the population calculated. We mapped epitopes for rabbit anti-PA28γ (proteasome activator 28γ) polyclonal sera, for a murine monoclonal antibody against PA28γ and for a murine monoclonal antibody against hamster polyomavirus major capsid protein VP1 as models. In each case, the identification of an individual peptide sequence from up to 18 sequences was possible. With this approach, an epitope can be mapped multiparametrically within three weeks.