Single Transverse Spin Asymmetry for Large-p_T Pion Production in Semi-Inclusive Deep Inelastic Scattering

We study the single spin asymmetry (SSA) for the pion production with large transverse momentum p_T in semi-inclusive deep inelastic scattering $ep^\uparrow\to e\pi X$. We derive the twist-3 cross section formula for SSA, focussing on the soft-gluon-pole contributions associated with the twist-3 distribution for the nucleon and with the twist-3 fragmentation function for the pion. We present a simple estimate of the asymmetries due to each twist-3 effect from nucleon and pion, respectively, by fixing the overall strength of the relevant nonperturbative quantities by the data on the SSA A_N in $p^\uparrow p\to\pi X$ collision.Comment: 19 pages in LaTex. Some discussions added. To appear in Nucl. Phys.

Single Transverse Spin Asymmetry for Semi-Inclusive Deep Inelastic Scattering

Abstract. Establishing the twist-3 formalsim for the single transverse spin asymmetry, we present a complete single-spin-dependent cross section for SIDIS, ep ↑ → eπX, associated with the twist-3 distribution for the transversely polarized nucleon. We emphasize that the consistency condition from the Ward identities for color gauge invariance is crucial to prove factorization property of the cross section

Analysis of Thyroid Hormones in Serum of Baikal Seals and Humans by Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS) and Immunoassay Methods: Application of the LC-MS/MS Method to Wildlife Tissues

Thyroid hormones (THs) are essential for the regulation of growth and development in both humans and wildlife. Until recently, TH concentrations in the tissues of animals have been examined by immunoassay (IA) methods. IA methods are sensitive, but for TH analysis, they are compromised by a lack of adequate specificity. In this study, we determined the concentrations of six THs, l-thyroxine (T₄), 3,3′,5-triiodo-l-thyronine (T₃), 3,3′,5′-triiodo-l-thyronine (rT₃), 3,5-diiodo-l-thyronine (3,5-T₂), 3,3′-diiodo-l-thyronine (3,3′-T₂), and 3-iodo-l-thyronine (3-T₁), in the serum of humans (<i>n</i> = 79) and wild Baikal seals (<i>n</i> = 37), by isotope ([¹³C₆]-T₄)-dilution liquid chromatography (LC)-tandem mass spectrometry (MS/MS), and compared the TH levels with those measured by an electrochemiluminescent immunoassay (ECLIA) method. T₃ and T₄ were detected in all serum samples of both humans and Baikal seals, whereas T₁, 3,3′-T₂, and 3,5-T₂ were below the limit of detection (LOD). rT₃ was detected in Baikal seal sera at concentrations higher than T₃ in 28 seal samples, indicating an anomaly in deiodinase activity in Baikal seals. In humans, regression analyses of TH concentrations, measured by ECLIA and LC-MS/MS methods, showed significant correlations for T₄ (<i>r</i> = 0.852) and T₃ (<i>r</i> = 0.676; after removal of a serum sample with abnormal T₃ levels). In Baikal seals, a low correlation coefficient (<i>r</i> = 0.466) for T₄ levels and no correlation for T₃ levels (<i>p</i> = 0.093) were found between ECLIA and LC-MS/MS methods. These results suggest that interference by a nonspecific reaction against anti-T₃ and anti-T₄ antibodies used in the ECLIA can contribute to inaccuracies in TH measurement in Baikal seals. When the relationship between concentrations of THs in sera and dioxin-like toxic equivalents in blubber samples of Baikal seals (<i>n</i> = 19) was examined, a significantly negative correlation was found for serum T₄ levels measured by the LC-MS/MS method, but not for those measured by ECLIA. Thus, our results indicate that the LC-MS/MS method is more reliable and accurate for the elucidation of alteration in circulating TH levels in wildlife, as caused by environmental and physiological factors

Induction of osteoblast differentiation by FoxOs.

<p>(A–C) Induction of osteoblast differentiation by FoxO3aTM. Primary osteoblasts from calvariae of wild-type mice were infected with adenovirus expressing GFP or FoxO3aTM, and ALP staining at 2 days and von Kossa staining at 6 days after infection (A), quantification of mineralization (B), and osteoblast marker gene expression (C) are shown. The value in GFP-introduced cells was set as 1 and the relative level is shown in B. Similar results were obtained in three independent experiments and representative data are shown. (D–F) Inhibition of the mineralization of MC3T3-E1 cells by sh<i>FoxO1</i> and sh<i>FoxO3a</i>. MC3T3-E1 cells were infected with retrovirus expressing GFP, sh<i>FoxO1</i>, or sh<i>FoxO3a</i>, and cultured in the presence of BMP2 (100ng/ml). The expression of <i>FoxO1</i> and <i>FoxO3a</i> was examined by real-time RT-PCR (D) and mineralization was examined by von Kossa staining (E) and its quantification (F) after culture for 2 weeks. The value in shGFP-introduced cells was set as 1 and the relative levels are shown in F. Similar results were obtained in three independent experiments and representative data are shown.</p

Expression and activation of FoxOs in Bcl2−/− calvariae.

<p>(A) Real-time RT-PCR analysis of the expression of FoxOs. RNA was directly extracted from newborn calvariae of wild-type and Bcl2^−/− mice. wild-type mice, n = 6; Bcl2^−/− mice, n = 15. *vs. wild-type mice, **p<0.01, ***p<0.001. (B) Reporter assay of Gadd45a promoter using wild-type and Bcl2^−/− primary osteoblasts. Similar results were obtained in two independent experiments and representative data are shown. (C, D) Western blot analysis. Protein was extracted from newborn calvariae of wild-type and Bcl2^−/− mice. The intensities of the bands were normalized against each β-actin, the normalized values in wild-type mice were set as 1, and relative levels are shown. Similar results were obtained in three independent experiments and representative data are shown. (E) Real-time RT-PCR analysis. RNA was directly extracted from calvariae of wild-type and Bcl2^−/− newborn mice. wild-type mice, n = 6; Bcl2^−/− mice, n = 15. *vs. wild-type mice. *P<0.05, **P<0.01. (F) <i>p53</i>, <i>Pten</i>, and <i>Igfbp3</i> expression in primary osteoblasts. The cDNA in Fig. 3I was used for real-time PCR analysis. n = 10−12. *vs. wild-type primary osteoblasts. **P<0.01. (G) Induction of <i>Pten</i> by p53. p53^−/− osteoblasts were infected with p53-expressing retrovirus or empty retrovirus. Next day, the cells were plated at the concentration of 1.5×10⁵/well in 48 well plates (day 0). 50 µg/ml ascorbic acid and 10mM β-glycerophosphate were added at day 1, and mRNA was extracted at day 4. The expression of <i>p53</i>, <i>Pten</i>, and <i>Igfbp3</i> was examined by real-time RT-PCR. Similar results were obtained in two independent experiments and representative data are shown. n = 12−13. *vs. empty retrovirus. **P<0.01, ***p<0.001. (H) Schematic presentation of the signaling pathway for FoxO activation. p53 induces Pten mRNA and Igfbp3 mRNA. Pten and Igfbp3 inhibit Akt activation. Akt inhibits the activation of FoxOs. Activation of JNK and Mst1 activate FoxOs. p53 failed to induce Igfbp3 in vitro (G). Dotted arrows indicate that the activation did not occur in Bcl2^−/− mice (C).</p