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1.
ACS Omega ; 6(21): 13802-13806, 2021 Jun 01.
Article in English | MEDLINE | ID: mdl-34095672

ABSTRACT

Terahertz spectroscopy can be utilized as an effective nondestructive identification tool for the study of artist's pigments. Consequently, extensive measurements have been conducted on representative pigment species, and a few terahertz spectral databases have been constructed. However, the reported spectra were often acquired from pigment samples mixed with polyethylene at room temperature with low resolution, which often led to low-quality spectra with unresolved overlapping lines further broadened due to thermal effects. Here, we present our study of vermilion (HgS, mercury sulfide) as an illustration of how we can overcome such difficulties by studying free-standing oil-paint samples at room temperature and then by performing low-temperature measurements on polyethylene-mixed samples to minimize line broadening due to thermal effects. Our results identify clearly resolved absorption peaks due to lattice vibrations of vermilion at 40.4, 44.5, and 89.9 cm-1 at 2 K. The temperature dependence of the peak shift and line broadening reveals anharmonic characteristics of these lattice vibrational modes. Our approach will definitely suggest new ways to improve and enhance existing terahertz spectral databases of ancient and modern pigments toward actual analysis, diagnosis, and conservation of heritage artworks.

2.
Nat Commun ; 10(1): 3496, 2019 08 02.
Article in English | MEDLINE | ID: mdl-31375680

ABSTRACT

The timely mobilization of hematopoietic stem and progenitor cells (HSPCs) is essential for maintaining hematopoietic and tissue leukocyte homeostasis. Understanding how HSPCs migrate between bone marrow (BM) and peripheral tissues is of great significance in the clinical setting, where therapeutic strategies for modulating their migration capacity determine the clinical outcome. Here, we identify an epigenetic regulator, Phc2, as a critical modulator of HSPC trafficking. The genetic ablation of Phc2 in mice causes a severe defect in HSPC mobilization through the derepression of Vcam1 in bone marrow stromal cells (BMSCs), ultimately leading to a systemic immunodeficiency. Moreover, the pharmacological inhibition of VCAM-1 in Phc2-deficient mice reverses the symptoms. We further determine that Phc2-dependent Vcam1 repression in BMSCs is mediated by the epigenetic regulation of H3K27me3 and H2AK119ub. Together, our data demonstrate a cell-extrinsic role for Phc2 in controlling the mobilization of HSPCs by finely tuning their bone marrow niche.


Subject(s)
Cell Movement/genetics , Epigenetic Repression , Hematopoietic Stem Cells/immunology , Polycomb Repressive Complex 2/metabolism , Vascular Cell Adhesion Molecule-1/genetics , Animals , Bone Marrow Transplantation/adverse effects , Cell Movement/immunology , Cells, Cultured , DNA Methylation/immunology , Hematopoietic Stem Cell Mobilization/methods , Hematopoietic Stem Cell Transplantation/adverse effects , Histones/genetics , Histones/metabolism , Mice , Mice, Knockout , Models, Animal , Polycomb Repressive Complex 2/genetics , Primary Cell Culture , Vascular Cell Adhesion Molecule-1/antagonists & inhibitors
3.
Microsc Microanal ; 19 Suppl 5: 162-6, 2013 Aug.
Article in English | MEDLINE | ID: mdl-23920198

ABSTRACT

A new method for determining the vitrification rate of pottery depending on the firing temperature was devised using secondary electron images (SEI) of scanning electron microscope (SEM). Several tests were performed to establish the appropriate operating conditions of SEM and reproducibility as well as to examine the applicability of the method. The grayscale values converted from each pixel of SEI were used to determine the vitrification rate of pottery, which in our study were artificially fired specimens composed of three types of clay. A comparison between the vitrification rate value and appearance temperature of minerals shows that mullite formation starts at 1,100°C, during which the vitrification rate rapidly increases by over 10%. In consequence, the result presented here demonstrates that the new method can be applied to estimate the firing temperature of pottery.

4.
Biotechnol Lett ; 34(12): 2191-7, 2012 Dec.
Article in English | MEDLINE | ID: mdl-22936302

ABSTRACT

Cytotoxic T lymphocyte-associated antigen-4 (CTLA-4; CD152) is a transmembrane protein that is structurally similar to CD28. As CTLA-4 has a much higher binding affinity to B7 than CD28, several approaches using soluble CTLA-4 have been tried to down-regulate T cell activity by blocking the interaction between CD28 and B7. We constructed soluble rhesus monkey CTLA-4 immunoglobulin (CTLA-4Ig) containing a critical binding site to B7 combined with a constant Ig heavy chain region in a mammalian system. Flow cytometry analyses indicated that soluble rhesus monkey CTLA-4Ig bound to rhesus monkey CD86 (B7.2). Moreover, soluble rhesus monkey CTLA-4Ig more effectively blocked the rhesus monkey-rhesus monkey allogeneic mixed lymphocyte reaction compared with that of humans. These results indicate that soluble rhesus monkey CTLA-4Ig may be useful in preclinical trials in a rhesus monkey model.


Subject(s)
B7-2 Antigen/antagonists & inhibitors , B7-2 Antigen/immunology , CTLA-4 Antigen/immunology , Immunoglobulins/immunology , Immunologic Factors/immunology , Animals , CTLA-4 Antigen/genetics , Immunoglobulins/genetics , Immunologic Factors/genetics , Lymphocyte Culture Test, Mixed , Macaca mulatta
5.
Biotechnol Lett ; 34(7): 1225-33, 2012 Jul.
Article in English | MEDLINE | ID: mdl-22456900

ABSTRACT

Since T cells express diverse sex steroid hormone receptors, they might be a good model to evaluate the effects of sex steroid hormones on immune modulation. Porcine testicular extract contains several sex steroid hormones and may be useful to study the effects of sex steroid hormones during T cell activation. We have examined the effects of the porcine testicular extract on T cell activation: proliferation and secretion of cytokines (IL-2 and IFN-γ) by activated T cells were severely decreased after treatment with porcine testicular extract. The extract produced an immunosuppressive effect and inhibited the proliferation of activated T cells by blocking the cell cycle transition from the G(1) phase to S phase. These effects were mediated by a decrease in the expression of cyclin D1 and cyclin E and constitutive expression of p27(KIP1) after T cell activation.


Subject(s)
Cell Cycle/drug effects , Cell Extracts/pharmacology , Cell Proliferation/drug effects , Immunologic Factors/isolation & purification , Immunologic Factors/pharmacology , T-Lymphocytes/physiology , Testis/chemistry , Animals , Cell Extracts/isolation & purification , Cytokines/metabolism , Male , Swine , T-Lymphocytes/drug effects
6.
Mol Immunol ; 48(15-16): 2189-97, 2011 Sep.
Article in English | MEDLINE | ID: mdl-21632113

ABSTRACT

Post-translational modification by small ubiquitin-like modifier (SUMO) is involved in several significant cellular events. In particular, SUMO-1 and SUMO-4 modifications of IκBα have been shown to be actively involved in NFκB regulation. However, among the SUMO family, the specific function of SUMO-2/3 remains relatively unknown. In addition, it is not clear whether SUMO-2/3 follows the same functional role as SUMO-1 and SUMO-4 during the activation of NFκB. In this study, we examined the influence of mouse SUMO-2 during the maturation of dendritic cells (DCs). Our results showed that the ectopic expression of SUMO-2 does not affect the cell surface expression of MHC class II molecule (A(b)) and co-stimulatory molecules (CD80 and CD86), and the efficiency of antigen uptake. However, the ectopic expression of mouse SUMO-2 inhibited IL-12 secretion by blocking the translocation of the p65 subunit of NFκB into the nucleus, which led to the polarization of naïve CD4(+) T cells to T helper 2 (Th2) shift in vitro. Further analyses showed that SUMO-2 directly modified IκBα. These results indicate that the functional role of SUMO-2/3 in the regulation of NFκB activity was conserved during evolution.


Subject(s)
Dendritic Cells/metabolism , Interleukin-12/biosynthesis , Small Ubiquitin-Related Modifier Proteins/metabolism , Transcription Factor RelA/metabolism , Animals , Antigen Presentation/immunology , Blotting, Western , Cell Differentiation/immunology , Cell Nucleus/chemistry , Cell Nucleus/immunology , Cell Nucleus/metabolism , Cell Separation , Chromatin Immunoprecipitation , Dendritic Cells/cytology , Dendritic Cells/immunology , Electrophoretic Mobility Shift Assay , Flow Cytometry , I-kappa B Proteins/immunology , I-kappa B Proteins/metabolism , Interleukin-12/immunology , Lymphocyte Activation/immunology , Mice , Mice, Inbred C57BL , Microscopy, Confocal , NF-KappaB Inhibitor alpha , Phagocytosis , Protein Transport/immunology , Reverse Transcriptase Polymerase Chain Reaction , Small Ubiquitin-Related Modifier Proteins/immunology , Sumoylation , Th2 Cells/cytology , Th2 Cells/immunology , Th2 Cells/metabolism , Transcription Factor RelA/immunology
7.
Biotechnol Lett ; 32(2): 203-8, 2010 Feb.
Article in English | MEDLINE | ID: mdl-19834647

ABSTRACT

Lymphocyte activation gene-3 (LAG-3; CD223) is a transmembrane protein that is structurally similar to CD4. Since LAG-3 has a much higher binding affinity to MHC class II than that of CD4, several approaches using soluble LAG-3 were used to modulate immune responses by activation or inhibition of MHC class II expressing antigen presenting cells. In this study, we constructed soluble pig LAG-3 containing a critical binding site (D1 and D2 region) to MHC class II molecules, combined with a constant region of an immunoglobulin (Ig) heavy chain. Flow cytometry analyses indicated that soluble pig LAG-3 binds to both pig and human MHC class II molecules. Moreover, soluble pig LAG-3 can inhibit human lymphocyte proliferation in the human-pig xenogeneic mixed lymphocyte reaction in a dose-dependent manner. These results indicate that soluble pig LAG-3 may be useful for controlling the xenogeneic T cell immune responses between the human and pig.


Subject(s)
Antibodies, Heterophile/immunology , Antigens, CD/immunology , Antigens, CD/pharmacology , Cell Communication/immunology , Lymphocyte Activation/immunology , Lymphocytes/immunology , Animals , Antigens, CD/chemistry , Cell Communication/drug effects , Cells, Cultured , Humans , Lymphocyte Activation/drug effects , Lymphocytes/drug effects , Solubility , Swine , Lymphocyte Activation Gene 3 Protein
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