122 117 OIPM TRPtransient receptor potential TRPV ruthenium red TRPV4 RN1734 ATP TRPV4
117 123 P SA 1 2 1 2 Glial fibrillary acidic protein GFAP S100β S100 S100A6 S100A6 CA1 S100A6 CA1 CA1 S100A6 GFAPS100β S100A6 brain lipid binding protein BLBP S100A6 P Distribution of corticosteroid receptors in oligodendrocytes of mice Yumiko Matsusue 1,2 , Noriko HoriiHayashi 2 , Takayo Sasagawa 2 , Wataru Matsunaga 2 , Katsuhiko Ono 3 , Mayumi Nishi 2 1 Dept. Oral. Maxillofac. Surg. Nara. Med. Univ., Nara, Japan, 2 Dept. Anat. & Cell Biol. Nara. Med. Univ., Nara, Japan, 3 Dept. Biol. Kyoto. Pref. Univ. Med., Kyoto, Japan Glucocorticoids are the mainstay in treating patients with diseases affecting the white matter, including multiple sclerosis in which the myelin sheaths around the axons of the brain, thereby leading to demyelination. In contrast, glucocorticoids are ineffective in gray matter injuries, such as head trauma. Many studies have reported glucocorticoid receptor GR is expressed in cultured oligodendrocytes. But very little study has revealed the expression of GR in oligodendrocytes in vivo. We investigated whether the oligodendorocytes were positive for GR by using two different oligodendorocyte markers, carbonic anhydrase CA II, a mature oligodendrocyte marker, and NG2, an oligodendrocyte progenitor marker. We focused on the gray matter regions including the cortex, hippocampus CA1, CA3, dentate gyrus, and amygdala, and the white matter regions including the external capsule, colpus callosum and fimbria hippocampus by using immunohistochemistry. We found over 80% of mature oligodendrocytes and oligodendrocyte progenitors express GR in various brain region. In contrast, neither oligodendrocytes nor oligodendrocyte progenitors express mineralocorticoid receptor MR. P F 1 1 1 1 1 2 2 3 1 2 3 4F2 9 4F2 4F2 DEAD box RNA Ddx54 MBP 21.5 kDa P Immunohistochemical Analyses of Protein .G in Enteric Peripheral Nervous Tissues by in vivo Cryotechnique Jiaorong Chen, Nobuo Terada, Nobuhiko Ohno, Sei Saitoh, Yurika Saitoh, Shinichi Ohno Department of Anatomy and Molecular Histology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi We have examined immunolocalization of protein 4.1G in peripheral nervous tissues of mouse large intestines with “in vivo cryotechnique” followed by freeze substitution. The 4.1G was mostly immunolocalized in Auerbach’s myenteric plexus. By immunofluorescence staining of 4.1G, GFAP and cKit, it was similarly immunolocalized with GFAP, but not with cKit. By preembedding immunoelectron microscopy, it was detected along glial cell membranes and their cytoplasmic processes around axon bundles. These findings indicate that 4.1G has some roles as adhesion and/or signal transduction in enteric glial cells of unmylinated nerve fibers in addition to myelination in the myelinated nerve ones. P in vivo in vitro 1 1 2 1 1 1 2 2 TJ TJ mesaxon, paranode, SchmidtLanterman autotypic tight junction TJ tricellulin TRIC, claudin19 cldn19, junctional adhesion moleculeC JAMC in vivo in vitro Myelin Protein Zero 13 P13 TJ TRICCldn19 JAMC 714 P714 Cldn19 JAMC 14 TRIC 21 TRIC 2 TJ 4 Cldn19 JAMC mesaxonparanode SchmidtLanterman TRIC mesaxon paranode SchmidtLanterman TJ Cldn19 JAMC TRIC P 1 2 2 1 2 1 1 2 10 14 MBP Calbindin Caspase3 Cux1 II/III, IV WGAHRP Laggard
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