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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.
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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.
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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
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1 2 2 1 2
1
1
2
10
14
MBP
Calbindin
Caspase3
Cux1
II/III, IV
WGAHRP
Laggard