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117 157<br />
P<br />
αMangostin <br />
1 2 3 1<br />
1<br />
2 <br />
3 <br />
HER2ER, PgR<br />
<br />
αMangostin <br />
<br />
MDAMB231 αMangostin<br />
Caspase <br />
c Realtime PCR <br />
<br />
<br />
Caspase389 <br />
Caspase4 <br />
c G1 S <br />
p21 Cip1 <br />
PCNACyclin D1cdc25ACdK2 Cdk6 <br />
Aktp38α ERK1/2 <br />
αMangostin Akt <br />
<br />
p21 Cip1 G1 G1 <br />
<br />
<br />
P<br />
Sevoflurane rat Per <br />
1,2 1 2 1<br />
1<br />
2 <br />
<br />
Per2 suprachiasmatic<br />
nucleus: SCN 24 <br />
mouse Per2 sevoflurane <br />
<br />
Ohe et al, 2010 SCN Per2 <br />
<br />
sevoflurane SCN <br />
Wister rat Per2 rPer2 mRNA <br />
RI in situ hybridizasion rPer2 <br />
Per2 <br />
<br />
rPer2 <br />
SCN rPer2<br />
25 rPer2<br />
sevofrurane <br />
SCN <br />
Per2 <br />
P<br />
Transverse anchoring system of myofibril to sarcolemma: the<br />
morphological study<br />
Khairani Astrid Feinisa, Yuki Tajika, Maiko Takahashi, Hitoshi Ueno,<br />
Tohru Murakami, Hiroshi Yorifuji<br />
Grad.Sch.of Medicine Gunma Univ.<br />
Transverse anchoring system of myofibril to sarcolemma is subplasmalemmal<br />
cytoskeleton network that is anchored into the sarcolemma and provides an<br />
overall diffuse protection system of skeletal muscle. Three types of filament have<br />
been indicated as the transverse anchoring system; γ actin, desmin, and keratin.<br />
We have examined these subsarcolemmal cytoskeletal components in diaphragm<br />
and lower limb muscles of adult wild type and mdx mice by electron microscopy<br />
EM and immunohistochemistry. Isolated single fibers as well as small blocks<br />
of the muscles are used for both methods. EM revealed that the intermediate<br />
filaments seemed to either connect between the sarcolemma and the Zdisc and<br />
Mline or run as a part of subsarcolemmal density. These filamentous networks<br />
apparently decrease in mdx mice. These data suggest a morphological model of<br />
transverse anchoring system and how it affects the functions of skeletal muscle.<br />
P<br />
<br />
Khairani Astrid Feinisa <br />
<br />
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<br />
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<br />
SNARE <br />
<br />
2 SNARE <br />
<br />
SNARE <br />
<br />
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P<br />
Prosaposin expression in cardiac muscle of mdx mice in early period<br />
of disease<br />
1 1 1 1 1 2 <br />
1<br />
1<br />
2 <br />
<br />
This study investigated the expression of the trophic factor prosaposin in the<br />
cardiac muscles of mdx mice. Prosaposin is strongly expressed in adult rat<br />
cardiac and skeletal muscles and plays a myotrophic role in vitro. However, few<br />
studies have focused on the role of prosaposin during muscle regeneration in mdx<br />
mice, which do not express the dystrophin gene. Dystrophin deficiency leads to<br />
progressive cardiac and skeletal muscle pathology. We examined the expression<br />
of prosaposin in the cardiac muscle in mdx and C57BL mice using HE staining,<br />
immunohistochemistry, and in situ hybridization in 4weekold mice. HE staining<br />
showed no obvious change in morphology of mdx cardiac muscles compared<br />
with control mice. The results of in situ hybridization showed that the main form<br />
of prosaposin mRNA is PS+0 in the cardiac muscle of mdx mice, and the mRNA<br />
expression is obviously lower in the cardiac muscles of mdx mice. Prosaposin<br />
protein also decreased in mdx cardiac muscle. These results suggest that the<br />
change of prosaposin expression happened earlier than morphological change in<br />
cardiac muscle of mdx mice.<br />
P<br />
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30%ST<br />
96 21<br />
34 56 58 42