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117 117<br />
OFPMVIII<br />
α <br />
<br />
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<br />
<br />
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<br />
<br />
<br />
NPC1L1 <br />
<br />
LC3II <br />
NPC1L1<br />
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Lamp1 Ragulator <br />
p18 Lamp1 mTOR <br />
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α1 ATZ <br />
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α1<br />
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OFPMVIII<br />
E HRD <br />
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<br />
ERassociated<br />
degradation; ERAD unfolded<br />
protein response; UPR E3 <br />
HRD1 ERAD UPR <br />
<br />
ERAD UPR <br />
HRD1 <br />
<br />
ICR 6 4% <br />
HRD1 Abgent1.25 μg/ml<br />
<br />
HRD1 <br />
<br />
<br />
<br />
HRD1 <br />
<br />
OFPMVIII<br />
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1 2 2<br />
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<br />
[Aim] We investigated the influence of the adrenal glands over the preservation<br />
of gap junctions between folliculostellate cells in the anterior pituitary glands of<br />
rats. [Maerials and Methods] 60 dayold WistarImamichi strain male rats were<br />
prepared. The animals were divided into six groups: untreated control, untreated<br />
but given 0.9 % NaCl drinking water, castrated, adrenalectomized, castrated and<br />
adrenalectomized, and castrated and adrenalectomized with the administration<br />
of testosterone. Five rats from each group were killed 1, 2, 3, 4, 5, 6 and 7<br />
days after the operation, and prepared for observation by transmission electron<br />
microscopy. [Results] The simultaneous removal of adrenal glands with castration<br />
resulted in the significantly decreasing effects of gap junctions, and the additional<br />
administration of testosterone to these rats could compensate for the decreasing<br />
effects of gap junctions, while few mitotic hormoneproducing granular cells<br />
were found. [Conclusion] These observations indicate that the preservation of gap<br />
junctions between folliculostellate cells is mainly dependent on the testosterone<br />
from both testes and adrenal glands in adult male rats.<br />
OGPMIV<br />
NEX <br />
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<br />
<br />
<br />
<br />
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<br />
NEX Math2 bHLHtype transcriptional factor <br />
Cre <br />
<br />
NEX <br />
<br />
OGPMIV<br />
FLRT Unc <br />
1,2 Falko Hampel 2 3 Daniel del Toro 2 <br />
Manuela Schwark 4 Elena Kvachnina 4 Martin Bastmeyer 5 3 <br />
Victor Tarabykin 4 Joaquim Egea 2 Ruediger Klein 2<br />
1<br />
2 MaxPlanck Institute of<br />
Neurobiology 3 4 MaxPlanck<br />
Institute for Experimental Medicine 5 Karlsruher Institute fuer Technologie<br />
<br />
<br />
<br />
FLRT <br />
Unc5 <br />
FLRT2 Unc5D UL2<br />
<br />
Unc5D UL2 <br />
RNA <br />
FLRT2 VVI UL2 <br />
IV Unc5D <br />
FLRT2/ UL2 <br />
FLRT2 UL2 <br />
<br />
OGPMIV<br />
Implications for cooperative versus noncooperative actions of the<br />
subunits of NatB, Mdm and Nat in mouse embryonic brain<br />
Kyoji Ohyama 1 , Kunihiko Yasuda 1 , Kazuko Onga 1 , Akira Kakizuka 2 ,<br />
Nozomu Mori 1<br />
1<br />
Dept. of Anatomy and Neurobiology, Grad. Sch. Biomedical Sciences, Nagasaki<br />
Univ., 1124 Sakamoto, Nagasaki 8528523, Japan, 2 Lab. of Functional Biology,<br />
Kyoto Univ. Grad. Sch.Biostudies, Kyoto 6068501, Japan<br />
The NatB complex, Nat5/Mdm20 acetyltransferase mediates Nacetylation to<br />
control cell cycle progression and actin dynamics in yeast. As yet, little is known<br />
about their expression patterns in multicellular organisms. Here we show that<br />
Mdm20 is highly expressed in mouse embryonic brain. At E11.5, Mdm20 was<br />
widely expressed in both neural progenitors and early differentiating neurons,<br />
whereas Nat5 was expressed in Sox1/3+/Mdm20+ neural progenitors. By E14.5,<br />
both Mdm20 and Nat5 were downregulated in ventricular zone neural progenitors,<br />
whereas both protein expression were found in differentiating neurons and<br />
maintained at E18.5 in derivatives of these cells, such as midbrain dopaminergic<br />
DA neurons. Intriguingly, our data also showed that Mdm20 is not always co<br />
expressed with Nat5 in all differentiated neurons, for example deep cerebellar<br />
neurons. Moreover, Mdm20 is also not necessarily colocalised with Nat5 within<br />
Nat5+/Mdm20+ midbrain DA neurons. Given that Nat5 is only a known member<br />
of Nat family protein that interacts with Mdm20, our data imply that Mdm20 may<br />
function either with an unidentified Nat protein partners or possibly in a Nat<br />
independent manner.