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116 117 OFPMVI Biodiversity and hepatic stellate cells Haruki Senoo 1 , Yoshihiro Mezaki 1 , Mitsutaka Miura 1 , Katsuyuki Imai 1 , Kiwamu Yoshikawa 1 , Mayako Morii 1 , Mutsunori Fujiwara 2 , Rune Blomhofff 3 1 Dept. Cell Biology and Morphology, Akita Uni. Grad. Sch. Med., 2 Divis. Clinical Pathol, Japanese Red Cross Med. Center, 3 Dept. Nutrition, Inst. Basic Med. Sci, Fac. Med., Univ. Oslo Hepatic stellate cells HSCs exist in the space between hepatocytes and sinusoidal endothelial cells, and store 5080% of vitamin A in the whole body as retinyl palmitate in lipid droplets in the cytoplasm. We have performed a systematic characterization of the hepatic vitamin A storage in animals of the Svalbard archipelago and Greenland, and compared that in polar bears kept in zoos. The top predators contained about 1020 times more vitamin A than all other arctic animals studied as well as their genetically related continental top predators. This massive amount of hepatic vitamin A was located in large lipid droplets in HSCs. The contents of retinyl esters in the liver for polar bear kept in zoos were dependent on vitamin A content in the diet. The development of such an efficient vitamin Astoring mechanism in HSCs may have contributed to the survival of top predators in the extreme environment of the arctic. HSC that has capacity of taking up and storing of a large amount of vitamin A plays pivotal roles in maintenance of food web, food chain, biodiversity, and eventually ecology of the arctic. OFPMVI A 1 1 1 1,2 1 1 1 1 2 A A A perilipin 2/ADRPperilipin 3/TIP47 ADRP TIP47 A A TIP47 A A ADRPTIP47 A ADRPTIP47 A 24 A TIP47 7 A TIP47 A A A TIP47 A A 24 7 TIP47 A A TIP47 ADRP A OFPMVI IEL DNA CD3 IEL 30 IEC DNA 2 IEC IEC DNA DNA DNA IEL IEC DNA IEL BGrB IEL GrB IEC DNA GrB IEC DNA Pfn/GrB DNA IEL Pfn GrB IEL Pfn DNA GrB DNA 3 IEL IEC DNA Pfn/GrB Pfn GrB DNA OFPMVII SU p Src SU6656 5F9A DNA BrdU DNA BrdU S 2 2 SU6656 p53 siRNA p53 SU6656 p53 Nutlin SU6656 SU6656 p53 p53 OFPMVII 1 1 1 1 2 1 2 2 1 A single cKit A single A aligned cKit A1 A single A paired Np95 OFPMVII HORMAD HORMAD1HORMAD2 Hop1 HORMA HORMAD1 HORMAD1 HORMAD2 HORMAD2 HORMAD2 XYbody HORMAD2 SPO11 HORMAD2 SPO11 HORMAD2 HORMAD1 HORMAD2 HORMAD2 HORMAD1 HORMAD2
117 117 OFPMVIII α NPC1L1 LC3II NPC1L1 Lamp1 Ragulator p18 Lamp1 mTOR α1 ATZ α1 OFPMVIII E HRD ERassociated degradation; ERAD unfolded protein response; UPR E3 HRD1 ERAD UPR ERAD UPR HRD1 ICR 6 4% HRD1 Abgent1.25 μg/ml HRD1 HRD1 OFPMVIII 1 2 2 1 2 [Aim] We investigated the influence of the adrenal glands over the preservation of gap junctions between folliculostellate cells in the anterior pituitary glands of rats. [Maerials and Methods] 60 dayold WistarImamichi strain male rats were prepared. The animals were divided into six groups: untreated control, untreated but given 0.9 % NaCl drinking water, castrated, adrenalectomized, castrated and adrenalectomized, and castrated and adrenalectomized with the administration of testosterone. Five rats from each group were killed 1, 2, 3, 4, 5, 6 and 7 days after the operation, and prepared for observation by transmission electron microscopy. [Results] The simultaneous removal of adrenal glands with castration resulted in the significantly decreasing effects of gap junctions, and the additional administration of testosterone to these rats could compensate for the decreasing effects of gap junctions, while few mitotic hormoneproducing granular cells were found. [Conclusion] These observations indicate that the preservation of gap junctions between folliculostellate cells is mainly dependent on the testosterone from both testes and adrenal glands in adult male rats. OGPMIV NEX NEX Math2 bHLHtype transcriptional factor Cre NEX OGPMIV FLRT Unc 1,2 Falko Hampel 2 3 Daniel del Toro 2 Manuela Schwark 4 Elena Kvachnina 4 Martin Bastmeyer 5 3 Victor Tarabykin 4 Joaquim Egea 2 Ruediger Klein 2 1 2 MaxPlanck Institute of Neurobiology 3 4 MaxPlanck Institute for Experimental Medicine 5 Karlsruher Institute fuer Technologie FLRT Unc5 FLRT2 Unc5D UL2 Unc5D UL2 RNA FLRT2 VVI UL2 IV Unc5D FLRT2/ UL2 FLRT2 UL2 OGPMIV Implications for cooperative versus noncooperative actions of the subunits of NatB, Mdm and Nat in mouse embryonic brain Kyoji Ohyama 1 , Kunihiko Yasuda 1 , Kazuko Onga 1 , Akira Kakizuka 2 , Nozomu Mori 1 1 Dept. of Anatomy and Neurobiology, Grad. Sch. Biomedical Sciences, Nagasaki Univ., 1124 Sakamoto, Nagasaki 8528523, Japan, 2 Lab. of Functional Biology, Kyoto Univ. Grad. Sch.Biostudies, Kyoto 6068501, Japan The NatB complex, Nat5/Mdm20 acetyltransferase mediates Nacetylation to control cell cycle progression and actin dynamics in yeast. As yet, little is known about their expression patterns in multicellular organisms. Here we show that Mdm20 is highly expressed in mouse embryonic brain. At E11.5, Mdm20 was widely expressed in both neural progenitors and early differentiating neurons, whereas Nat5 was expressed in Sox1/3+/Mdm20+ neural progenitors. By E14.5, both Mdm20 and Nat5 were downregulated in ventricular zone neural progenitors, whereas both protein expression were found in differentiating neurons and maintained at E18.5 in derivatives of these cells, such as midbrain dopaminergic DA neurons. Intriguingly, our data also showed that Mdm20 is not always co expressed with Nat5 in all differentiated neurons, for example deep cerebellar neurons. Moreover, Mdm20 is also not necessarily colocalised with Nat5 within Nat5+/Mdm20+ midbrain DA neurons. Given that Nat5 is only a known member of Nat family protein that interacts with Mdm20, our data imply that Mdm20 may function either with an unidentified Nat protein partners or possibly in a Nat independent manner.
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