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1
The Release of Hepatic Triglyceride Lipase from Rat Monolayered Hepatocytes in Primary Culture

윤대헌(Tai Heon Yoon),Yamada N(Nobuhiro Yamada),Ishibashi S(Shun Ishibashi),Shimano H(Hitoshi Shimano),Gotohda T(Takanari Gotohda),Harada K(Kenji Harada),OAkanuma Y(Yasuo Akanuma),Murase T(Toshio Murase) 한국식품영양과학회 1991 한국식품영양과학회지 Vol.20 No.1
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쥐간세포 배양시 간트리글리세리드 lipase의 유리 및 호르몬 조절에 관하여 연구하였다. 배양 2일째 헤파린 첨가구 배양액에 유리된 lipase 활성은 24시간 동안 계속 증가하였다. 반면에 헤파린 무첨가의 lipase활성은 헤파린 첨가가우에 비하여 10%에 지나지 않았다. 간세포를 anti-hepatic triglyceride lipase IgG와 배양시 lipase 활성이 92%까지 저해되었다. Monensin 첨가시 lipase활성 저해는 61%였다. 인슐린은 lipase활성을 20% 상승시켰으며 dexamethasone은 44% 저해시켰다. 이상의 결과로 미루어 보아 간트리글리세리드 lipase는 헤파린 존재하에 분비 및 유리되며 그 분비는 호르몬에 의해 조절됨을 시사한다. The release of hepatic triglyceride lipase from cultured rat hepatocytes and its hormonal regulation were studied. The activity of lipase released into the medium in the presence of heparin was increasing during 24 hours on the 2nd day of culture, while this was 10% in the absence of heparin as compared with the lipase activity in the presense of heparin. When hepatocytes were cultured with anti-hepatic triglyceride lipase IgG, the lipase activity was suppressed by 92%. The results suggest that the enzyme released into culture medium is identical to hepatic triglyceride lipase which can be released only in the presence of heparin, the model of release being similar to that of lipoprotein lipase from adipocytes. The addition of monensin to the medium resulted in the inhibition of lipase secretion by 61%. Insulin enhanced lipase activity only 20%, whereas dexamethasone suppressed the activity by 44%. These data indicated that hepatic triglyceride lipase is secreted and released from hepatocytes in the presence of heparin and its secretion is regulated by hormones.
2
Histone deacetylase inhibitors promote neurosteroid-mediated cell differentiation and enhance serotonin-stimulated brain-derived neurotrophic factor gene expression in rat C6 glioma cells

Morita, Kyoji,Gotohda, Takako,Arimochi, Hideki,Lee, Mi-Sook,Her, Song Wiley Subscription Services, Inc., A Wiley Company 2009 Journal of neuroscience research Vol.87 No.11
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<P>Progesterone treatment has previously been reported to promote the differentiation of glial cells probably through the production of 5α-reduced neurosteroids, resulting in the enhancement of serotonin-stimulated brain-derived neurotrophic factor (BDNF) gene expression, which is considered to contribute to the survival, regeneration, and plasticity of neuronal cells in the brain and hence has been suggested to improve mood disorders and other symptoms in depressive patients. Based on these previous observations, the effects on glial cells of histone deacetylase (HDAC) inhibitors, which are known as agents promoting cell differentiation, were examined using rat C6 glioma cells as a model for in vitro studies. Consequently, trichostatin A (TSA), sodium butyrate (NaB), and valproic acid (VPA) stimulated glial fibrillary acidic protein (GFAP) gene expression, and their stimulatory effects on GFAP gene expression were inhibited by treatment of these cells with finasteride, an inhibitor of the enzyme producing 5α-reduced neurosteroids. In addition, HDAC inhibitors enhanced serotonin-stimulated BDNF gene expression, the enhancement of which could be abolished by the inhibition of 5α-reduced neurosteroid production in the glioma cells. These results suggest that HDAC inhibitors may be able to promote the differentiation of rat C6 glioma cells through the production of 5α-reduced neurosteroids, resulting in the enhancement of serotonin-stimulated BDNF gene expression as a consequence of promoting their differentiation, indicating the possibility that differentiated glial cells may be implicated in preserving the integrity of neural networks as well as improving the function of neuronal cells in the brain. © 2009 Wiley-Liss, Inc.</P>