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Hwang, Onyou,Na, Doesun,Song, Kyuyoung,Cho, Sung-Woo,Lee, Jae Dam 울산대학교 의과대학 1992 울산의대학술지 Vol.1 No.1
Histamine은 부신 수질 세포의 H₁수용체 활성화를 통한 phosphatidylinositide 가수 분해와 함께 catecholamine 유리를 촉진시킨다고 알려진 바 있다. 본 논문에서는 histamine의 세포 내 작용 기전을 밝히고자 histamine이 catecholamine 생합성 효소인 phenylenolamine N-methytransferase(PNMT)의 유전자 발현 및 catecholamine유리에 미치는 영향을 연구하였다. Histamine에 의한 catecholamine유리는 세포 외 calcium 유입에 의존적이었으나, 세포 내 저장 calcium과는 무관하였고, reserpine 및 탈분극에 의한 유리와 비슷한 수준이었다. Protein kinase C(PKC) 활성제 TPA에 의한 유리와 구별 될 수 없었으며, 그 억제제인 staurosporin에 의해 억제되었다. 또한, histamine은 PNMT mRNA를 증가시켰는데, 이 현상은 TPA에 의한 증가와 동일하며, dantrolene에 의한 차이는 없었으나, PKC 억제제인 sphingosine에 의해 억제되었다. 이상의 결과는 histamine이 chromaffin세포에서 PKC활성화를 통하여 catecholamine 유리 및 PNMT 유전자 발현의 증가시킴으로 catecholamine의 유리와 합성을 연결시킴을 시사하였다.
Dopamine β-Hydroxylase : Past, Present and Future
황온유 한국생화학분자생물학회 1990 생화학분자생물학회 소식 Vol.10 No.2
Dopamine β-hydroxylase (DBH) is one of the four enzymes in the catecholamine biosynthetic pathway and catalyzes the conversion of dopamine to norepinephrine. This paper reviews what is known about the distribution, localization, regulation, catalysis of this important neurotransmitter synthesizing enzyme. It further discusses the structure of DBH with emphasis on the structural complexity existing in multiple forms, and the recent cDNA cloning and primary structural analysis. The significance of the work on this enzyme done thus far is discussed and the direction of further research in this field proposed.
Shin, Eun Sil,Hwang, Onyou,Hwang, Yu-Shik,Suh, Jun-Kyo Francis,Chun, Young Il,Jeon, Sang Ryong The Korean Neurosurgical Society 2014 Journal of Korean neurosurgical society Vol.56 No.5
Objective : Neural tissue transplantation has been a promising strategy for the treatment of Parkinson's disease (PD). However, transplantation has the disadvantages of low-cell survival and/or development of dyskinesia. Transplantation of cell aggregates has the potential to overcome these problems, because the cells can extend their axons into the host brain and establish synaptic connections with host neurons. In this present study, aggregates of human brain-derived neural stem cells (HB-NSC) were transplanted into a PD animal model and compared to previous report on transplantation of single-cell suspensions. Methods : Rats received an injection of 6-OHDA into the right medial forebrain bundle to generate the PD model and followed by injections of PBS only, or HB-NSC aggregates in PBS into the ipsilateral striatum. Behavioral tests, multitracer (2-deoxy-2-[$^{18}F$]-fluoro-D-glucose ([$^{18}F$]-FDG) and [$^{18}F$]-N-(3-fluoropropyl)-2-carbomethoxy-3-(4-iodophenyl)nortropane ([$^{18}F$]-FP-CIT) microPET scans, as well as immunohistochemical (IHC) and immunofluorescent (IF) staining were conducted to evaluate the results. Results : The stepping test showed significant improvement of contralateral forelimb control in the HB-NSC group from 6-10 weeks compared to the control group (p<0.05). [$^{18}F$]-FP-CIT microPET at 10 weeks posttransplantation demonstrated a significant increase in uptake in the HB-NSC group compared to pretransplantation (p<0.05). In IHC and IF staining, tyrosine hydroxylase and human ${\beta}2$ microglobulin (a human cell marker) positive cells were visualized at the transplant site. Conclusion : These results suggest that the HB-NSC aggregates can survive in the striatum and exert therapeutic effects in a PD model by secreting dopamine.
Role of matrix metalloproteinase‐3 in neurodegeneration
Kim, Eun‐,Mee,Hwang, Onyou Blackwell Publishing Ltd 2011 Journal of Neurochemistry Vol.116 No.1
<P> <I>J. Neurochem.</I> (2011) <B>116,</B> 22–32.</P><P><B>Abstract</B></P><P>Matrix metalloproteinase‐3 (MMP‐3) is a member of the class of zinc‐dependent proteases known to degrade the extracellular matrix. MMP‐3 activity is regulated at three different levels: gene expression, proteolytic activation of the zymogen, and inhibition by the endogenous tissue inhibitors of metalloproteinase. A line of evidence indicates a role of MMP‐3 in neurodegeneration. In neuronal cells, MMP‐3 expression is increased in response to cell stress, and the cleaved, active MMP‐3 participates in apoptotic signaling. In the extracellular space, MMP‐3 triggers microglia to produce proinflammatory and cytotoxic molecules as well as MMP‐3, which in turn contribute to neuronal damage. MMP‐3 is increased in various experimental models of Parkinson’s disease that are produced by selective toxins and by inflammagen, and the neuronal death is attenuated by various ways that inhibit MMP‐3. α‐Synuclein, whose gene mutations are associated with familial forms of Parkinson’s disease, is proteolyzed by MMP‐3. Contribution of MMP‐3 toward the pathogenesis of Alzheimer’s disease and other neurodegenerative diseases has also been suggested. Thus, modulation of MMP‐3 expression and/or activity could be of therapeutic value for neurodegenerative diseases.</P>