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임은주,오용석,신원호,진병관,정재영,신민상,김동운,장진혁,김형준,하창만,정운주,문경준,김상룡 한국식품영양과학회 2019 Journal of medicinal food Vol.22 No.3
Parkinson's disease (PD) and Alzheimer's disease exhibit common features of neurodegenerative diseases and can be caused by numerous factors. A common feature of these diseases is neurotoxic inflammation by activated microglia, indicating that regulation of microglial activation is a potential mechanism for preserving neurons in the adult brain. Recently, we reported that upregulation of prothrombin kringle-2 (pKr-2), one of the domains that make up prothrombin and which is cleaved and generated by active thrombin, induces nigral dopaminergic (DA) neuronal death through neurotoxic microglial activation in the adult brain. In this study, we show that silibinin, a flavonoid found in milk thistle, can suppress the production of inducible nitric oxide synthase and neurotoxic inflammatory cytokines, such as interleukin-1β and tumor necrosis factor-α, after pKr-2 treatment by downregulating the extracellular signal-regulated kinase signaling pathway in the mouse substantia nigra. Moreover, as demonstrated by immunohistochemical staining, measurements of the dopamine and metabolite levels, and open-field behavioral tests, silibinin treatment protected the nigrostriatal DA system resulting from the occurrence of pKr-2-triggered neurotoxic inflammation in vivo. Thus, we conclude that silibinin may be beneficial as a natural compound with anti-inflammatory effects against pKr-2-triggered neurotoxicity to protect the nigrostriatal DA pathway and its properties, and thus, may be applicable for PD therapy.
망막아세포종 세포주(Y-79)의 Arylalkylamine N-acetyltransferase 활성에 미치는 Dopamine의 영향
김석민,정미영,윤경식,진병관,백행운,백형환,조용호 慶熙大學校 1997 論文集 Vol.26 No.-
The arylalkylamine N-acetyltransferase(AA-NAT, EC 2.3.1.87) in vertebral pineal gland and retina is rate-limiting enzyme in the pathway of biosynthesis of melatonin. AA-NAT activities are remarkably increased during night with 10-150 folds. Neurohormone melatonin is thought to play roles in a broad range of physiological functions in human, primarily through effects on the biological clock in the suprachiasmatic nucleus of the hypothalamus, This rhythm reflects large changes in the activities of AA-NAT. So the important regulatory role of AA-NAT has made it central interest in research on melatonin biochemistry and neurochemical signal transduction. The neurotransmitter that regulates the AA-NAT activities is norepinephrine, which acts through a cyclic AMP mechanism. The effect of dopamine on AA-NAT in human retinoblastoma Y-79 cells was studied. the obtained results are as follows; AA-NAT activities in Y-79 cells were increased by cyclic AMP, and dopamine inhibited the AA-NAT activities stimulated by forskolin. The pattern of inhibition of dopamine on the AA-NAT activities in Y-79 cells was time and concentration dependent. The results suggest that dopamine participates in the regulation of the AA-NAT activities through the inhibitory mechanism in the human pineal and retinal tissues.
Escherichia coli(M15)을 이용한 serotonin N-acetyltransferase 유전자의 발현
김용만,정미영,윤경식,진병관,백행운,조용호,백형환 慶熙大學校 1997 論文集 Vol.26 No.-
AA-NAT cDNA was obtained by RT-PCR technique from total RNA of rat sacrified at night(02:00am). pCRNAT was cloned using the pCRII vector with insertion of AA-NAT cDNA(about 1.4 kb) at EcoRI site. For the expression of the gene, pQECNAT was subcloned, in which the coding region of AA-NAT was inserted into expression vector pQE30 at BamHI and HindIII sites. According to the experimental results, Escherichia coli strain M15, transformed by the expession vector pQECNAT, was selected as a host to express AA-NAT gene with the induction of isopropyl β-D-thiogalactoside(IPTG). Optimal condition for the expression of AA-NAT gene was achieve from the experimental results, showing that the expression of the protein was inducible much 19.800 ± 2,200 dpm per ml of culture volume in 4 hours at the concentration of 2 mM IPTG. Partial purification through the affinity column(Ni-NTA agarose) binding to the continuous 6 histidine residues of protein resulted in 5 times more increase in the specific activity of AA-NAT than that of the homogenate of bacterial pellet. These experimental results will provide basic data in further study for the enzymatic kinetics and antibody production of AA-NAT.