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Streptomyces subrutilus P5가 생산하는 철 함유 superoxide dismutase의 분비
박재승,김재헌,Park, Jae-seung,Kim, Jae-heon 한국미생물학회 2015 미생물학회지 Vol.51 No.2
본 연구에서는 Streptomyces subrutilus P5의 생장과 세포내 외 철 함유 superoxide dismutase 활성을 비교 분석하여 철함유 superoxide dismutase의 분비 시점을 확인하고 분자 수준에서 이 효소의 분비에 관여하는 유전정보를 확인하고자 하였다. Streptomyces subrutilus P5의 균체 생장은 건체 중량을 측정하여 결정하였다. Glucose는 log phase에서 급격히 소모되어 24시간 후에 이르러 완전히 고갈되었다. 세포내의 철 함유 superoxide dismutase는 배양 후 3시간에 나타나며 세포외 철 함유 superoxide dismutase는 배양 후 7.5시간부터 나타난다. 따라서 superoxide dismutase는 용균에 의해서가 아니라 능동적인 분비기작에 의해서 세포 외로 분비된 것으로 추측할 수 있다. Streptomyces subrutilus P5의 sodF에는 signal peptide 유전정보가 존재하지 않았다. 그러나 sodF의 상류지역에서 다른 세균의 type III 분비단백질 유전자와 유사한 type III 분비상자가 발견되었다. Streptomyces 균주에서 type III 분비단백질이 존재할 가능성이 있음을 처음으로 제시하였다. We tried to analyze the growth time for secretion of the iron containing superoxide dismutase by comparing the intra-and extracellular enzyme activity from Streptomyces subrutilus P5 and analyze possible genetic information for this enzyme secretion. The mycelial dry weights and glucose concentrations in culture filtrates were determined during growth. Glucose was consumed rapidly during logarithmic growth phase and almost exhausted at 24 h of cultivation. While the intracellular activity of iron containing superoxide dismutase was first appeared at three hours, the extracellular activity of this enzyme appeared from 7.5 h of cultivation, early logarithmic growth phase. This early presence of the superoxide dismutase might not be the result of cell lysis but active secretion pathway. There was no information for signal peptide responsible for the enzyme secretion in sodF. However, we found a type three secretion box in the promoter region of sodF that has been known for the genes of type III secreted proteins in other bacteria. This is the first report on the possible existence of type III secretion in Streptomyces.
Enhancement of potency and stability of human extracellular superoxide dismutase
( Sung Hwan Kim ),( Hae Young Kim ),( Jung Ho Kim ),( Jung Hye Choi ),( Won Kook Ham ),( Yoon Jae Jeon ),( Hara Kang ),( Tae Yoon Kim ) 생화학분자생물학회(구 한국생화학분자생물학회) 2015 BMB Reports Vol.48 No.2
Cells express several antioxidant enzymes to scavenge reactive oxygen species (ROS) responsible for oxidative damages and various human diseases. Therefore, antioxidant enzymes are considered biomedicine candidates. Among them, extracellular superoxide dismutase (SOD3) had showed prominent efficacy against asthma and inflammation. Despite its advantages as a biomedicine, the difficulty in obtaining large quantity of active recombinant human SOD3 (rhSOD3) has limited its clinical applications. We found that a significant fraction of overexpressed rhSOD3 was composed of the inactive apo-enzyme and its potency against inflammation depended on the rate of metal incorporation. Also, purified rhSOD3 was unstable and lost its activity very quickly. Here, we suggest an ideal preparative method to express, purify, and store highly active rhSOD3. The enzymatic activity of rhSOD3 was maximized by incorporating metal ions into rhSOD3 after purification. Also, albumin or polyethylene glycol prevented rapid inactivation or degradation of rhSOD3 during preparative procedures and long-term storage. [BMB Reports 2015; 48(2): 91-96]
Human extracellular superoxide dismutase (EC-SOD) expression in transgenic chicken
Sung June Byun,Mi Ran Ji,Ye Jin Jang,A In Hwang,Hee Kyoung Chung,Jeom Sun Kim,Kyung Woon Kim,Hak Jae Chung,Byoung Chul Yang,Ik Soo Jeon,Jin Ki Park,Jae Gyu Yoo,Tae Yoon Kim 생화학분자생물학회(구 한국생화학분자생물학회) 2013 BMB Reports Vol.46 No.8
Kim, Hae-Young,Sah, Shyam Kishor,Choi, Sung S.,Kim, Tae-Yoon Elsevier 2018 Life sciences Vol.210 No.-
<P><B>Abstract</B></P> <P><B>Aims</B></P> <P>Several anti-melanogenic molecules have been developed or identified, but their uses are limited due to either adverse effects or instability during the treatment. We aimed to evaluate the effects of extracellular superoxide dismutase (SOD3), a powerful antioxidant, as a candidate anti-melanogenic molecule.</P> <P><B>Main methods</B></P> <P>UVB-induced reactive oxygen species (ROS) production and proliferation in melan-a cells was evaluated by 6-carboxy-2′,7′-dichlorodihydrofluorescein diacetate staining and bromodeoxyuridine incorporation assay, respectively. Quantitative real-time polymerase chain reaction and western blot were performed to detect the melanogenesis-related gene expression and downstream signaling. Anti-melanogenic effects of SOD3 were also evaluated using SOD3 transgenic mice under UVB exposure in-vivo condition.</P> <P><B>Key findings</B></P> <P>SOD3 inhibited UVB-induced proliferation, ROS production and melanogenesis in melanocytes. Measurement of melanin content and tyrosinase activity assays showed that SOD3 significantly inhibited melanin synthesis. Moreover, these suppressive effects of SOD3 were dependent on the endothelin-1 (ET-1)/endothelin B receptor, protein kinase C, melanocortin 1 receptor/protein kinase A, Wnt7a/β-catenin, and mitogen-activated protein kinase pathways, with concomitant downregulation of microphthalmia-associated transcription factor, tyrosinase, and tyrosinase-related proteins 1, dopachrome tautomerse. Interestingly, SOD3 was found to inhibit transforming growth factor-beta 1 (TGF-β1) to inactivate the ET-1 signaling pathway, and finally prevents the production of melanin.</P> <P><B>Significance</B></P> <P>Our results provide novel insights into the role of SOD3 in melanocyte homeostasis and its uses as a potential biomedicine to treat hyperpigmentary conditions of the skin.</P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>