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운동전략이 기립자세의 기능적 전방 팔뻗기에 미치는 영향
박제상,권오윤,최흥식,김택훈 한국전문물리치료학회 2000 한국전문물리치료학회지 Vol.7 No.1
The purpose of this study is to determine whether movement strategies affect functional forward reach distance in a standing position. Forty-seven healthy subjects were selected for this study: 23 men and 24 women, with an average age of 22.3. Functional forward reach distances were measured as hip strategy and squat strategy(included knee and ankle movement strategy) in a standing position, respectively. The mean values of functional forward reach distance in hip strategy, squat strategy were 33.57㎝, 29.48㎝, respectively. There was significantly difference in functional forward reach distance between hip strategy and squat strategy(p<.001). There was no difference of functional forward reach distance between male and female in hip strategy, but there was significant difference in other strategy(p<.05). These results suggest that movement strategies should be considered during functional forward reach test in standing. Further study is required to determine whether movement strategies affect functional reach distance in elderly and disabled groups.
착화제와 유기산이 Wistar rat체내의 Sr 분포에 미치는 영향
이기호,이제호,박상윤,이승훈,유용운,윤택구 대한방사선 방어학회 1990 방사선방어학회지 Vol.15 No.2
Wistar rat에 85SrCl2를 꼬리 정맥에 주사하여 체내 기관과 혈액 내 분포, 잔존율을 조사하였고 착화제와 유기산을 투여하여 혈장 단백질에 결합하는 Sr양의 변화를 측정하였다. 혈액내에서 Sr은 혈장에 60%, 세포에 40%부착되어 이동하였다. 혈장에 존재하는 Sr중 약 50%정도는 혈장 단백질과 결합한 상태였고, 세표에는 세포 표면에 가볍게 부착되어 있었다. Erythrocyte나 granulocyte보다 lymphocyte에 많은 양의 Sr이 부착되어 있었다. 투여후 초기 1시간 이내에 혈액 내에서 급격히 감소하여 뼈에 침착되었다. 이때 각 기관에서도 Sr의 잔존율은 24시간 이내에 크게 감소하였고, 뼈로 침착된 Sr은 24시간 이후에 서서히 감소하였다. 착화제 EDTA, EGTA 및 DTPA를 투여한 경우, 혈장 단백질에 결합하는 Sr의 양은 대조군의 57%에서 27-33%로 감소하였으며 citrate 및 oxalate의 투여시는 이값이 19%와 40%로 각각 감소하였다. 85SrCl2 was injected to the tail vein of Wistar rats and investigated its distribution and clearance in the tissues and blood. We also measured the changes in Sr binding to the blood plasma protein by administrating chelating agents and organic acids. For the blood, 60% of the Sr occurred in the plasma and 40% on the cell membrane. Fifty percent of Sr in the blood plasma was bound to plasma protein. Sr on the cell membrane seemed to be bound loosely. The binding in the lymphocyte was higher than in the erythrocyte and granulocyte. Within one hour Sr was quickly disappeared from the blood stream, to be accumulated in the bone. Twenty four hours after the injection, Sr decreased rapidly in the organs of soft tissue, but slowly in the bone. The binding of Sr to plasma protien decreased from 57% of the control to 27-33% in the group treated with chelating agents. EDTA. EGTA and DTPA and to 19% and 40% in the groups treated with organic acids, citrate and oxalate, respectively.
JNK2 silencing and caspase-9 activation by hyperosmotic polymer inhibits tumor progression
Garg, Pankaj,Pandey, Shambhavi,Hoon, Seonwoo,Jang, Kyoung-Je,Lee, Myung Chul,Choung, Yun-Hoon,Choung, Pill-Hoon,Chung, Jong Hoon Elsevier 2018 International journal of biological macromolecules Vol.120 No.2
<P><B>Abstract</B></P> <P>c-Jun N-terminal kinase 2 (JNK2) is primarily responsible for the oncogenic transformation of the transcription factor c-Jun. Expression of the proto-oncogene c-Jun progresses the cell cycle from G1 to S phase, but when its expression becomes awry it leads to uncontrolled proliferation and angiogenesis. Delivering a JNK2 siRNA (siJNK2) in tumor tissue was anticipated to reverse the condition with subsequent onset of apoptosis which predominantly requires an efficient delivering system capable of penetrating through the compact tumor mass. In the present study, it was demonstrated that polymannitol-based vector (PMGT) with inherent hyperosmotic properties was able to penetrate through and deliver the siJNK2 in the subcutaneous tumor of xenograft mice. Hyperosmotic activity of polymannitol was shown to account for the enhanced therapeutic delivery both in vitro and in vivo because of the induction of cyclooxygenase-2 (COX-2) which stimulates caveolin-1 for caveolae-mediated endocytosis of the polyplexes. Further suppression of JNK2 and hence c-Jun expression led to the activation of caspase-9 to induce apoptosis and inhibition of tumor growth in xenograft mice model. The study exemplifies PMGT as an efficient vector for delivering therapeutic molecules in compact tumor tissue and suppression of JNK2 introduces a strategy to inhibit tumor progression.</P> <P><B>Graphical abstract</B></P> <P>Hyperosmotic PMGT driven siJNK2 delivery in compact cancer cells inhibits c-jun phosphorylation resulting in tumor growth arrest via caspase-9 induction and apoptosis.</P> <P>[DISPLAY OMISSION]</P>
Yun, Sung-Ho,Choi, Chi-Won,Kwon, Sang-Oh,Park, Gun Wook,Cho, Kun,Kwon, Kyung-Hoon,Kim, Jin Young,Yoo, Jong Shin,Lee, Je Chul,Choi, Jong-Soon,Kim, Soohyun,Kim, Seung Il American Chemical Society 2011 Journal of proteome research Vol.10 No.2
<P><I>Acinetobacter baumannii</I> is a Gram-negative, nonmotile aerobic bacterium that has emerged as an important nosocomial pathogen. Multidrug-resistant (MDR) <I>A. baumannii</I> is difficult to treat with antibiotics, and treatment failure in infected patients is of great concern in clinical settings. To investigate proteome regulation in <I>A. baumannii</I> under antibiotic stress conditions, quantitative membrane proteomic analyses of a clinical MDR <I>A. baumannii</I> strain cultured in subminimal inhibitory concentrations of tetracycline and imipenem were performed using a combination of label-free (one-dimensional electrophoresis-liquid chromatography−tandem mass spectrometry) and label (isobaric tag for relative and absolute quantitation) approaches. In total, 484 proteins were identified, and 302 were classified as outer membrane, periplasmic, or plasma membrane proteins. The clinical <I>A. baumannii</I> strain DU202 responded specifically and induced different cell wall and membrane protein sets that provided resistance to the antibiotics. The induction of resistance-nodulation-cell division transporters and protein kinases, and the repression of outer membrane proteins were common responses in the presence of tetracycline and imipenem. Induction of a tetracycline resistant pump, ribosomal proteins, and iron-uptake transporters appeared to be dependent on tetracycline conditions, whereas β-lactamase and penicillin-binding proteins appeared to be dependent on imipenem conditions. These results suggest that combined liquid chromatography-based proteomic approaches can be used to identify cell wall and membrane proteins involved in the antibiotic resistance of <I>A. baumannii</I>.</P><P><I>Acinetobacter baumannii</I> is a Gram-negative, nonmotile aerobic bacterium that has emerged as an important nosocomial pathogen. To investigate proteome regulation in <I>A. baumannii</I> under antibiotic stress conditions, quantitative membrane proteomic analyses of a clinical multidrug-resistant <I>A. baumannii</I> strain cultured in subminimal inhibitory concentrations of tetracycline and imipenem were performed. Our results suggest that combined liquid chromatography-based proteomic approaches can be used to identify cell wall and membrane proteins involved in the antibiotic resistance of <I>A. baumannii</I>.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jprobs/2011/jprobs.2011.10.issue-2/pr101012s/production/images/medium/pr-2010-01012s_0004.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/pr101012s'>ACS Electronic Supporting Info</A></P>
Effects of Storage Buffer and Temperature on the Integrity of Human DNA
( Yun-tae Kim ),( Eun-hee Choi ),( Bo-kyoung Son ),( Eun-hee Seo ),( Eun-kyoung Lee ),( Je-kwon Ryu ),( Gi-won Ha ),( Jin-seon Kim ),( Mi-ran Kwon ),( Jae-hoon Nam ),( Young-jin Kim ),( Kyoung-ryul Le 대한임상검사과학회 2012 대한임상검사과학회지(KJCLS) Vol.44 No.1
In this study, we have examined the effects of the storage time and temperature on DNA quality and have also studied the effects of the hydration buffer in which DNA is dissolved. This study was performed using 160 human blood samples collected with informed consent from 2007 to 2008 in the hospital where this cohort study was performed. The DNA extracted was dissolved using distilled water (DW) or Tris-EDTA (TE) buffer, and stored in the deep freezer or refrigerator for up to 10 weeks at -70℃, -20℃, 4℃, and 25℃, respectively. DNA integrity was determined by the degree of smearing of DNA on the gel. After four weeks, all of the 20 DNA samples dissolved in DW and stored at 25℃ were entirely degraded. After 10 weeks, 6 of the 20 DNA samples dissolved in TE buffer and stored at 25℃ were fairly degraded, and 4 of the 20 DNA samples dissolved in DW and stored at 4℃ were fairly degraded. The 20 DNA samples dissolved in TE buffer and stored at 4℃ were stable for 10 weeks. DNA samples stored at -20℃ and -70℃ did not appear to degrade in either DW or TE buffer, even at the 10-week point. We suggest that TE buffer should use for DNA elution, in order to protect against degradation and to preserve DNA for a long period of time, and the samples should be stored at -20℃ or -70℃.