• Title/Summary/Keyword: center in Seoul

Search Result 11,613, Processing Time 0.057 seconds

PROTEIN-CROSS-LINKING BY METHYLGLYOXAL

  • Lee, Cheolju;Kang, Sa-Ouk
    • Proceedings of the Korean Biophysical Society Conference
    • /
    • 1996.07a
    • /
    • pp.46-46
    • /
    • 1996

  • To elucidate the mechanism for the cross-linking reaction in the glycation or Maillard reaction, we studied the reaction between proteins, and a three-carbon ${\alpha}$-ketoaldehyde, methylglyoxal. When Cu, Zn-SOD was incubated with 200 mM of methylglyoxal, the peroxidase activity as well as the superoxide dismutase activity was reduced. This reduction is accompanied by the decrease of the anion binding affinity of the enzyme. (omitted)

  • PDF

Micromagnetic simulations based on directly observed microstructures

  • Lee, Je-Hyun;Kim, Sang-Koog
    • Proceedings of the Korean Magnestics Society Conference
    • /
    • 2011.12a
    • /
    • pp.9-10
    • /
    • 2011

  • We have prepared FePtCu L10 bit patterned media, of which magnetic properties and microstructural details are obtained by direct measurement and observations. The patterning process on the continuous film induced a drastic changes in the coercivity, SFD, and angular dependencies. The origin of the changes are explained by micromagnetic simulations with the finite element models including the details of the microstructures.

  • PDF

Free Radicals during the Oxidation and Reduction of Methylglyoxal-Modified Protein

  • Lee, Cheolju;Kang, Sa-Ouk
    • Proceedings of the Korean Biophysical Society Conference
    • /
    • 1997.07a
    • /
    • pp.36-36
    • /
    • 1997

  • Protein glycation was studied with bovine serum albumin (BSA) as a model protein and methylglyoxal, a 3-carbon ${\alpha}$-ketoaldehyde. Methylglyoxal reacted with BSA, forming a radical as observed in the reaction of methylglyoxal wtih L-alanine or N-acetyl-L-lysine.(omitted)

  • PDF

Expression of COX-2 and IDO by Uteroglobin Transduction in NSCLC Cell Lines (비소세포폐암 세포주에서 Uteroglobin Transduction이 COX-2 및 IDO의 발현에 미치는 영향)

  • Park, Gun Min;Lee, Sang-Min;Yim, Jae-Joon;Yang, Seok-Chul;Yoo, Chul Gyu;Lee, Choon-Taek;Han, Sung Koo;Sim, Young-Soo;Kim, Young Whan
    • Tuberculosis and Respiratory Diseases
    • /
    • v.66 no.4
    • /
    • pp.274-279
    • /
    • 2009

  • Background: Uteroglobin (UG) is a secretary protein that has strong immunomodulatory properties, and which is synthesized in most epithelia including lung tissue. Overexpression of UG is associated with decreased expression of cyclooxygenase (COX)-2 and suppression of cancer cell growth. Indoleamine 2,3-dioxygenase (IDO) catalyzes tryptophan along the kynurenine pathway, and both the reduction in local tryptophan and the production of tryptophan metabolites contribute to the immunosuppressive effects of IDO. Methods: In this study, we investigated the pattern of expression of COX-2 and IDO, and the effect of UG transduction in the expression of COX-2 and IDO in several non-small cell lung cancer cell lines, especially A549. Results: Both COX-2 and IDO were constitutionally expressed in A549 and H460 cells, and was reduced by UG transduction. In A549 cells, the slightly increased expression of COX-2 and IDO with the instillation of interferon-gamma (IFN-$\gamma$) was reduced by UG transduction. However, the reduced expression of COX-2 and IDO by UG transduction was not increased with IFN-$\gamma$ instillation in A549 cells. In both the A549 COX-2 sense and the A549 COX-2 anti-sense small interfering RNA (siRNA)-transfected cells, IDO was expressed; expression was reduced by UG transduction, irrespective of the expression of COX-2. Conclusion: The results suggest that the anti-proliferative function of UG may be associated with the immune tolerance pathway of IDO, which is independent of the COX-2 pathway.

  • https://doi.org/10.4046/trd.2009.66.4.274 인용 PDF KSCI