이서구 / Rhee, Sue-Goo
석좌교수

Department / Institute / Center :
Lab of cell signaling/의생명과학부

Contact Information

Phone +82-2-2228-0600 Email rheesg@yuhs.ac Website

Educational Background

Undergraduate Education 1965 B.S., Seoul National University
Final Degree (University, Major) 1972 Ph. D., Catholic University of America (Organic chemistry)
Overseas Training (Institute, Supervisor) 1973 – 1975: Postdoctoral Fellow, Laboratory of Biochemistry
National Heart, Lung, and Blood Institute (NHLBI), National
Institutes of Health (NIH) Bethesda, MD (Drs. Earl R. Stadtman and Boon Chock)

Professional Societies and current positions

American Society of Biochemistry and Molecular Biology
American Chemical Society
The Society for Free Radical Biology and Medicine
The Korean Society for Molecular and Cellular Biology

Research Area(s)

Basic research
Research Field We discovered a family of peroxiredoxin (Prx) that catalyzes reduction of H2O2 and established that mammalian cells express six distinct Prx enzymes that not only protect against oxidative damage but also mediate cell signaling by modulating intracellular H2O2 levels. We showed that growth factors (EGF) induce a transient increase in intracellular H2O2 levels and that the essential cysteine of protein tyrosine phosphatases is the target of specific, reversible oxidation by H2O2 produced in cells stimulated with growth factors. These observations led to a new paradigm in receptor signaling wherein protein tyrosine phosphorylation is achieved not via activation of receptor protein tyrosine kinases alone, but through concurrent inhibition of protein tyrosine phosphatases by H2O2. Our studies revealed that Prx isozymes are extensively regulated via phosphorylation as well as hyperoxidation of the active site cysteine to cysteine sulfinic acid, with the reverse reaction catalyzed by sulfiredoxin. The reversible Prx cysteine hyperoxidation discovered by us proved critical for feedback regulation of steroidogenesis and constitutes a universal marker for circadian rhythms in all domains of life.
Diseases Diseases caused by defects in ROS metabolism or signaling
Possible Collaboration Intracellular messenger function of hydrone peroxidie in receptor signaling pathways..
Development of inhibitors of peroxiredoxin and sulfiredoxin as chemotherapeutics.
Effect of the disruption of circadian rhythm on various organ functions (Brown adipo tissue, heart, muscle, liver, adrenal gland).
Role of STAT3 in the signaling by cytokines and growth factors
Role of reactive oxygen species in fatty liver disease

Research Methods

Protein purification.
Assay of various antioxidant enzymes
Protein carbonylation assay
Surface plasmon resonance
Phage display
Develop intrabody

Lab.

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Location of Office ABMRC center
Location of Lab. ABMRC center 208호
Contact person Name: 길인섭 / Tel: 2228-0752 / E-mail: iskil@yuhs.ac

Major Published Articles and Books

1.Bae SH, Sung SH, Oh SY, Lim JM, Lee SK, Park YN, Lee HE, Kang D, Rhee SG. (2013). Sestrins activate Nrf2 by promoting p62-dependent autophagic degradation of Keap1 and prevent oxidative liver damage. Cell Metab. 8;17(1):73-84.
2.Kil IS, Lee SK, Ryu KW, Woo HA, Hu MC, Bae SH, Rhee SG. (2012). Feedback control of adrenal steroidogenesis via H2O2-dependent, reversible inactivation of peroxiredoxin III in mitochondria. Mol Cell. 8;46(5):584-94.
3.Bae, S. H., Sung, S. H., Cho, E. J., Lee, S. K., Lee, H. E., Woo, H. A., Yu, D.-Y.,, Kil, I. S. and Rhee, S. G (2011).: Concerted Action of Sulfiredoxin and peoxiredoxin I Protects Against Alcohol-Induced Oxidative Injury in Mouse Liver. Hepatology 53, 945-953, 2011
4.Woo HA, Yim SH, Shin DH, Kang D, Yu DY, Rhee SG. (2010). Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. Cell. 19;140(4):517-28.