Mr. Khon Chan Huynh
Molecular Vascular Biology
Institute for Hemostasis and Transfusion Medicine
Heinrich Heine University Medical center
Moorenstr. 5, Geb. 12.49.00 R 011
40225 Düsseldorf, Germany
Mini Academic CV
University degrees:First degree or intermediate examination:
- B.Sc. 2006, University of Agriculture and Forestry, Ho Chi Minh, Vietnam.
- M.Sc. 2009, Ajou University, Suwon, Korea.
- H.W. Lee, T.I. Kim, K.H. Chan, M.H. Kwon, J.S. Kim, M. Jin, and Y.S. Kim, Inducing rigid local structure around the zinc-binding region by hydrophobic interactions enhances the homotrimerization and apoptotic activity of zinc-free TRAIL. Biochem Biophys Res Commun 62 (2007) 766-72.
- Khon HC, Lee HW, Kim TI, Kwon MH, Jin MS and Kim YS, “TRAIL Engineering for trimeric stability and apoptotic activity without zinc ion: Brief study about the working of Arg 227 in the absence of zinc ion” – Poster in International Symposium, KMB meeting 2007, Seoul, Korea.
- The 3rd antibody engineering symposium 2007, Mountain Jiri, Korea.
- Spring KSBB meeting and international symposium, Jeonchu 2008, Korea.
- The 4th antibody engineering symposium, Mountain Deogyu 2008, Korea.
- Brain Korea 21 fellowship (2006-2008)
- Graduate scholarship, Ajou University (2006-2008)
- Scholarship for outstanding academic achievement, Nong Lam University (2005-2006)
BioStruct PhD projectβ3-Integrin-Dependent Fibrillogenesis of Macromolecular RGD-Ligands in Relation to Biome-chanic Stress
Integrins and their ligands are prominent players regulating interactions of the extracellular environment and cellular functions. Sensing the biomechanic microenvironment integrins bidirectionally transmit conformational changes across the membrane. The resulting signals modulate cytoskeletal functions (outside-in signalling) and vice versa the cytoskeleton regulates the molecular relationship between receptor molecules and their ligands (inside-out signalling). Thus, mechanotransduction of ligand-occupied integrins regulate stable but flexible interactions between neighbouring cells. This is particular true for cells which are exposed to shear forces. The integrins αIIbβ3 and αvβ3 both incorporate the same β-subunit. β3-integrins bind RGD containing ligands e.g. fibronectin (Fn), fibrinogen and von Willebrand Faktor (vWF). Whereas Fn is a core component of extracellular matrices fibrinogen and vWF are plasmatic proteins. Fn and vWF are of a compact structure. They are unfolded by either shear stress or β3-integrins and cell traction forces modulate their fibrillogenesis. In our project we focus on the dynamic of β3-integrin-ligand interaction in response to conformational and functional changes upon exposure to shear stress. In a flow model we use human platelets or cell lines expressing β3-integrins to measure fibrillogenesis of Fn in response to mechanotransduction. Therefore, fluorescently labelled Fn is used to measure e.g. disappearance of fluorescence resonance energy transfer (FRET). To assess the specific role of the β3-subunit, two isoforms (Leu33 and Pro33) are compared because the Pro33 isoform is a risk determinant of acute coronary syndromes due to a prothrombotic characteristics like enhanced platelet adhesion and increased outside-in signaling.
Topic Supervisor: Dr. Volker R. Stoldt, Dept. Hemostasis and Transfusion Medicine, Heinrich Heine University Medical Center, Stoldt Group
Complementary Supervisor: Prof. Dr. Dieter Willbold, DInstitute of Physical Biology, Heinrich Heine University Düsseldorf, Willbold Group
Complementary Supervisor: Prof. Dr. Rüdiger Scharf, Institut für Hämostaseologie und Transfusionsmedizin
BioStruct Fellow: Mr. Khon Chan Huynh
Last updated: 22.11.2012, 14:20