ADHESIVENESS EVALUATION OF ACTIVATED PLATELET USING Arg-Gly-Asp-Phe(RGDF)-IMMOBILIZED SURFACE

  • Kim, J.H. (Institute of Medical and Biological Engineering, Medical Research Center Seoul National University) ;
  • Kim, H.J. (Institute of Medical and Biological Engineering, Medical Research Center Seoul National University) ;
  • Kim, J. (Institute of Medical and Biological Engineering, Medical Research Center Seoul National University) ;
  • Ryu, G.H. (Department of Medical Devices and Radiation Health, Korea Food and Drug Administration) ;
  • Min, B.G. (Institute of Medical and Biological Engineering, Medical Research Center Seoul National University) ;
  • Choe, T.B. (Department of Microbiological Engineering, College of Engineering, Kon-Kuk University)
  • Published : 1997.11.28

Abstract

The adhesion of activated and normal platelets to fibrinogen requires the receptor binding site of GPIIb/IIIa. These recognition sites exists in the A ${\alpha}$ chain(RGDS at 572-575 and RGDF at 95-98) and the carboxy-terminal of ${\gamma}$ chain (HHLGGAKQAGDV at 400-411) of fibrinogen. In this study, we developed RGDF-immobilized surface to detect the unctional state of platelet. RGDF-immobilized surface was prepared on the glass using photolithographic technology. Platelet adhesion to RGDF-immobilized surface was observed by staining platelets with mepacrine using a fluorescence microscope using mepacrine. Using the RGDF peptide of fragment E, we observed that the platelets pretreated with PGE1 interacted incompletely with RGDF-immobilized surface, whereas ADP activated platelets interacted with the surface extensively. These results show that the distinct selectivity of RGDF-immobilized micro-patterned surface can be used to detect the unctional state of platelets.

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