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001-es BibID:	BIBFORM004685
Első szerző:	Mátyus László (biofizikus)
Cím:	Organization of the glycoprotein (GP) IIb/IIIa heterodimer on resting human platelets studied by flow cytometric energy transfer / Matyus, L., Bene, L., Harsfalvi, J., Alvarez, M. V., Gonzalez-Rodriguez, J., Jenei, A., Muszbek, L., Damjanovich, S.
Dátum:	2001
Megjegyzések:	Glycoprotein IIb/IIIa is a heterodimer of glycoproteins IIb and IIIa which serves as the inducible receptor for fibrinogen and other adhesive proteins at the surface of platelets. Although a model of the quaternary structure of the GPIIb/IIIa molecule has been constructed in solution by Calvete et al. [Biochem. J. 282 (1992) 523], a corresponding model at the surface of intact platelets is still missing. In the present work conformation and lateral distribution of the GPIIb/IIIa heterodimer were studied at a nanometer resolution on the surface of resting human platelets under physiological conditions. The experiments were based on dual wavelength flow cytometric detection of fluorescence resonance energy transfer and application of a panel of monoclonal antibodies raised against well described binding sites. Monodisperse distribution of the GPIIb/IIIa heterodimer has been observed and a detailed three-dimensional proximity map of antibody binding sites was constructed on the platelet membrane, under physiological conditions, for the first time. Our data support the view that the GPIIb subunit is in a bent conformation. A detailed analysis of the K(d)-values and the number of binding sites for a set of monoclonal antibodies was also carried out giving supplementary data for the topology of the binding sites. Our results provide a refinement of the membrane-topology of the GPIIb/IIIa heterodimer.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban analysis Animal Antibodies,Monoclonal Binding Sites Blood Platelets Dimerization Energy Transfer Flow Cytometry Fluorescence Glycoproteins Human Hungary metabolism Mice Platelet Glycoprotein GPIIb-IIIa Complex Support, Non-U.S.Gov't egyetemen (Magyarországon) készült közlemény
Megjelenés:	Journal of Photochemistry and Photobiology. B, Biology. - 65 : 1 (2001), p. 47-58. -
További szerzők:	Bene László (1963-) (biofizikus) Hársfalvi Jolán (1949-) (klinikai biokémikus) Alvarez, M. V. Gonzalez-Rodriguez, J. Jenei Attila (1966-) (biofizikus) Muszbek László (1942-) (haematológus, kutató orvos) Damjanovich Sándor (1936-2017) (biofizikus)
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001-es BibID:	BIBFORM004714
Első szerző:	Novák Levente (biológus)
Cím:	Shear-dependent morphology of von Willebrand factor bound to immobilized collagen / Novak, L., Deckmyn, H., Damjanovich, S., Harsfalvi, J.
Dátum:	2002
Megjegyzések:	We have developed an immunogold von Willebrand factor (VWF) detection method that permits almost complete coverage of individual VWF molecules, and by this unequivocal localization and morphologic analysis of collagen-bound VWF by atomic force microscopy (AFM). Perfusion of gel filtration-purified VWF in parallel plate perfusion chambers over glass coverslips coated with calf skin collagen, followed by AFM imaging in air, enabled us to assess possible morphologic differences between VWF bound at low (0.07 N/m(2) = 0.7 dynes/cm(2)) and high (4.55 N/m(2) = 45.5 dynes/cm(2)) shear stresses. No significant differences in VWF morphology were found, the molecules were oriented almost randomly, and there were no clear signs of VWF "uncoiling" either at a high or at a low shear regime. After perfusing 1 microg/mL VWF for 5 minutes, surface coverage at high shear was almost twice the one seen at low shear, and some larger and more irregularly shaped VWF molecules could be seen at high shear. This difference disappeared, however, at 15 minutes of perfusion and was probably caused by diffusion kinetics. Moreover, the presence of 68 x 10(9)/L washed fixed platelets in the perfusate did not have any visible effect on VWF morphology at high versus low shear stress. These findings suggest that shear stress does not influence significantly the overall molecular morphology of VWF during its binding to collagen-coated surface and are consistent with a constitutively expressed affinity of collagen-bound VWF for glycoprotein Ib.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban analysis Animal Blood Platelets Cattle chemistry Collagen Type I Diffusion Human Hungary Immunohistochemistry Kinetics metabolism methods Microscopy Microscopy,Atomic Force pathology Perfusion Platelet Adhesiveness Protein Binding Stress,Mechanical Support,Non-U.S.Gov't ultrastructure von Willebrand Factor
Megjelenés:	Blood. - 99 : 6 (2002), p. 2070-2076. -
További szerzők:	Deckmyn, Hans Damjanovich Sándor (1936-2017) (biofizikus) Hársfalvi Jolán (1949-) (klinikai biokémikus)
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