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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:	BIBFORM033194
035-os BibID:	PMID:22056526
Első szerző:	Mendelboum Raviv, Shlomit (biológus)
Cím:	Coating conditions matter to collagen matrix formation regarding von Willebrand factor and platelet binding / Shlomit Mendelboum Raviv, Katalin Szekeres-Csiki, Attila Jenei, Janos Nagy, Boris Shenkman, Naphtali Savion, Jolan Harsfalvi
Dátum:	2012
ISSN:	0049-3848
Megjegyzések:	IntroductionVon Willebrand factor (VWF) and platelet binding needs a uniform collagen matrix therefore we aimed to find an optimal condition for the preparation of human type-I and type-III collagen matrices.MethodThe effects of pH, salt and ligand concentration and binding time were tested when collagen matrices were prepared by adsorption. Surface-bound collagen and collagen-bound VWF measured by specific antibodies. Platelet adhesion was tested under flow conditions at a shear rate of 1800 s? 1 for 2 min. Matrices and platelets were visualized by atomic force and scanning electron microscope.ResultsThe extent of human collagens type-I and III binding to the surface was 10 and 4 times greater and binding was maximal under 8?16 hours, when coated from physiological buffer solution versus acid solution. Collagen fibrils were more developed and platelet adhesion was higher, with more organized and denser aggregates. VWF binding was parallel to the surface bound collagen in both collagen types.ConclusionCollagen coating of surfaces for VWF binding and platelet adhesion studies is very variable from acid solution. Our experiments provide evidences that neutralizing the acid and adding NaCl in physiological concentration, thereby facilitating formation of collagen fibril molecules in solution, results in efficient coating of human type-I and type III collagens, which then bind normal VWF equally well.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Collagen matrix Von Willebrand factor Platelet adhesion Thrombus formation egyetemen (Magyarországon) készült közlemény
Megjelenés:	Thrombosis Research. - 129 : 4 (2012), p. e29-e35. -
További szerzők:	Szekeres-Csiki Katalin (1979-) (orvos) Jenei Attila (1966-) (biofizikus) Nagy János (biofizikus) Shenkman, Boris Savion, Naphtali Hársfalvi Jolán (1949-) (klinikai biokémikus)
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