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001-es BibID:	BIBFORM043577
Első szerző:	Cauwenberghs, Nancy
Cím:	Epitope mapping of inhibitory antibodies against platelet glycoprotein Ibalpha reveals interaction between the leucine-rich repeat N-terminal and C-terminal flanking domains of glycoprotein Ibalpha / Cauwenberghs N., Vanhoorelbeke K., Vauterin S., Westra D. F., Romo G., Huizinga E. G., Lopez J. A., Berndt M. C., Harsfalvi J., Deckmyn H.
Dátum:	2001
ISSN:	0006-4971
Megjegyzések:	The interaction of von Willebrand factor (vWF) with the platelet receptor glycoprotein Ibalpha (GPIbalpha) is important for platelet adhesion at high shear stress. Two functionally important antigenic areas within GPIbalpha were identified through the characterization of 5 new inhibitory anti-GPIb monoclonal antibodies (mAbs). The binding sites of 3 of these anti-GPIb mAbs, which were intercompeting and potently inhibiting shear stress-induced binding of vWF, were mapped within the N-terminal amino acid (aa) 1-59 area by the use of canine-human chimeras. These antibodies, however, had little or no effect (approximately 40% inhibition) on the binding of vWF induced by either botrocetin or ristocetin. On the other hand, the anti-GPIb mAbs 24G10 and 6B4, which blocked GPIb-vWF binding under all conditions examined, bound to 2 different regions of GPIbalpha, aa 1-81 and aa 201-268, respectively. The epitope for 6B4 was further narrowed by phage display revealing 2 sets of peptide sequences aligning within aa 259-262 and aa 230-242. In the latter region of GPIbalpha, the gain-of-function platelet-type von Willebrand disease (PT-vWD) mutations have been identified. Alignment was partially confirmed because the binding of 6B4 to recombinant GPIbalpha fragments carrying either one of the PT-vWD mutations was considerably impaired but not completely abolished. In contrast, mAb 24G10 bound more strongly to mutant PT-vWD GPIbalpha. However, although 24G10 competed with 6B4 for binding to platelets, it bound to an epitope within aa 1-81 of GPIbalpha. In conclusion, 2 functionally important areas within GPIbalpha were identified: one localized within the leucine-rich repeat N-terminal aa 1-59 area and one composed of residues aa 1-81 in close contact with aa 201-268. Moreover, further support is provided for the existence of an intramolecular interaction between the N-terminal flanking (aa 1-81) and C-terminal flanking (aa 201-268) regions.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban glycoprotein Ibalpha
Megjelenés:	Blood. - 98 : 3 (2001), p. 652-660. -
További szerzők:	Vanhoorelbeke, Karen Vauterin, Stephan Westra, Douwe F. Romo, Gabriel Huizinga, Eric G. Lopez, José A. Berndt, Michael C. Hársfalvi Jolán (1949-) (klinikai biokémikus) Deckmyn, Hans
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001-es BibID:	BIBFORM043579
Első szerző:	Cauwenberghs, Nancy
Cím:	Antithrombotic effect of platelet glycoprotein Ib-blocking monoclonal antibody Fab fragments in nonhuman primates / Cauwenberghs N., Meiring M., Vauterin S., van Wyk V., Lamprecht S., Roodt J. P., Novák L., Harsfalvi J., Deckmyn H., Kotzé H. F.
Dátum:	2000
Megjegyzések:	Platelet adhesion in arterial blood flow is mainly supported by the platelet receptor glycoprotein (GP) Ib, which interacts with von Willebrand factor (vWF) that is bound to collagen at the site of vessel wall injury. Antibody 6B4 is a monoclonal antibody (MoAb) raised against purified human GPIb. MoAb 6B4 inhibits both ristocetin- and botrocetin-induced, vWF-dependent human platelet agglutination. MoAb 6B4 furthermore blocks shear-induced adhesion of human platelets to collagen I. We studied the antithrombotic effect of this inhibitory murine MoAb 6B4 in a baboon model of arterial thrombosis. When injected into baboons, intact IgG and its F(ab')(2) fragments caused almost immediate thrombocytopenia, whereas injection of the Fab fragments alone did not. Fab fragments were subsequently used to investigate their in vivo effect on platelet deposition onto a thrombogenic device, consisting of collagen-rich, glutaraldehyde-fixed bovine pericardium (0.6 cm(2)), at a wall shear rate ranging from 700 to 1000 s(-1). Baboons were either pretreated with Fabs to study the effect of inhibition on platelet adhesion or treated 6 minutes after placement of the thrombogenic device to investigate the effect on interplatelet cohesion. Pretreatment of the animals with bolus doses ranging from 80 to 640 microgram/kg Fab fragments significantly reduced (111)In-labeled platelet deposition onto the collagen surface by approximately 43% to 65%. Only the highest dose caused a significant prolongation (doubling) of the bleeding time. Ex vivo ristocetin-induced platelet agglutination was equally reduced. Treatment with a bolus of 110 microgram/kg Fab fragments after a thrombus was allowed to form for 6 minutes had no effect on further platelet deposition. We therefore conclude that Fab fragments or derivatives of inhibitory anti-GPIb antibodies may be useful compounds to prevent thrombosis.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban platelet adhesion platelet aggregation thrombosis glycoprotein Ib monoclonal antibodies
Megjelenés:	Arteriosclerosis, Thrombosis, and Vascular Biology. - 20 : 5 (2000), p. 1347-1353. -
További szerzők:	Meiring, Muriel Vauterin, Stephan van Wyk, Veronika Lamprecht, Seb Roodt, Jan P. Novák Levente (1967-) (biológus) Hársfalvi Jolán (1949-) (klinikai biokémikus) Deckmyn, Hans Kotzé, Harry F.
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001-es BibID:	BIBFORM002138
Első szerző:	Szántó Tímea
Cím:	The A/T1381 polymorphism in the A1-domain of von Willebrand factor influences the affinity of von Willebrand factor for platelet glycoprotein Ibalpha / Szanto T., Schlammadinger A., Staelens S., De Meyer S. F., Freson K., Pareyn I., Vauterin S., Harsfalvi J., Deckmyn H., Vanhoorelbeke K.
Dátum:	2007
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Thrombosis Haemostasis. - 98 : 1 (2007), p. 178-185. -
További szerzők:	Schlammadinger Ágota (1971-) (belgyógyász, haematológus) Staelens, Stephanie De Meyer, Simon F. Freson, Kathleen Pareyn, Inge Vauterin, Stephan Deckmyn, Hans Vanhoorelbeke, Karen Hársfalvi Jolán (1949-) (klinikai biokémikus)
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001-es BibID:	BIBFORM002137
Első szerző:	Szántó Tímea
Cím:	Type 2B von Willebrand disease in seven individuals from three different families : phenotypic and genotypic characterization / Szanto T., Schlammadinger A., Salles I., Pareyn I., Vauterin S., Harsfalvi J., Vanden Bulcke A. M., Deckmyn H., Vanhoorelbeke K.
Dátum:	2007
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Thrombosis Haemostasis. - 98 : 1 (2007), p. 251-254. -
További szerzők:	Schlammadinger Ágota (1971-) (belgyógyász, haematológus) Salles, Isabelle Pareyn, Inge Vauterin, Stephan Vanden Bulcke, Anne-Marie Deckmyn, Hans Vanhoorelbeke, Karen Hársfalvi Jolán (1949-) (klinikai biokémikus)
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