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1.

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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2.

001-es BibID:BIBFORM073777
Első szerző:Pályu Eszter
Cím:Major changes of von Willebrand factor multimer distribution in cirrhotic patients with stable disease or acute decompensation / Eszter Palyu, Jolan Harsfalvi, Tamas Tornai, Maria Papp, Miklos Udvardy, Katalin Szekeres-Csiki, Lajos Pataki, Karen Vanhoorelbeke, Hendrik B. Feys, Hans Deckmyn, Istvan Tornai
Dátum:2018
ISSN:0340-6245
Megjegyzések:Background and aims: There is an unstable balance between pro- and anti-haemostatic processes in patients with cirrhosis. We hypothesized, that in patients with acute decompensation (AD) the major alterations of von Willebrand factor (VWF) could contribute to the prothrombotic situation as compared to patients with stable (ST) cirrhosis. Methods: We analyzed different parameters of VWF, including detailed multimer distribution by densitometry and platelet adhesion together with ADAMTS13 activity and antigen and C-reactive protein (CRP) levels in patients with ST (n=99), with AD (n=54) and controls (n=92). Results: VWF antigen, ristocetin cofactor as well as collagen binding activities were elevated in both cirrhotic groups in a stepwise manner. There was a decrease in high and an increase in low molecular weight multimer ratios in the majority of ST cirrhosis. However, in 24 out of 54 AD patients ultra-large VWF multimers (ULMWM) were found. ADAMTS13 activity in ST and AD patients without ULMWM was similar to controls [median, (IQR)%: 98 (67-132) and 91 (60-110) vs. 106 (88-117), respectively]. The presence of ULMWM in AD patients was associated with low ADAMTS13 activity [33 (24-49)%] and high CRP level [23 (7.1-83.6)mg/l]. Adhesion of normal platelets showed a stepwise increase in the presence of cirrhotic plasmas, reaching the highest level in AD patients with ULMWM. Conclusion: Characteristic changes of VWF parameters are seen in ST cirrhosis. In AD patients highly increased VWF and reduced ADAMTS13 activity could be found, along with the presence of ULMWM, which are possible markers and contributors of the disease progression.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
cirrhosis
acute decompensation
systemic inflammation
von Willebrand factor multimers
trhombotic microangiopathy
Megjelenés:Thrombosis and Haemostasis. - 118 : 8 (2018), p. 1397-1408. -
További szerzők:Hársfalvi Jolán (1949-) (klinikai biokémikus) Tornai Tamás István (1984-) (belgyógyász) Papp Mária (1975-) (belgyógyász, gasztroenterológus) Udvardy Miklós (1947-) (belgyógyász, haematológus) Szekeres-Csiki Katalin (1979-) (orvos) Pataki Lajos Vanhoorelbeke, Karen Feys, Hendrik B. Deckmyn, Hans Tornai István (1954-) (belgyógyász, gasztroenterológus)
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3.

001-es BibID:BIBFORM010452
Első szerző:Szántó Tímea
Cím:Identification of a VWF peptide antagonist that blocks platelet adhesion under high shear conditions by selectively inhibiting the VWF-collagen interaction / Szanto, T., Vanhoorelbeke, K., Toth, G., Vandenbulcke, A., Toth, J., Noppe, W., Deckmyn, H., Harsfalvi, J.
Dátum:2009
ISSN:1538-7933 (Print)
Megjegyzések:Because the collagen-VWF-GPIb/IX/V axis plays an important role in thrombus formation, it represents a promising target for development of new antithrombotic agents. Objectives: We used phage display to identify potential small peptides that interfere with the VWF-collagen binding and might serve as lead products for the development of possible oral antithrombotic compounds. Methods: A random linear heptamer peptide library was used to select VWF-binding peptides. Results: We identified a phage clone, displaying the YDPWTPS sequence, further referred to as L7-phage, that bound to VWF in a specific and a dose-dependent manner. This L7-phage specifically inhibited the VWF-collagen interaction under both static and flow conditions. Epitope mapping using deletion mutants of VWF revealed that the L7-phage does not bind to the known collagen-binding A3 domain within VWF, but to the more carboxyterminal situated C domain. This inhibition was not due to steric hindrance of the A3 domain-collagen interaction by the L7-phage. Indeed, a tetrabranched multi-antigen peptide (MAP) presenting four copies of the peptide, but not the scrambled MAP, also inhibited VWF-collagen interaction under conditions of high shear stress at a concentration of 148 nmol L<sup>-1</sup>. Conclusions: Based on these results, we conclude that we have identified the first peptide antagonist that binds to the VWF C domain and by this specifically inhibits the VWF binding to collagen, suppressing platelet adhesion and aggregation under high shear conditions. As a consequence, this peptide and its future derivates are potentially interesting antithrombotic agents.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Antithrombotic therapy
Collagen
Peptide inhibitor
Phage display
Platelet adhesion
Von Willebrand factor
antithrombocytic agent
collagen
epitope
unclassified drug
von Willebrand factor
amino acid sequence
article
biopanning
carboxy terminal sequence
concentration response
controlled study
deletion mutant
drug mechanism
drug protein binding
drug screening
human
normal human
phage display
priority journal
protein binding
protein domain
protein protein interaction
shear stress
stereospecificity
thrombocyte adhesion
thrombocyte aggregation inhibition
Collagen
Dose-Response Relationship
Drug
Drug Design
Drug Evaluation
Preclinical
Epitope Mapping
Fibrinolytic Agents
Hemorheology
Humans
Oligopeptides
Peptide Library
Platelet Adhesiveness
Platelet Aggregation
Platelet Aggregation Inhibitors
Protein Binding
Stress
Mechanical
von Willebrand Factor
Megjelenés:Journal of Thrombosis and Haemostasis. - 7 : 10 (2009), p. 1680-1687. -
További szerzők:Vanhoorelbeke, Karen Tóth Gábor (Szeged) Vandenbulcke, A. Tóth Judit (1978-) (laboratóriumi szakorvos) Noppe, W. Deckmyn, Hans Hársfalvi Jolán (1949-) (klinikai biokémikus)
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4.

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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5.

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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