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1.

001-es BibID:BIBFORM035082
Első szerző:Cauwenberghs, Nancy
Cím:Fc-receptor Dependent Platelet Aggregation Induced by Monoclonal Antibodies against Platelet Glycoprotein Ib or von Willebrand Factor / Nancy Cauwenberghs, Agotha Schlammadinger, Stephan Vauterin, Susan Cooper, Gretel Descheemaeker, István Tornai, Hans Deckmyn
Dátum:2001
ISSN:0340-6245
Megjegyzések:In this paper we describe two pathways leading to platelet activation by crosslinking glycoprotein (GP) Ibalpha to the platelet Fc-receptor (FcgammaRII). First the monoclonal antibody (MoAb) 9C8, raised against human platelet GPIbalpha, dose-dependently induced platelet aggregation of citrate-anticoagulated platelet-rich plasma, an effect that can be inhibited by several activation inhibitors. The FcgammaRII-inhibitory MoAb IV.3 was able to prevent the aggregatory effects of MoAb 9C8, indicating that crosslinking of the antigen GPIbalpha to the FcgammaII-receptor is necessary for the activating effect. Secondly we observed a synergistic activating effect of two anti-von Willebrand factor (vWF) MoAbs IC1E7 and B724, both known to enhance vWF binding to GPIbalpha in the presence of shear or ristocetin. When these antibodies are added together to PRP, platelet aggregation is induced without further need for an additional modulator. This effect can be blocked by either MoAb IV.3 or an inhibitory anti-GPIb MoAb, indicating that again the platelet activation results from signaling through FcgammaRII crosslinked to vWF bound to GPIbalpha. In addition, both the anti-GPIb MoAb 9C8, or the two anti-vWF MoAbs 1C1E7 and B724 induce genuine platelet activation, as evidenced by the secretion of ATP and protein tyrosine phosphorylation. These findings with both anti-GPIb and anti-vWF MoAbs add further proof to recent reports demonstrating an interaction between the platelet receptors GPIb and FcgammaRII, suggesting a role for the FcgammaII-receptor in GPIb-related signaling.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Monoclonal antibody
von Willebrand factor
glycoprotein Ib
FeyII-receptor
külföldön készült közlemény
platelet activation
Megjelenés:Thrombosis and Haemostasis. - 85 : 4 (2001), p. 679-685. -
További szerzők:Schlammadinger Ágota (1971-) (belgyógyász, haematológus) Vauterin, Stephan Cooper, Susan Descheemaeker, Gretel Tornai István (1954-) (belgyógyász, gasztroenterológus) Deckmyn, Hans
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM034925
Első szerző:Deckmyn, Hans
Cím:An echistatin-like Arg-Gly-Asp (RGD)-containing sequence in the heavy chain CDR3 of a murine monoclonal antibody that inhibits human platelet glycoprotein IIb/IIIa function / Deckmyn H., Stanssens P., Hoet B., Declerck P. J., Lauwereys M., Gansemans Y., Tornai I., Vermylen J.
Dátum:1994
ISSN:0007-1048
Megjegyzések:We describe the production and biochemical characterization of the first GPIIb/IIIa-inhibiting monoclonal antibody that contains an RGD sequence in the CDR3 region of the heavy chain. Monoclonal antibodies obtained by immunizing mice with human platelets were screened using consecutive ELISAs based on human platelets and immuno-affinity-purified glycoprotein (GP) IIb/IIIa coated on microtitre plates. Out of 30 monoclonal antibodies reacting with GPIIb/IIIa, one, MA-16N7C2, potently inhibited platelet aggregation induced by ADP, thrombin, arachidonic acid, collagen, U46619, adrenaline and platelet-activating factor, whereas ristocetin-induced aggregation was unaffected. MA-16N7C2 (IgG2a) bound approximately 4 times faster to activated than to resting platelets, with a Kdcalc of 6.6nM and of 17.5nM, respectively. Equilibrium binding studies to non-activated platelets showed a Kd of 18.2nM with 41 x 10(3) binding sites per platelet. The antibody recognized GPIIb/IIIa only as a Ca(2+)-dependent complex. MA-16N7C2 blocked fibrinogen and von Willebrand factor binding to GPIIb/IIIa in a competitive manner with a Ki of 8.5nM and 13.2nM, respectively. Sequence analysis revealed a RGD-containing sequence with homology to disintegrins, in the CDR3 region of the heavy chain. That this RGD-containing sequence could be involved in the interaction of the antibody to GPIIb/IIIa was finally indicated by showing that the binding is completely and competitively inhibited by echistatin.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
antiplatelet
disintegrin
integrin
antibody sequence
külföldön készült közlemény
Megjelenés:British Journal Of Haematology. - 87 : 3 (1994), p. 562-571. -
További szerzők:Stanssens, Patrick Hoet, Bernard Declerck, Paul J. Lauwereys, Marc Gansemans, Yannick Tornai István (1954-) (belgyógyász, gasztroenterológus) Vermylen, Jozef
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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3.

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)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM035072
Első szerző:Tornai István (belgyógyász, gasztroenterológus)
Cím:Acquired Bernard-Soulier syndrome : a case with necrotizing vasculitis and thrombosis / Istvan Tornai, Zoltan Boda, Agota Schlammadinger, Attila Juhasz, Nancy Cauwenberghs, Hans Deckmyn, Jolan Harsfalvi
Dátum:1999
Megjegyzések:We describe a patient with positive antinuclear antibodies, polyclonal gammopathy and high level of circulating immunocomplexes, resulting in vascular purpura. In addition, the patient had a slightly prolonged bleeding time and an isolated defect of ristocetin-induced platelet aggregation (RIPA) in platelet-rich plasma (PRP). The patient's plasma also inhibited RIPA in normal PRP and in normal platelet suspension. The activity and multimeric structure of plasmatic von Willebrand factor showed no alteration. We could demonstrate an autoantibody against platelet membrane glycoprotein (GP) Ib, using an ELISA-type assay. These data suggest an acquired Bernard-Soulier syndrome. We suggest that the patient had an immunocomplex-mediated leukocytoclastic vasculitis accompanied by production of antinuclear autoantibodies as well as the presence of an autoantibody against GPIb. The titer of the anti-GPIb antibody, however, was too low to induce significant platelet-type bleeding tendency, only laboratory alterations were found. Moreover, in a later stage of her disease, she developed a severe necrotizing vasculitis which was followed by a deep venous thrombosis.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Haemostasis. - 29 : 4 (1999), p. 229-236. -
További szerzők:Boda Zoltán (1947-) (belgyógyász, haematologus, klinikai onkológus) Schlammadinger Ágota (1971-) (belgyógyász, haematológus) Juhász Attila (1970-) (szakorvos, klinikai mikrobiológus) Cauwenberghs, Nancy Deckmyn, Hans Hársfalvi Jolán (1949-) (klinikai biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM034913
Első szerző:Tornai István (belgyógyász, gasztroenterológus)
Cím:Von Willebrand faktor-ellenes monoklonális antitestek kísérletes és gyakorlati alkalmazása / Tornai István, Arnout Jef, Deckmyn Hans, Declerck Paul, Peerlinck Kathelijne, Boda Zoltán, Vermylen Jos
Dátum:1994
Tárgyszavak:Orvostudományok Klinikai orvostudományok magyar nyelvű folyóiratközlemény hazai lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Magyar Belorvosi Archívum. - 47 : 6 (1994), p. 441-447. -
További szerzők:Arnout, Jef Deckmyn, Hans Declerck, Paul J. Peerlinck, Kathelijne Boda Zoltán (1947-) (belgyógyász, haematologus, klinikai onkológus) Vermylen, Jozef
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:BIBFORM034911
Első szerző:Tornai István (belgyógyász, gasztroenterológus)
Cím:Measurement of von Willebrand Factor Antigen in Plasma and Platelets with an Enzyme-Linked Immunosorbent Assay Based on Two Murine Monoclonal Antibodies / I. Tornai, P. J. Declerck, L. Smets, J. Arnout, H. Deckmyn, K. M. J. Caekebeke-Peerlinck, J. Vermylen
Dátum:1991
ISSN:0301-0147
Megjegyzések:Two murine monoclonal antibodies, raised against von Willebrand factor (vWF), were used to construct an enzyme-linked immunosorbent assay (ELISA), for quantitation of vWF antigen (vWFAg) in human plasma and platelets. This assay had a lower limit of sensitivity of 0.0001 IU/ml in buffer, and thus is one to two orders of magnitude more sensitive than other ELISA assays which have been reported. The intraassay, interassay and interdilution coefficients of variation were 4.1, 10.4 and 9.9%, respectively. In normal plasma (n = 20), the vWFAg level was 0.83 (range: 0.42-1.25) IU/ml. In normal washed platelets (n = 10), 0.35 (0.25-0.49) IU/10(9) platelets was found. In plasma obtained from various patient groups the following vWFAg levels (geometric mean and range) were observed: von Willebrand's disease (n = 19): 0.18 (0.02-0.77) IU/ml; patients with liver cirrhosis (n = 20): 3.73 (1.68-9.20) IU/ml; patients with pregnancy-induced hypertension (n = 20): 4.14 (2.28-7.44) IU/ml and patients with malignant disease (n = 10), 2.54 (1.51-5.60) IU/ml. A linear correlation was found between vWFAg levels measured with a polyclonal antibody based Laurell electroimmunoassay (r = 0.92, n = 58) or with a polyclonal antibody based ELISA (r = 0.94, n = 64). The present assay is based on stable and reproducible reagents and allows the specific measurement of vWFAg in plasma and in platelets. This assay may constitute a useful tool for the further investigation of clinical conditions associated with changes in vWFAg levels. In addition, its high sensitivity may facilitate a more detailed study of platelet vWFAg in normal and in pathological conditions.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Monoclonal antibodies
külföldön készült közlemény
Immunosorbent assay
Plasma von Willebrand factor
Platelet von Willebrand factor
Megjelenés:Hemostasis. - 21 : 3 (1991), p. 125-134. -
További szerzők:Declerck, Paul J. Smets, L. Arnout, Jef Deckmyn, Hans Caekebeke-Peerlinck, K. M. J. Vermylen, Jozef
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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7.

001-es BibID:BIBFORM034425
035-os BibID:(PMID)8423224
Első szerző:Tornai István (belgyógyász, gasztroenterológus)
Cím:A monoclonal antibody recognizes a von Willebrand factor domain within the amino-terminal portion of the subunit that modulates the function of the glycoprotein IB- and IIB/IIIA-binding domains / Istvan Tornai, Jef Arnout, Hans Deckmyn, Kathelijne Peerlinck, Jos Vermylen
Dátum:1993
ISSN:0021-9738 1558-8238
Megjegyzések:We developed a monoclonal antibody, 1C1E7, against vWf that increases ristocetin-induced platelet aggregation in a dose-dependent manner and lowers the threshold concentration of ristocetin needed to obtain a full aggregatory response. The platelet aggregatory effect of asialo vWf (ASvWf) also is enhanced by 1C1E7, in the presence or absence of glycoprotein (GP) IIb/IIIa receptor antagonism. In the presence of ristocetin, both intact 1C1E7 and its Fab fragments enhance specific binding of 125I-vWf to platelets. With 1C1E7, the intermediate and higher molecular weight multimers of vWf are preferentially bound to both GP Ib and GP IIb/IIIa. Thrombin-induced 125I-vWf binding to GP IIb/IIIa also is increased by 1C1E7. Maximal binding of 1C1E7 to vWf corresponds to 0.97 mol/mol vWf monomer with a Kd of 4.7 x 10(-10) M. 1C1E7 reacts with a 34/36-kD tryptic fragment (III-T4) and a 34-kD plasmic fragment (P34), which localizes the epitope between amino acid residues 1 and 272; this was confirmed by NH2-terminal amino acid sequencing. Finally, platelet aggregation by ASvWf was associated with a sharp rise in intracellular Ca2+ only in the presence of 1C1E7. An antibody-mediated conformational change of vWf may result in an improved presentation of the GP Ib- and GP IIb/IIIa-binding domains of mainly the larger multimers; the increased density of vWf on the platelet surface leads to platelet activation. The antibody may thus recognize a domain of relevance for vWf physiology.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
külföldön készült közlemény
Megjelenés:The Journal of Clinical Investigation. - 91 : 1 (1993), p. 273-282. -
További szerzők:Arnout, Jef Deckmyn, Hans Peerlinck, Kathelijne Vermylen, Jozef
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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8.

001-es BibID:bibEBI00018624
Első szerző:Ulrichts, Hans
Cím:A monoclonal antibody directed against human von Willebrand factor induces type 2B-like alterations / Ulrichts, H., Hársfalvi, J., Bene, L., Matkó, J., Vermylen, J., Ajzenberg, N., Baruch, D., Deckmyn, H., Tornai, I.
Dátum:2004
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Thrombosis and Haemostasis. - 2 : 9 (2004), p. 1622-1628. -
További szerzők:Hársfalvi Jolán (1949-) (klinikai biokémikus) Bene László (1963-) (biofizikus) Matkó János (1952-) (biológus) Vermylen, Jozef Ajzenberg, N. Baruch, D. Deckmyn, Hans Tornai István (1954-) (belgyógyász, gasztroenterológus)
Internet cím:elektronikus változat
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