Találati lista | Tudóstér

001-es BibID:	BIBFORM043575
Első szerző:	Dardik, Rima
Cím:	Factor XIII mediates adhesion of platelets to endothelial cells through alpha(v)beta(3) and glycoprotein IIb/IIIa integrins / Dardik, R., Shenkman, B., Tamarin, I., Eskaraev, R., Harsfalvi, J., Varon, D., Inbal, A.
Dátum:	2002
ISSN:	0049-3848
Megjegyzések:	Coagulation factor XIII (FXIII) is a transglutaminase that catalyzes crosslink formation in fibrin clots. Endothelial cells (EC) were demonstrated to bind FXIII via their alpha(v)beta3 integrin receptor. FXIII was also shown to bind platelet glycoprotein IIb/IIIa receptor. In the present study, we analyzed if FXIII can mediate platelet-EC interaction. Both FXIII and activated FXIII (FXIIIa) bound to EC monolayers; this binding was enhanced by the addition of Mn2+ and was inhibited by the monoclonal antibody L609 against alpha(v)beta3 integrin. Normal washed platelets also bound surface-immobilized or soluble FXIII and FXIIIa, and the binding was GPIIb/IIIa dependent. The effect of FXIII concentrate (Fibrogammin-P) treatment on the interaction of ECs with platelets from six FXIII-deficient patients was studied. Patients' platelets were radiolabeled with 3H-Adenine, washed, resuspended in autologous plasma and allowed to adhere to immortalized EC line EAhy926. Adhesion of platelets from FXIII-deficient patients to ECs increased 1.7+/-0.4-fold (P=.01) following intravenous infusion of FXIII concentrate. Similarly, addition of 1 U/ml of FXIII concentrate to the patients' PRP in vitro increased the adhesion 1.8+/-0.5-fold (P=.008). Preincubation of the EC monolayers with increasing concentrations of either FXIII or FXIIIa augmented the adhesion of normal washed platelets to ECs in a dose-dependent manner. At 10 U/ml of EC-bound FXIII or FXIIIa, platelet adhesion enhanced 1.7+/-0.25-fold (P=.03) and 2.5+/-0.5-fold (P=.02), respectively. The increase in platelet adhesion was completely abolished by pretreatment of ECs with the anti-alpha(v)beta3 antibody L609 or by preincubation of the platelets with the GPIIb/IIIa inhibitor Abciximab. Taken together, our data indicate that FXIII mediates the interaction of platelets with ECs by bridging between endothelial alpha(v)beta3 and platelet GPIIb/IIIa integrins. This interaction may be relevant for tissue remodeling and wound repair after vascular injury in FXIII-deficient patients.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban FXIII Endothelial cells Platelets GPIIb/IIIa alpha(v)beta(3)
Megjelenés:	Thrombosis Research. - 105 : 4 (2002), p. 317-323. -
További szerzők:	Shenkman, Boris Tamarin, I. Eskaraev, R. Hársfalvi Jolán (1949-) (klinikai biokémikus) Varon, D. Inbal, Aida
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

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)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon: