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001-es BibID:	BIBFORM037102
Első szerző:	Kappelmayer János (laboratóriumi szakorvos)
Cím:	The emerging value of P-selectin as a disease marker / Kappelmayer János, Nagy Béla, Miszti-Blasius Kornél, Hevessy Zsuzsa, Setiadi Hendra
Dátum:	2004
ISSN:	1434-6621
Megjegyzések:	Activated platelets are key components in many arterialdisorders. P-selectin is an activation-dependentplatelet receptor, which is also identified in endothelialcells. Together with E- and L-selectin it constitutesthe selectin family. These transmembrane proteinshave continued to attract great interest as they supportrapid and reversible cell adhesion in flow systemsand thus play an essential role in multicellularinteractions during thrombosis and inflammation.Similarly to other lectins, selectins bind to differentglycoconjugates with varying affinities. Proteinligands, equipped with the appropriate carbohydrateand sulfate moieties for P-selectin binding, have beenidentified in normal peripheral blood leukocytes andseveral non-hematopoietic organs, as well as on cancercells. For diagnostic purposes, P-selectin can readilybe detected on the platelet surface by flowcytometry and by ELISA as a soluble ligand in theplasma. Along with other markers, these data can beused in the assessment of platelet activation status.Such results bear clinical significance since P-selectinhas been implicated in the pathogenesis of widespreaddisorders including coronary artery disease,stroke, diabetes and malignancy.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban microparticle platelet P-selectin P-selectin glycoprotein ligand-1 (PSGL-1) vascular disorders
Megjelenés:	Clinical Chemistry and Laboratory Medicine. - 42 : 5 (2004), p. 475-486. -
További szerzők:	Nagy Béla Jr. (1980-) (labordiagnosztikai szakorvos) Miszti-Blasius Kornél (1977-) (laboratóriumi szakorvos) Hevessy Zsuzsanna (1966-) (laboratóriumi szakorvos) Setiadi, Hendra
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001-es BibID:	BIBFORM006863
Első szerző:	Miner, Jonathan J.
Cím:	Separable requirements for cytoplasmic domain of PSGL-1 in leukocyte rolling and signaling under flow / Miner, J. J., Xia, L., Yago, T., Kappelmayer, J., Liu, Z., Klopocki, A. G., Shao, B., McDaniel, J. M., Setiadi, H., Schmidtke, D. W., McEver, R. P.
Dátum:	2008
Megjegyzések:	In inflamed venules, leukocytes use P-selectin glycoprotein ligand-1 (PSGL-1) to roll on P-selectin and E-selectin and to activate integrin alphaLbeta2 (lymphocyte function-associated antigen-1, LFA-1) to slow rolling on intercellular adhesion molecule-1 (ICAM-1). Studies in cell lines have suggested that PSGL-1 requires its cytoplasmic domain to localize in membrane domains, to support rolling on P-selectin, and to signal through spleen tyrosine kinase (Syk). We generated "DeltaCD" mice that express PSGL-1 without the cytoplasmic domain. Unexpectedly, neutrophils from these mice localized PSGL-1 normally in microvilli, uropods, and lipid rafts. DeltaCD neutrophils expressed less PSGL-1 on their surfaces because of inefficient export from the endoplasmic reticulum. Limited digestion of wild-type neutrophils with O-sialoglycoprotein endopeptidase was used to reduce the PSGL-1 density to that on DeltaCD neutrophils. At matched PSGL-1 densities, both DeltaCD and wild-type neutrophils rolled similarly on P-selectin. However, DeltaCD neutrophils rolling on P-selectin did not trigger Syk-dependent activation of LFA-1 to slow rolling on ICAM-1. These data demonstrate that the PSGL-1 cytoplasmic domain is dispensable for leukocyte rolling on P-selectin but is essential to activate beta2 integrins to slow rolling on ICAM-1.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Animals Antigens, CD18 Hemorheology Intercellular Adhesion Molecule-1 Intracellular Signaling Peptides and Proteins Leukocyte Rolling Membrane Glycoproteins Membrane Microdomains Mice Mice, Knockout Mice, Transgenic Microvilli Models, Biological Models, Molecular Molecular Sequence Data P-Selectin Peptide Fragments Protein Structure, Tertiary Protein-Tyrosine Kinases Recombinant Proteins Signal Transduction Amino Acid Sequence
Megjelenés:	Blood. - 112 : 5 (2008), p. 2035-2045. -
További szerzők:	Xia, Lijun Yago, Tadayuki Kappelmayer János (1960-) (laboratóriumi szakorvos) Liu, Zhenghui Klopocki, Arkadiusz G. Shao, Bojing McDaniel, J. Michael Setiadi, Hendra Schmidtke, David W. McEver, Rodger P.
Internet cím:	elektronikus változat elektronikus változat DOI
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001-es BibID:	BIBFORM012332
Első szerző:	Simon Zsuzsa
Cím:	Protein phosphatase inhibitor calyculin-A modulates activation markers in TRAP-stimulated human platelets / Simon Zs., Kiss A., Erdődi F., Setiadi H., Beke Debreceni I., Nagy B., Kappelmayer J.
Dátum:	2010
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban calyculin-A Ser/Thr specific protein phosphatase P-selectin microparticles
Megjelenés:	Platelets. - 21 : 7 (2010), p. 555-562. -
További szerzők:	Kiss Andrea (1979-) (biokémikus, vegyész) Erdődi Ferenc (1953-) (biokémikus) Setiadi, Hendra Bekéné Debreceni Ildikó (1970-) (biológus) Nagy Béla Jr. (1980-) (labordiagnosztikai szakorvos) Kappelmayer János (1960-) (laboratóriumi szakorvos)
Pályázati támogatás:	T75199 OTKA
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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