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001-es BibID:	BIBFORM068923
Első szerző:	Antal-Szalmás Péter (laboratóriumi szakorvos)
Cím:	Spare CD14 molecules on human monocytes enhance the sensitivity for low LPS concentrations / Antal-Szalmás Péter, Poppelier Miriam J. J. G, Sümegi Andrea, van der Bruggen Tjomme, Verhoef Jan, van Kessel Kok P. M., van Strijp Jos A. G
Dátum:	2004
ISSN:	0165-2478
Megjegyzések:	Human monocytes express on their plasma membrane relatively large number of CD14 molecules, known to play a crucial role in thelipopolisaccharide (LPS)-mediated cellular activation. Indirect data (J. Biol. Chem. 270 (1995) 9904) suggest that not all of these CD14molecules participate in LPS-signaling, but the importance of these spare receptors and the exact number of CD14 involved in activation upondifferent LPS-stimuli is not known. Using different concentrations of a blocking anti-CD14 monoclonal antibody (mAb 60bca) we createdmonocytes with graded amounts of CD14. The exact number of occupied and free receptors was quantitated by flow cytometry and specialmAb-labeled standard beads. The number of free CD14 molecules per monocyte in the presence of 10, 3.33, 0.73, 0.25 and 0.041 g/mlmAb was 0, 13 100, 49 300, 97 700 and 165 900. Stimulation of these partially blocked monocytes with 0.1, 1, 10 and 100 ng/ml ReLPS inthe presence of 3% human serum revealed that already 13 100 and 97 700 CD14 molecules provided a maximal Tumor necrosis factor (TNF ) mRNA response using 100 and 10 ng/ml ReLPS, while the activation totally depended on the number of available CD14 moleculesin the case of 1 and 0.1 ng/ml ReLPS. Our data imply that the number of CD14 molecules available for LPS-binding influence the cellularresponse. In the presence of higher concentrations of LPS only fractions of CD14 participate in the cell activation, while the presence of thespare receptors enhance the sensitivity against lower LPS amounts.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban CD14
Megjelenés:	Immunology Letters 93 : 1 (2004), p. 11-15. -
További szerzők:	Poppelier, Miriam J. J. G Sümegi Andrea (1969-) (biológus) van der Bruggen, Tjomme Verhoef, Jan Kessel, Kok P. M., van Strijp, Jos A. G., van
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001-es BibID:	BIBFORM055878
Első szerző:	Antal-Szalmás Péter (laboratóriumi szakorvos)
Cím:	CD14/Fc fusion protein - an artificial antibody / Antal-Szalmás Péter, Vida András, Majoros László, Sümegi Andrea, Bácsi Attila, Vereb György, van Strijp Jos, van Kessel Kok
Dátum:	2012
Tárgyszavak:	Természettudományok Biológiai tudományok idézhető absztrakt
Megjelenés:	Cytometry. Part B, Clinical Cytometry 82 (2012), p. 410. -
További szerzők:	Vida András (1979-) (molekuláris biológus, genetikus) Majoros László (1966-) (szakorvos, klinikai mikrobiológus) Sümegi Andrea (1969-) (biológus) Bácsi Attila (1967-) (immunológus) Vereb György (1965-) (absztraktok, könyvfejezetek) Strijp, Jos A. G., van Kessel, Kok P. M., van
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001-es BibID:	BIBFORM038589
035-os BibID:	PMID:11590623
Első szerző:	Antal-Szalmás Péter (laboratóriumi szakorvos)
Cím:	A novel flow cytometric assay to quantify soluble CD14 concentration in human serum / Péter Antal-Szalmás, Ibolya Szöllősi, Gabriella Lakos, Emese Kiss, István Csípő, Andrea Sümegi, Sándor Sipka, Jos A. G. van Strijp, Kok P. M. van Kessel, Gyula Szegedi
Dátum:	2001
ISSN:	0196-4763
Megjegyzések:	BACKGROUND: CD14, the major lipopolysaccharide (LPS)-binding protein of myeloid cells, is found as a soluble molecule in human serum. Recent data describe the presence of elevated soluble CD14 (sCD14) concentration in various disorders, confirming disease activity. A novel, easy, and rapid flow cytometric assay was developed to measure sCD14 levels in serum. METHODS: The assay is based on the competition between membrane-expressed CD14 of isolated monocytes from healthy volunteers and sCD14 in the sample sera for binding to anti-CD14 monoclonal antibodies (mAb; 26ic or 60bca). The amount of cell-associated mAb is determined with a fluorescein isothiocyanate (FITC)-labeled anti-mouse conjugate and flow cytometry. The fluorescence signal is inversely proportional with the amount of serum sCD14. Using dilutions of a standard serum, the concentration of sCD14 in the samples is calculated and compared with results obtained by a commercial sCD14 enzyme-linked immunosorbent assay (ELISA). RESULTS: After optimization, the assay showed log-log linearity of 122.1-984.7 ng/ml sCD14 using mAb 26ic and 29.5-246.2 ng/ml sCD14 using mAb 60bca. It revealed similar results as the ELISA (mAb 26ic: r = 0.88, mAb 60bca: r = 0.92) and provided significantly elevated sCD14 levels in systemic lupus erythematosus patients compared with controls (26ic: 2,213 versus 1,676 ng/ml, P < 0.002; 60bca: 2,625 versus 1,907 ng/ml, P < 0.0002). Receiver operating characteristic curve analysis suggested a reasonable diagnostic efficacy of sCD14 quantification in this autoimmune disease. CONCLUSIONS: The method is easy, rapid, sensitive, and can be used in the follow-up of patients suffering from sepsis or chronic inflammatory disorders.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	Cytometry 45 : 2 (2001), p. 115-123. -
További szerzők:	Szöllősi Ibolya Lakos Gabriella (1963-) (laboratóriumi szakorvos, transzfúziológus, immunológus) Kiss Emese (1960-) (belgyógyász, immunológus) Csípő István (1953-) (vegyész) Sümegi Andrea (1969-) (biológus) Sipka Sándor (1945-) (laboratóriumi szakorvos) Strijp, Jos A. G., van Kessel, Kok P. M., van Szegedi Gyula (1936-2013) (belgyógyász, immunológus)
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001-es BibID:	BIBFORM037557
Első szerző:	Vida András (molekuláris biológus, genetikus)
Cím:	Fusion of the Fc part of human IgG1 to CD14 enhances its binding to gram-negative bacteria and mediates phagocytosis by Fc receptors of neutrophils / András Vida, Bart Bardoel, Fin Milder, László Majoros, Andrea Sümegi, Attila Bácsi, György Vereb, Kok P. M. van Kessel, Jos A. G. van Strijp, Péter Antal-Szalmás
Dátum:	2012
ISSN:	0165-2478
Megjegyzések:	Microbial resistance to antimicrobial drugs is promoting a search for new antimicrobial agents that target highly conservative structures of pathogens. Human CD14 a known pattern recognition receptor (PRR) which recognizes multiple ligands from different microbes might be a worthy candidate. The aim of our work was to create a CD14/Fc dimer protein and evaluate its whole bacteria binding and opsonizing capabilities. Fusion of CD14 with the fragment crystallisable (Fc) part of human IgG1 could not only lead to an artificial opsonin but the dimerization through the Fc part might also increase its affinity to different ligands. Human CD14 and the Fc part of human IgG1 was fused and expressed in HEK293 cells. A histidine tagged CD14 (CD14/His) was also expressed as control. Using flow cytometry we could prove that CD14/Fc bound to whole Gram-negative bacteria, especially to short lipopolysaccharide (Ra and Re) mutants, and weak interaction was observed between the fusion protein and Listeria monocytogenes. Other Gram-positive bacteria and fungi did not show any association with CD14/Fc. CD14/His showed about 50-times less potent binding to Gram-negative bacteria. CD14/Fc acted as an opsonin and enhanced phagocytosis of these bacteria by neutrophil granulocytes, monocyte-derived macrophages and dendritic cells. Internalization of bacteria was confirmed by trypan blue quenching and confocal microscopy. On neutrophils the Fc part of the fusion protein was recognized by Fc receptors (CD16, CD32), as determined by blocking experiments. CD14/Fc enhanced the killing of bacteria in an ex vivo whole blood assay. Our experiments confirm that PRR/Fc fusion proteins can give a boost to FcR dependent phagocytosis and killing provided the antimicrobial part binds efficiently to microbes.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban CD14 Fc Gram-negative bacteria Opsonization Phagocytosis Molekuláris Medicina
Megjelenés:	Immunology Letters. - 146 : 1-2 (2012), p. 31-39. -
További szerzők:	Bardoel, Bart Milder, Fin Majoros László (1966-) (szakorvos, klinikai mikrobiológus) Sümegi Andrea (1969-) (biológus) Bácsi Attila (1967-) (immunológus) Vereb György (1965-) (biofizikus, orvos) Kessel, Kok P. M., van Strijp, Jos A. G., van Antal-Szalmás Péter (1968-) (laboratóriumi szakorvos)
Pályázati támogatás:	T046694 OTKA TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Celluláris hematológia - immunológia TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Az oxidatív DNS károsodások javítása és a gyulladás kialakulásának kapcsolata
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