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1.

001-es BibID:BIBFORM005181
035-os BibID:(scopus)40149107884 (wos)000255092200005
Első szerző:Friedländer Elza (biofizikus)
Cím:ErbB-directed immunotherapy : antibodies in current practice and promising new agents / Elza Friedländer, Márk Barok, János Szöllősi, György Vereb
Dátum:2008
Megjegyzések:The ErbB family is well known for its significance in oncogenesis. As bad prognostic markers, overexpressed or mutated ErbB1 and ErbB2 have an important role in the molecular diagnosis of various cancers, but as membrane proteins, expressed often selectively in tumor tissues, they can be targeted with kinase inhibitors or therapeutic antibodies. In addition to trastuzumab, the first humanized antibody that was approved for the therapy of solid tumors by the FDA, now many humanized antibodies are in late clinical trials, or already approved. Conjugation of antibodies with radioactive isotopes, cytotoxic agents or liposomes loaded with chemotherapeutic drugs led to improved therapeutic efficiency over their parent "unarmed" antibodies. Novel, engineered antibody derivates with better pharmacodynamic properties are also available and allow the targeting of ErbB1 or ErbB2 positive cancers in a wider patient population. In this review, we discuss the biological and clinical background of ErbB targeting, and describe the most successful antibodies against ErbB1 (cetuximab, panitumumab, matuzumab, nimotuzumab, ICR62, mAb 528, ch806 and MDX-447) and ErbB2 (trastuzumab, pertuzumab, MDX-H210, 2B1, C6.5xscFv(NM3E2), ertumaxomab and FRP-5 derivates) that are in clinical trials or already approved, along with the various relevant conjugation and engineering strategies. Recent data pertinent to the prevalent problem of clinical resistance to treatment with trastuzumab are also discussed.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
agonists
analysis
Animal
Antibodies
Antibody conjugation
Antibody targeted delivery
Apoptosis
Biophysics
Brain
Carcinoma
Cell Line
Cell Proliferation
Cell Survival
Cells
Clinical trial
Cysteine
diagnosis
Dimerization
Down-Regulation
Drug Resistance
EGFR
Endocytosis
Engineered antibody
Epidermal Growth Factor
Epitopes
ErbB1
ErbB2
Fibroblasts
Glioblastoma
Glioma
Human
Humanized antibody
Hungary
In Vitro
Insulin
Membrane Proteins
Mice
Microscopy
Microspheres
Mutation
Necrosis
Paclitaxel
Phenotype
Phosphorylation
Prevalence
Progesterone
Proteins
radiotherapy
Research
Signal Transduction
therapy
toxicity
Trastuzumab resistance
Tumor Necrosis Factor
Tumor therapy/cancer therapy
Tyrosine
Up-Regulation
Megjelenés:Immunology Letters. - 116 : 2 (2008), p. 126-140. -
További szerzők:Barok Márk (1976-) (biofizikus) Szöllősi János (1953-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
Internet cím:elektronikus változat
DOI
elektronikus változat
Borító:

2.

001-es BibID:BIBFORM015628
Első szerző:Szöőr Árpád (orvos)
Cím:Rafts and the battleships of defense : the multifaceted microdomains for positive and negative signals in immune cells / Szoor, A., Szollosi, J., Vereb, G.
Dátum:2010
Megjegyzések:Recognition of the heterogeneity of the cell membrane was one of the most important scientific achievements in the last decades. Since coining the term "lipid rafts", continuous development of advanced microscopic and spectroscopic techniques has vastly expanded our view on these cell membrane microdomains that appear to have almost as many faces as researchers that look at them; they are variable in stability, size and composition that can change in a highly dynamic manner both by recruiting and expelling components as well as by coalescing and breaking up into smaller units. They have, however, one common feature: all eukaryotic cells present some variation of lipid rafts. Cells of the immune system are not exception to this, regardless of their lymphoid or myeloid origin their membranes show a domain structure and these domains serve to condense or reject particular transmembrane, GPI-linked and intracellularly membrane-anchored proteins as function requires. Here we provide a concise overview about the various weapons and shields that immune cells concentrate into their rafts, which have come into sight during the past years. The positive and negative regulatory roles of these microdomains are essential both in the functions of innate immunity and processes concatenated in the adaptive immune response
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
article
Biophysics
Cell Membrane
Cells
Eukaryotic Cells
Hungary
Immune System
lipid raft
Membrane Microdomains
Proteins
Research
Research Support
Support
OTKA::1
MAB::3.1
Megjelenés:Immunology Letters. - 130 : 1-2 (2010), p. 2-12. -
További szerzők:Szöllősi János (1953-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

3.

001-es BibID:BIBFORM008379
Első szerző:Tóth Beáta
Cím:Over-expression of integrin β3 can partially overcome the defect of integrin β3 signaling in transglutaminase 2 null macrophages / Tóth, B., Sarang, Zs., Vereb, Gy., Zhang, A., Tanaka, S., Melino, G., Fésüs, L., Szondy, Zs.
Dátum:2009
ISSN:0165-2478
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Immunology Letters. - 126 : 1-2 (2009), p. 22-28. -
További szerzők:Sarang Zsolt (1976-) (mikrobiológus) Vereb György (1965-) (biofizikus, orvos) Zhang, Ailiang Tanaka, Sakae Melino, Gerry Fésüs László (1947-) (orvos biokémikus) Szondy Zsuzsanna (1959-) (molekuláris sejtbiológus, biokémikus)
Internet cím:elektronikus változat
DOI
Borító:

4.

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

5.

001-es BibID:BIBFORM005110
035-os BibID:(scopus)33644694046 (wos)000236477900020
Első szerző:Zsebik Barbara (biofizikus)
Cím:Hsp90 inhibitor 17-AAG reduces ErbB2 levels and inhibits proliferation of the trastuzumab resistant breast tumor cell line JIMT-1 / Zsebik, B., Citri, A., Isola, J., Yarden, Y., Szollosi, J., Vereb, G.
Dátum:2006
ISSN:165-2478 (Print)
Megjegyzések:ErbB2, a member of the EGF receptor family of tyrosine kinases is overexpressed on many tumor cells of epithelial origin and is the molecular target of trastuzumab (Herceptin), the first humanized antibody used in the therapy of solid tumors. Trastuzumab, which is thought to act, at least in part, by downregulating ErbB2 expression is only effective in approximately 30-40% of ErbB2 positive breast tumors. Geldanamycin and its derivative 17-AAG are potential antitumor agents capable of downregulating client proteins of Hsp90, including ErbB2. To investigate the ability of 17-AAG to downregulate ErbB2 in trastuzumab resistant breast cancer cells and the possibility of 17-AAG and trastuzumab potentiating each other's effect, the recently established trastuzumab resistant breast cancer cell line, JIMT-1 was compared to the known trastuzumab sensitive SKBR-3 line. Baseline and stimulus-evoked dimerization and activation levels of ErbB2, and the effects of trastuzumab and 17-AAG alone and in combination on cell proliferation and apoptosis, as well as on ErbB2 expression and phosphorylation have been measured. Baseline activation and amenability to activation and downregulation by trastuzumab was much lower in the resistant line. However, 17-AAG enhanced ErbB2 homodimerization after 5-10 min of treatment in both cell lines, and decreased proliferation with an IC50 of 70 nM for SKBR-3 and 10nM for JIMT-1. Thus, 17-AAG may be a useful drug in trastuzumab resistant ErbB2 overexpressing tumors. The antiproliferative effect of 17-AAG was positively correlated with phosphorylation and downregulation of ErbB2 and was dominated by apoptosis, although, especially at higher doses, necrosis was also present. Interestingly, IC50 values for ErbB2 downregulation and phosphorylation, in the 30-40 nM range, were not significantly different for the two cell lines. This observation and the negative correlation between resting ErbB2 levels and the antiproliferative effect of 17-AAG may indicate that activation of ErbB2 to some extent could counteract the overall cytostatic effect, especially at higher levels of ErbB2 expression. The usual therapeutic dose of trastuzumab did not change the IC50 of 17-AAG on the proliferation of either cell line, but nevertheless decreased overall ErbB2 phosphorylation and at low doses of 17-AAG further decreased cell growth in the sensitive SKBR-3, thus trastuzumab may be a good combination partner to counteract undesired activating effects of 17-AAG.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
analogs and derivatives
antagonists and inhibitors
Antibodies
Antibodies,Monoclonal
Antineoplastic Agents
Apoptosis
Benzoquinones
Biophysics
Breast Neoplasms
Cell Line
Cell Line,Tumor
Cell Proliferation
Cells
Dimerization
drug effects
Drug Resistance,Neoplasm
drug therapy
enzymology
HSP90 Heat-Shock Proteins
Humans
Hungary
Lactams,Macrocyclic
metabolism
Necrosis
pharmacology
Phosphorylation
Protein Kinase Inhibitors
Proteins
Receptor,erbB-2
Research
Rifabutin
Support
therapeutic use
therapy
Megjelenés:Immunology Letters. - 104 : 1-2 (2006), p. 146-155. -
További szerzők:Citri, Ami Isola, Jorma Yarden, Yosef Szöllősi János (1953-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
Internet cím:elektronikus változat
DOI
Borító:
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