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1.

001-es BibID:BIBFORM035551
Első szerző:Bacsó Zsolt (biofizikus)
Cím:Quantitative methods for examining the drug resistance phenotype of micrometastatic cancer cells in bone marrow : expression of resistance related proteins / Zs. Bacsó, S. J. Land, J. Klein, J. C. States, R. B. Everson, J. F. Eliason
Dátum:1999
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
külföldön készült közlemény
Megjelenés:Proceedings of the American Association for Cancer Research. - 40 (1999), p. 675. -
További szerzők:Land, S. J. Klein, J. States, J. C. Everson, Richard B. Eliason, James F.
Borító:

2.

001-es BibID:BIBFORM004656
035-os BibID:WOS:000088961100053
Első szerző:Bacsó Zsolt (biofizikus)
Cím:The DNA of annexin V-binding apoptotic cells is highly fragmented / Bacso, Z., Everson, R. B., Eliason, J. F.
Dátum:2000
Megjegyzések:Jurkat leukemia cells induced to undergo apoptosis by treatment with an antibody against the Fas receptor have two annexin V (AV)-binding subpopulations: (a) single-positive cells that bind AV but not propidium iodide (PI); and (b) double-positive cells that bind AV and PI. The single-positive population is thought to represent an early stage of apoptosis. We have examined the relationship between AV binding and a classical characteristic of apoptosis, DNA fragmentation. Time course studies with Jurkat cells treated for 1, 2, or 4 h with anti-Fas indicated that the proportion of AV-binding cells was increased after 2 h. A significant increase in DNA fragmentation was observed only at 4 h as measured by the mean tail moment determined with the alkaline single cell gel electrophoresis (comet) assay. This correlation suggests a temporal relationship between the two parameters, but does not provide direct evidence of what happens in individual cells. We developed a method to measure fluorescent markers of cellular structure or function with a laser scanning cytometer and then perform the comet assay on the same cells. Cells in each AV-binding subpopulation were re-examined before and after electrophoresis. Most AV-/PI- cells had no DNA damage, although a few cells showed a pattern of damage characteristic for apoptosis. Double-positive cells all had damaged DNA; approximately half had the apoptotic pattern, and the rest had a pattern typical for necrosis. Nearly all of the single-positive cells had damaged DNA with the apoptotic pattern. Both AV-positive populations contained cells with little or no detectable DNA after electrophoresis, indicating that the DNA was highly fragmented. These results indicate that AV binding is an excellent marker for apoptotic cells, but that these cells already have fragmented DNA.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Annexin V
Antibodies
Antibodies, Monoclonal
Antigens, CD95
Apoptosis
Cell Membrane
Cells
Comet Assay
cytology
Dna
DNA Damage
DNA Fragmentation
DNA, Neoplasm
Dyes
Flow Cytometry
Human
immunology
Jurkat Cells
metabolism
Necrosis
pharmacology
Phosphatidylserines
physiology
Propidium
Support, Non-U.S.Gov't
Tumor Cells, Cultured
külföldön készült közlemény
Megjelenés:Cancer research. - 60 : 16 (2000), p. 4623-4628. -
További szerzők:Everson, Richard B. Eliason, James F.
Internet cím:elektronikus változat
Borító:

3.

001-es BibID:BIBFORM006033
Első szerző:Feuerstein, Burt G.
Cím:alpha-Difluoromethylornithine alters calcium signaling in platelet-derived growth factor-stimulated A172 brain tumor cells in culture / Feuerstein, B. G., Szollosi, J., Basu, H. S., Marton, L. J.
Dátum:1992
Megjegyzések:alpha-Difluoromethylornithine (DFMO), an irreversible inhibitor of the polyamine biosynthetic enzyme ornithine decarboxylase, inhibits the growth of brain tumor cell lines and is undergoing clinical trials as a treatment for brain tumors. Platelet-derived growth factor (PDGF) is thought to regulate the growth and development of precursors of both normal and neoplastic astrocytic cells; calcium signaling is thought to play a role in the transduction of PDGF signals. Using laser fluorescence image cytometry, flow cytometry, and spectrofluorometry, we studied the effect of DFMO on the calcium signals induced by PDGF in A172 human glioblastoma cells. Four days of treatment with 5 mM DFMO substantially shortened PDGF-induced calcium signals. The effect was reversed more than 10 h but less than 24 h after putrescine treatment, even though polyamines were repleted 4 h after putrescine and spermidine were added. DFMO did not substantially affect intracellular calcium release or the timing of the opening and closing of plasma membrane calcium channels. These findings support the notion that calcium signaling may be a target for inhibitors of polyamine metabolism.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Biogenic Polyamines
Brain Neoplasms
Calcium
Calcium Channels
Calcium Signaling
Cell Line
drug effects
Eflornithine
Flow Cytometry
Fluorescence
Glioblastoma
Human
Image Cytometry
Ion Channel Gating
metabolism
pathology
pharmacology
Platelet-Derived Growth Factor
Polyamines
Signal Transduction
Support, Non-U.S.Gov't
Support, U.S.Gov't,P.H.S.
Tumor Cells, Cultured
Megjelenés:Cancer Research. - 52 : 24 (1992), p. 6782-6789. -
További szerzők:Szöllősi János (1953-) (biofizikus) Basu, Hirak S. Marton, Laurence J.
Internet cím:elektronikus változat
Borító:

4.

001-es BibID:BIBFORM004879
Első szerző:Nagy Péter (biofizikus)
Cím:Decreased accessibility and lack of activation of ErbB2 in JIMT-1, a herceptin-resistant, MUC4-expressing breast cancer cell line / Nagy, P., Friedlander, E., Tanner, M., Kapanen, A. I., Carraway, K. L., Isola, J., Jovin, T. M.
Dátum:2005
ISSN:0008-5472
Megjegyzések:Overexpression of erbB2 in breast tumors is associated with poor prognosis and is a target of receptor-oriented cancer therapy. Trastuzumab (Herceptin), a monoclonal antibody against a membrane-proximal epitope in the extracellular region of erbB2, shows a therapeutic effect against a fraction of erbB2-amplified breast tumors. Unfortunately, resistance to Herceptin is common, and its cause is as yet unclear. Here we investigated the properties of erbB2 in a Herceptin-resistant cell line, JIMT-1, established from a breast cancer patient showing erbB2 gene amplification and primary resistance to Herceptin. The expression profile of erbB proteins, Herceptin-induced erbB2 internalization, and down-regulation in JIMT-1 were similar to those in Herceptin-sensitive lines. However, the mean number of Herceptin Mab binding sites in JIMT-1 was 1/5 that of the expressed erbB2 molecules, although 5% to 10% of the cells showed a approximately 10-fold higher Herceptin binding than the main population. Herceptin Fab and Mab 2C4, an antibody binding to an epitope in the ectodomain further removed from the membrane, bound more efficiently to JIMT-1 cells than Herceptin Mab, implying that erbB2 was partly masked. The expression of MUC4, a membrane-associated mucin that according to reports contributes to the masking of membrane proteins, was higher in JIMT-1 than in Herceptin-sensitive lines, and its level was inversely correlated with the Herceptin binding capacity of single cells. Knockdown of MUC4 expression by RNA interference increased the binding of Herceptin. Western blotting showed a low level of proteolytic processing, shedding, and tyrosine phosphorylation of erbB2 in JIMT-1. The latter finding may explain its Herceptin-resistant phenotype characterizing both the low and high Herceptin binding subpopulations. We conclude that masking of erbB2 in JIMT-1 leads to diminished Herceptin binding and isolation of erbB2 from its normal interaction and activation partners.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Antibodies
Antibodies,Monoclonal
Antineoplastic Agents
Binding Sites
biosynthesis
Breast Neoplasms
Cell Line
Cell Line,Tumor
Cells
chemistry
Down-Regulation
Drug Resistance,Neoplasm
drug therapy
Enzyme Activation
enzymology
Epitopes
Gene Amplification
Humans
immunology
Membrane Proteins
metabolism
Metalloproteases
Mucins
pharmacology
Phenotype
Phosphorylation
Proteins
Receptor,erbB-2
Research
Support
therapy
Tyrosine
Megjelenés:Cancer Research. - 65 : 2 (2005), p. 473-482. -
További szerzők:Friedländer Elza (1980-) (biofizikus) Tanner, Minna Kapanen, Anita I. Carraway, Kermit L. Isola, Jorma Jovin, Thomas M.
Internet cím:elektronikus változat
Borító:

5.

001-es BibID:BIBFORM004934
Első szerző:Szöllősi János (biofizikus)
Cím:ERBB-2 (HER2/neu) gene copy number, p185HER-2 overexpression, and intratumor heterogeneity in human breast cancer / Szollosi, J., Balazs, M., Feuerstein, B. G., Benz, C. C., Waldman, F. M.
Dátum:1995
Megjegyzések:Amplification of the ERBB-2 (HER-2/neu) gene is accompanied by overexpression of its cell surface receptor product, p185HER-2. Heterogeneity has been observed for both the gene copy number and the level of overexpression of its protein product. To better understand their relationship, correlation between the level of cellular expression of p185HER-2 and ERBB-2 gene amplification was studied in four human breast cancer cell lines (BT-474, SK-BR-3, MDA-453, and MCF-7) and in a primary human breast tumor sample. The relative expression of p185HER-2 was measured by immunofluorescence by using flow and/or image cytometry while correlated DNA analysis was performed on the same cells by fluorescence in situ hybridization to determine ERBB-2 gene and chromosome 17 copy numbers. Marked heterogeneity was observed in both protein expression and ERBB-2 copy number. Despite this heterogeneity, and in accordance with previous studies, the average levels of p185HER-2 expression correlated well with average ERBB-2 gene copy numbers in the four lines examined (r = 0.99). When the relationship between copy number and protein expression was studied on a cell-by-cell basis, p185HER-2 expression correlated with both the absolute number of ERBB-2 gene copies/cell (r = 0.59-0.63) and chromosome 17 copy number (r = 0.45-0.61). It is of interest that there was weak or no correlation between p185HER-2 protein expression and the ERBB-2 copy number:chromosome 17 copy number ratio (r = 0.0-0.25). In more than one-half of cells expressing a high level of p185HER-2, the chromosome 17 copy number was high (two or three times the average copy number), whereas < 2% of an unselected population had a high chromosome 17 copy number. Bromodeoxyuridine incorporation indicated that the S-phase-labeling index was homogeneous across various p185HER-2-expressing subpopulations in the SK-BR-3 cell line. Analysis of the primary breast tumor sample showed results similar to the cell lines, supporting the strong possibility of a mechanistic link among p185HER-2 overexpression, ERBB-2 amplification, and high chromosome 17 copy number.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
biosynthesis
Breast Neoplasms
Cell Line
Chromosomes,Human,Pair 17
Dna
Female
Fluorescence
Gene Amplification
Gene Dosage
Genes,erbB-2
genetics
Human
Hybridization
Image Cytometry
Receptor,erbB-2
Support,Non-U.S.Gov't
Support,U.S.Gov't,P.H.S.
Tumor Cells,Cultured
Megjelenés:Cancer Research. - 55 : 22 (1995), p. 5400-5407. -
További szerzők:Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Feuerstein, Burt G. Benz, Christopher C. Waldman, Frederick
Internet cím:elektronikus változat
Borító:

6.

001-es BibID:BIBFORM087079
035-os BibID:(WoS)000567785500005 (Scopus)85100381509
Első szerző:Volpin, Valentina
Cím:CAMK1D Triggers Immune Resistance of Human Tumor Cells Refractory to Anti-PD-L1 Treatment / Valentina Volpin, Tillmann Michels, Antonio Sorrentino, Ayse Nur Menevse, Gertrud Knoll, Madlen Ditz, Vladimir Milija Milenkovic, Chih-Yeh Chen, Anchana Rathinasamy, Klaus Griewank, Michael Boutros, Sebastian Haferkamp, Mark Berneburg, Christian H. Wetzel, Anja Seckinger, Dirk Hose, Hartmut Goldschmidt, Martin Ehrenschwender, Mathias Witzens-Harig, Arpad Szoor, Gyorgy Vereb, Nisit Khandelwal, Philipp Beckhove
Dátum:2020
ISSN:2326-6066 2326-6074
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Cancer Immunology Research. - 8 (2020), p. 1163-1179. -
További szerzők:Michels, Tillmann Sorrentino, Antonio Menevse, Ayse Nur Knoll, Gertrud Ditz, Madlen Milenkovic, Vladimir Milija Chen, Chih-Yeh Rathinasamy, Anchana Griewank, Klaus Boutros, Michael Haferkamp, Sebastian Berneburg, Mark Wetzel, Christian H. Seckinger, Anja Hose, Dirk Goldschmidt, Hartmut Ehrenschwender, Martin Witzens-Harig, Mathias Szöőr Árpád (1984-) (orvos) Vereb György (1965-) (biofizikus, orvos) Khandelwal, Nisit Beckhove, Philipp
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

7.

001-es BibID:BIBFORM044944
Első szerző:Wiedmann, Romina M.
Cím:The V-ATPase-inhibitor archazolid abrogates tumor metastasis via inhibition of endocytic activation of the Rho-GTPase Rac1 / Romina M. Wiedmann, Karin von Schwarzenberg, Andrea Palamidessi, Laura Schreiner, Rebekka Kubisch, Johanna Liebl, Christina Schempp, Dirk Trauner, Gyorgy Vereb, Stefan Zahler, Ernst Wagner, Rolf Müller, Giorgio Scita, Angelika M. Vollmar
Dátum:2012
Megjegyzések:The abundance of the multimeric vacuolar ATP-dependent proton pump, V-ATPase, on the plasma membrane of tumor cells correlates with the invasiveness of the tumor cell, suggesting the involvement of V-ATPase in tumor metastasis. V-ATPase is hypothesized to create a proton efflux leading to an acidic pericellular microenvironment that promotes the activity of proinvasive proteases. An alternative, not yet explored possibility is that V-ATPase regulates the signaling machinery responsible for tumor cell migration. Here, we show that pharmacologic or genetic reduction of V-ATPase activity significantly reduces migration of invasive tumor cells in vitro. Importantly, the V-ATPase inhibitor archazolid abrogates tumor dissemination in a syngeneic mouse 4T1 breast tumor metastasis model. Pretreatment of cancer cells with archazolid impairs directional motility by preventing spatially restricted, leading edge localization of epidermal growth factor receptor (EGFR) as well as of phosphorylated Akt. Archazolid treatment or silencing of V-ATPase inhibited Rac1 activation, as well as Rac1-dependent dorsal and peripheral ruffles by inhibiting Rab5-mediated endocytotic/exocytotic trafficking of Rac1. The results indicate that archazolid effectively decreases metastatic dissemination of breast tumors by impairing the trafficking and spatially restricted activation of EGFR and Rho-GTPase Rac1, which are pivotal for directed movement of cells. Thus, our data reveals a novel mechanism underlying the role of V-ATPase in tumor dissemination
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
ACTIVATION
article
Cells
EGFR
Epidermal Growth Factor
EPIDERMAL-GROWTH-FACTOR
GROWTH
In Vitro
Metastasis
mouse
Movement
Research
Research Support
Support
TUMORS
Megjelenés:Cancer Research. - 72 : 22 (2012), p. 5976-5987. -
További szerzők:Schwarzenberg, Karin von Palamidessi, Andrea Schreiner, Laura Kubisch, Rebekka Liebl, Johanna Schempp, Christina Trauner, Dirk Vereb György (1965-) (biofizikus, orvos) Zahler, Stefan Wagner, Ernst Müller, Rolf Scita, Giorgio Vollmar, Angelika M.
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
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