CCL

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1.

001-es BibID:BIBFORM046090
Első szerző:Bacsó Zsolt (biofizikus)
Cím:Raft and cytoskeleton associations of an ABC transporter : P-glycoprotein / Zsolt Bacso, Henrietta Nagy, Katalin Goda, László Bene, Ferenc Fenyvesi, János Matkó, Gábor Szabó
Dátum:2004
ISSN:0196-4763
Megjegyzések:A novel flow cytometric assay has been described in an accompanying report (Gombos et al., METHODS: The kinetics of the decrease in immunofluorescence intensity was analyzed after the addition of the raft-preserving Triton X-100 or Nonidet P-40, both of which disrupt the entire membrane. Mild treatments by both detergents leave cells attached to only those proteins that are anchored to the cytoskeleton by rafts or independent of rafts. Agents that affect microfilaments and modulate membrane levels of cholesterol by cyclodextrin were used to distinguish between the raft-mediated and non-raft-related associations of the Pgp. Confocal microscopy and flow cytometric fluorescence energy transfer measurements were used to confirm colocalization of Pgp with raft constituents. RESULTS: The assay was proved to be sensitive enough to resolve differences between the resistance of UIC2-labeled cell-surface Pgps to Triton X-100 versus Nonidet P-40. Approximately 34% of the UIC2 Fab-labeled Pgp molecules were associated with the cytoskeleton through detergent-resistant, cholesterol-sensitive microdomains or directly, whereas approximately 15% were found to be directly linked to the cytoskeleton. Accordingly, confocal microscopy showed that Pgps colocalize with raft markers, mainly in microvilli. Fluorescence resonance energy transfer efficiency data indicating molecular proximity between Pgp and the raft markers CD44, CD59, and G(M1)-gangliosides also suggested that a significant fraction of Pgps resides in raft microdomains. Raft association of Pgp appears to be of functional significance because its modulation markedly affected drug pumping. CONCLUSIONS: By using the flow cytometric detergent resistance assay in kinetic mode, we were able to assess the extent of raft association and actin cytoskeleton anchorage of Pgp expressed at physiologically relevant levels. We demonstrated that a significant fraction of Pgp is raft associated on LS-174-T human colon carcinoma cells and that this localization may influence its transporter function. The kinetic flow cytometric detergent resistance assay presented in this report is considered to be generally applicable for the analysis of molecular interactions of membrane proteins expressed at low levelsújratöltve - BIBFORM004828
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cytometry. - 61 : 2 (2004), p. 105-116. -
További szerzők:Nagy Henrietta Goda Katalin (1969-) (biofizikus) Bene László (1963-) (biofizikus) Fenyvesi Ferenc (1977-) (gyógyszerész, gyógyszertechnológus) Matkó János (1952-) (biológus) Szabó Gábor (1953-) (biofizikus)
Pályázati támogatás:T032563
OTKA
034393
OTKA
T046945
OTKA
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2.

001-es BibID:BIBFORM063788
035-os BibID:(Cikkazonosító)24810 (WOS)000374905300001 (Scopus)84964597348
Első szerző:Bársony Orsolya (molekuláris biológus)
Cím:A single active catalytic site is sufficient to promote transport in P-glycoprotein / Orsolya Bársony, Gábor Szalóki, Dóra Türk, Szabolcs Tarapcsák, Zsuzsanna Gutay-Tóth, Zsolt Bacsó, Imre J. Holb, Lóránt Székvölgyi, Gábor Szabó, László Csanády, Gergely Szakács, Katalin Goda
Dátum:2016
ISSN:2045-2322
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Scientific Reports. - 6 : 24810 (2016), p. 1-16. -
További szerzők:Szalóki Gábor (1986-) (molekuláris biológus) Türk Dóra Tarapcsák Szabolcs (1989-) (Molekuláris biológus) Gutay-Tóth Zsuzsanna (gyógyszerész) Bacsó Zsolt (1963-) (biofizikus) Holb Imre (1973-) (agrármérnök) Székvölgyi Lóránt (1977-) (biofizikus, biokémikus, sejtbiológus) Szabó Gábor (1953-) (biofizikus) Csanády László Szakács Gergely Goda Katalin (1969-) (biofizikus)
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3.

001-es BibID:BIBFORM004862
035-os BibID:(WOS)000229754600013 (scopus)19944422793
Első szerző:Fenyvesi Ferenc (gyógyszerész, gyógyszertechnológus)
Cím:Conformational and topological states of P-glycoprotein, an ABC transporter involved in multidrug resistance : novel assays of transporter modulation / Fenyvesi, F., Goda, K., Bacso, Z., Vecsernyes, M., Juhasz, I., Marian, T., Tron, L., Krasznai, Z., Szabo, G.
Dátum:2005
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
folyóiratcikk
P-Glycoprotein
egyetemen (Magyarországon) készült közlemény
Megjelenés:European Journal of Pharmaceutical Sciences. - 25 : Suppl. 1 (2005), p. S16. -
További szerzők:Goda Katalin (1969-) (biofizikus) Bacsó Zsolt (1963-) (biofizikus) Vecsernyés Miklós (1959-) (gyógyszertechnológus, endokrinológus) Juhász István (1956-) (bőrgyógyász, bőrsebész, kozmetológus, klinikai onkológus) Márián Teréz (1950-) (radiobiológus) Trón Lajos (1941-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Szabó Gábor (1953-) (biofizikus)
Borító:

4.

001-es BibID:BIBFORM004116
035-os BibID:(WOS)000258489900004 (scopus)47249099723
Első szerző:Fenyvesi Ferenc (gyógyszerész, gyógyszertechnológus)
Cím:P-glycoprotein inhibition by membrane cholesterol modulation / Fenyvesi F., Fenyvesi E., Szente L., Goda K., Bacsó Z., Bácskay I., Váradi J., Kiss T., Molnár E., Janáky T., Szabó G. Jr, Vecsernyés M.
Dátum:2008
Megjegyzések:P-glycoprotein (Pgp) is a transmembrane protein that actively exports lipophilic chemotherapeutics from the cells causing multidrug resistance. Pgp molecules are partially localized in TX-100-resistant rafts, and the activity of the transporter is highly sensitive to the presence of cholesterol. To better understand these relationships, the influence of membrane cholesterol content on Pgp function, as measured via calcein accumulation, was studied in correlation with changes elicited in membrane structure. Membrane cholesterol was modulated by heptakis(2,6-di-O-methyl)-béta-cyclodextrin (DIMEB) and the cholesterol inclusion complex of DIMEB (Chol-DIMEB). Changes in membrane cholesterol level were reflected by alterations in the overall lipid packing as measured by Merocyanine 540 (MC540) staining andwere also accompanied by changes in the raft association of the pump. DIMEB and Chol- DIMEB treatments have also lead to increased permeability of the cell membrane in both directions, raising the possibility that the effects on pumping efficiency reflect leakage of ATP also from the non-permeabilized cells. However, the treatments did not influence the intracellular ATP levels of the non-permeabilized cells. Our data suggest that Pgp inhibition by cyclodextrin treatments arises through modulation of its membrane microenvironment, rather than as a result of concomitant cytotoxicity.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
P-glycoprotein
cyclodextrin
egyetemen (Magyarországon) készült közlemény
Megjelenés:European Journal of Pharmaceutical Sciences. - 34 : 4-5 (2008), p. 236-242. -
További szerzők:Fenyvesi Éva Szente Lajos (1951-) (vegyész) Goda Katalin (1969-) (biofizikus) Bacsó Zsolt (1963-) (biofizikus) Bácskay Ildikó (1969-) (gyógyszerész, gyógyszertechnológus) Váradi Judit (1973-) (gyógyszerész, gyógyszertechnológus) Kiss Tímea (1983-) (gyógyszerész) Molnár Éva (1977-) (analitikus) Janáky Tamás Szabó Gábor (1953-) (biofizikus) Vecsernyés Miklós (1959-) (gyógyszertechnológus, endokrinológus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM046298
Első szerző:Goda Katalin (biofizikus)
Cím:Reversal of Multidrug Resistance by Valinomycin is Overcome by CCCP / Goda K., Krasznai Z., Gaspar R., Lankelma J., Westerhoff H. V., Damjanovich S., Szabo G.
Dátum:1996
ISSN:0006-291X
Megjegyzések:Reversal of P-glycoprotein-mediated multidrug resistance by valinomycin is overcome by the proton ionophore, CCCP. This effect, a complete suppression of the 5- to 10-fold valinomycin-induced reversal ("re-reversal"), exhibits a sharp extracellular potassium concentration ([K+(0)]) dependence. It is observed at [K+(0)] > 2-4 mM and not at [K+(0)] greater than or equal to 2 mM, in the case of the fluorescent substrates rhodamine 123 and daunorubicin. The fact that "re-reversal" is detected only for the combination of CCCP with valinomycin raises the possibility that a direct interaction between these ionophores may explain the phenomenon. We show spectroscopic evidence of such an interaction, with a [K+(0)]-dependence similar to that of the "re-reversal." These data suggest that the reversal of P-glycoprotein activity by valinomycin can be compromised by anionic compounds such as CCCP due to complex formation. More generally, molecular interactions involving P-glycoprotein substrates or reversing agents may significantly affect drug accumulation in multidrug resistant cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical And Biophysical Research Communications. - 219 : 2 (1996), p. 306-310. -
További szerzők:Krasznai Zoltán (1950-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Lankelma, Jan Westerhoff, Hans V. Damjanovich Sándor (1936-2017) (biofizikus) Szabó Gábor (1953-) (biofizikus)
Pályázati támogatás:T14655
OTKA
17592
OTKA
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6.

001-es BibID:BIBFORM046295
Első szerző:Goda Katalin (biofizikus)
Cím:Intracellular pH does not affect drug extrusion by P-glycoprotein / Goda Katalin, Balkay László, Márián Teréz, Trón Lajos, Aszalós Adorján, Szabó Gábor
Dátum:1996
ISSN:1011-1344
Megjegyzések:The intracellular pH (pH(i)) of cells exhibiting multidrug resistance (MDR) related to the expression of the P-glycoprotein (Pgp) is often more alkaline than that of the parental cells, as also observed for the KB-V1/KB-3-1 system in this paper. The possible role of an elevated pH(i) in Pgp-related MDR has been investigated by shifting back the pH(i) of the MDR+ cells to a more acidic value using the mobile proton ionophore carbonylcyanide m-chlorophenylhydrazone (CCCP). The influence of CCCP-evoked delta pH(i) on relative daunorubicin (DNR) accumulation was similar in the case of several Pgp positive and negative cell lines, in view of flow cytometric and radioactive drug accumulation studies and measuring DNR levels in the medium in a flow-through system. Our data argue against a significant effect of pH(i) on Pgp pumping efficiency. However, an indirect connection between pH(i) regulation and the MDR phenotype is suggested by the fact that acidification of the external medium in the presence of verpamil could be observed exclusively in MDR+ cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal Of Photochemistry And Photobiology B: Biology. - 34 : 2-3 (1996), p. 177-182. -
További szerzők:Balkay László (1963-) (biofizikus) Márián Teréz (1950-) (radiobiológus) Trón Lajos (1941-) (biofizikus) Aszalos Adorján Szabó Gábor (1953-) (biofizikus)
Pályázati támogatás:T017592
OTKA
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7.

001-es BibID:BIBFORM067229
Első szerző:Goda Katalin (biofizikus)
Cím:Flow cytometric functional assays for the detection of p-glycoprotein and multidrug resistance-associated protein / Goda Katalin, Szakács Gergely, Nagy Henrietta, Szabó Gábor, Sarkadi Balázs
Dátum:1998
ISBN:9639070319
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
flow cytometry
Megjelenés:Practical guide to physical analysis of cell surface receptors / Szerk. Krasznai Zoltán, Mátyus László. - p. 110-126. -
További szerzők:Szakács Gergely Nagy Henrietta Szabó Gábor (1953-) (biofizikus) Sarkadi Balázs
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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8.

001-es BibID:BIBFORM039166
035-os BibID:(scopus)0036272752 (wos)000175906900005
Első szerző:Goda Katalin (biofizikus)
Cím:Effects of ATP depletion and phosphate analogues on P-glycoprotein conformation in live cells / Goda, K., Nagy, H., Mechetner, E., Cianfriglia, M., Szabo, G.
Dátum:2002
ISSN:0014-2956
Megjegyzések:P-glycoprotein (Pgp), a membrane pump often responsible for the multidrug resistance of cancer cells, undergoes conformational changes in the presence of substrates/modulators, or upon ATP depletion, reflected by its enhanced reactivity with the UIC2 monoclonal antibody. When the UIC2-shift was elicited by certain modulators (e.g. cyclosporin A or vinblastine, but not with verapamil or Tween 80), the subsequent binding of other monoclonal anti-Pgp Ig sharing epitopes with UIC2 (e.g. MM12.10) was abolished [Nagy, H., Goda, K., Arceci, R., Cianfriglia, M., Mechetner, E. & Szabó Jr, G. (2001) Eur. J. Biochem.268, 2416?2420]. To further study the relationship between UIC2-shift and the suppression of MM12.10 binding, we compared, on live cells, how ATP depletion and treatment of cells with phosphate analogues (sodium orthovanadate, beryllium fluoride and fluoro-aluminate) that trap nucleotides at the catalytic site, affect the two phenomena. Similarly to modulators or ATP depleting agents, all the phosphate analogues increased daunorubicin accumulation in Pgp-expressing cells. Prelabeling of ATP depleted cells with UIC2 completely abolished the subsequent binding of MM12.10, in accordance with the enhanced binding of the first mAb. Vanadate and beryllium fluoride, but not fluoro-aluminate, reversed the effect of cyclosporin A, preventing UIC2 binding and allowing for labeling of cells with MM12.10. Thus, changes in UIC2 reactivity are accompanied by complementary changes in MM12.10 binding also in response to direct modulation of the ATP-binding site, confirming that conformational changes intrinsic to the catalytic cycle are reflected by both UIC2-related phenomena. These data also fit a model where the UIC2 epitope is available for antibody binding throughout the catalytic cycle including the step of ATP binding, to become unavailable only in the catalytic transition state.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:European Journal Of Biochemistry. - 269 : 11 (2002), p. 2672-2677. -
További szerzők:Nagy Henrietta Mechetner, Eugene Cianfriglia, Maurizio Szabó Gábor (1953-) (biofizikus)
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9.

001-es BibID:BIBFORM024791
Első szerző:Goda Katalin (biofizikus)
Cím:Simultaneous detection of p-glycoprotein substrates, rhodamine 123 and daunorubicin in multidrug resistant cell lines by high-performance liquid chromatography / Goda, K., Nagy, E., Kiss, A., Telek, B., Szabo, G.
Dátum:1998
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
P-Glycoprotein
Rhodamine 123
Daunorubicin
Cell Line
Megjelenés:Advances in Chromatography. - 1 (1998), p. 53-59. -
További szerzők:Nagy E. Kiss A. (orvos) Telek Béla (1948-) (belgyógyász, haematológus) Szabó Gábor (1953-) (biofizikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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10.

001-es BibID:BIBFORM010351
035-os BibID:(WOS)000266994100004 (scopus)65649131520
Első szerző:Goda Katalin (biofizikus)
Cím:Multidrug resistance through the spectacle of P-glycoprotein / Katalin Goda, Zsolt Bacsó, Gábor Szabó
Dátum:2009
ISSN:1568-0096 (Print)
Megjegyzések:P-glycoprotein (Pgp), coded for by the mdr1 gene, is one of the ABC transporters held responsible for the phenomenon of multidrug resistance (mdr), which is reflected by a rapidly escalating failure of chemotherapy with different classes of cytotoxic agents: anthracyclins, vinca alkaloids, taxanes, epipodophylotoxins. Although overcoming resistance conveyed by Pgp alone may not be sufficient for reaching effective treatment, the abundance of observations available for this paradigmatic multidrug transporter at both in vitro and in vivo setting is a tempting ground for an updated assessment of the main currents of mdr research. In this review we attempt to help keep track of the features of Pgp-mediated drug transport that serve as the major starting points for ongoing efforts of mdr reversal. We will analyze the slowly narrowing gaps that prevail between our ever increasing understanding at the protein, cell and organism level, focusing on the molecular interactions involving Pgp.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Algorithms
Alkaloids
Amino Acids
analysis
anthracycline
Antibodies
antineoplastic activity
Antineoplastic Agents
Apoptosis
Ascites
beta cyclodextrin derivative
beta methylcyclodextrin
binding affinity
binding site
Biological Transport
Biophysics
blood
Brain
cancer chemotherapy
cancer resistance
Capillaries
Caveolae
Cell Membrane
Cells
ceramide
chemistry
Cho Cells
Cholesterol
Cloning,Molecular
colchicine
concentration response
cyclodextrin derivative
cyclosporin A
Daunorubicin
Dexamethasone
Dna
doxorubicin
drug binding
drug distribution
drug effect
Drug Interactions
drug potentiation
Drug Resistance
Drug Resistance,Multiple
drug transport
drug treatment failure
drug uptake
Enzymes
Epitopes
Fluorescence
Fluorescence correlation spectroscopy
Genes,MDR
glycoprotein P
histone deacetylase inhibitor
Hiv
Hiv-1
Homeostasis
Human
human cell
Humans
Hungary
Hydrolysis
Hydrophobicity
hydroxymethylglutaryl coenzyme A reductase inhibitor
In Vitro
Ivermectin
Kinetics
Light
lipid composition
lipid raft
Lipids
Membrane Microdomains
membrane permeability
Membrane Proteins
metabolism
methods
Mice
Microscopy
Models,Genetic
Molecular Biology
molecular interaction
monoclonal antibody
monoclonal antibody uic2
mouse
Multidrug resistance
Mutation
Neoplasms
nicardipine
nonhuman
Ovary
P-Glycoprotein
Paclitaxel
Peptides
Permeability
pharmacokinetics
pharmacology
Phospholipids
physiology
Proteins
Research
review
Rhodamine 123
Signal Transduction
Sphingosine
sphingosine 1 phosphate
Substrate Specificity
tariquidar
taxane derivative
Temperature
therapy
toxicity
trends
unclassified drug
Valinomycin
valspodar
Verapamil
Vinblastine
Vinca alkaloid
vincristine
Water
Xenopus
Megjelenés:Current Cancer Drug Targets. - 9 : 3 (2009), p. 281-297. -
További szerzők:Bacsó Zsolt (1963-) (biofizikus) Szabó Gábor (1953-) (biofizikus)
Internet cím:elektronikus változat
Intézményi repozitóriumban (DEA) tárolt változat
DOI
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11.

001-es BibID:BIBFORM004664
035-os BibID:(scopus)0033670124 (wos)000165543500002
Első szerző:Goda Katalin (biofizikus)
Cím:Conformational heterogeneity of P-glycoprotein / Goda, K., Nagy, H., Bene, L., Balazs, M., Arceci, R., Mechetner, E., Szabo, G.
Dátum:2000
Megjegyzések:P-glycoprotein (P-gp) acts as an active efflux mechanism for a large number of cytostatics and seems to be involved in the frequent failure of cancer chemotherapy. The molecular events of substrate recognition and transport still are not understood completely. We show here that the percentage of P-gp epitopes available for labeling with UIC2 monoclonal antibody is increased significantly after methanol permeabilization/fixation of cells. At the same time, binding of the MRK16 and 4E3 anti-P-gp antibodies is changed only moderately. Confocal microscopical images of UIC2-PE-labeled cells show that the epitopes becoming available after fixation are situated mainly in the plasma membrane. Thus, only a minority of P-gp molecules are accessible for UIC2 in the cell membrane of live cells, and methanol treatment can expose a large pool of previously plasma membrane-embedded, cryptic UIC2 epitopes. The UIC2-reactive P-gp molecules do not appear to be sequestered spatially, as suggested by the high fluorescence resonance energy transfer efficiency measured between the fluorescently labeled competing UIC2 and MRK16 antibodies, suggestive of P-gp dimerization and oligomerization on live cells
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
3T3 Cells
Animal
Antibodies
Antibodies,Monoclonal
Biophysics
Cell Membrane
Cell Membrane Permeability
Cells
chemistry
Dimerization
drug effects
Energy Transfer
Epitopes
Fixatives
Flow Cytometry
Fluorescence
Human
Hungary
immunology
KB Cells
metabolism
Methanol
Mice
Microscopy,Confocal
P-Glycoprotein
pharmacology
Protein Conformation
Support,Non-U.S.Gov't
Megjelenés:Cancer Detection and Prevention. - 24 : 5 (2000), p. 415-421. -
További szerzők:Nagy H. Bene László (1963-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Arceci, Robert Mechetner, Eugene Szabó Gábor (1953-) (biofizikus)
Borító:

12.

001-es BibID:BIBFORM046091
Első szerző:Gombos Imre
Cím:Cholesterol sensitivity of detergent resistance : a rapid flow cytometric test for detecting constitutive or induced raft association of membrane proteins / Imre Gombos, Zsolt Bacsó, Cynthia Detre, Henrietta Nagy, Katalin Goda, Márton Andrásfalvy, Gábor Szabó, János Matkó
Dátum:2004
ISSN:0196-4763
Megjegyzések:Lipid rafts are cholesterol- and glycosphingolipid-rich microdomains in the cellular plasma membranes that play critical roles in compartmentalization (concentration, coupling, and isolation) of receptors and signal molecules. Therefore, detecting constitutive or induced raft associations of such proteins is of central interest in cell biology. This has mostly been done with time- and cell-consuming immunobiochemical techniques affected by several sources of artifacts. A flow cytometric analysis of immunocytochemical staining under differential circumstances of detergent treatment offers a new alternative to this method. METHODS: Membrane microdomains are resistant to nonionic detergents due to extensive, strong interactions between their molecular constituents. We used this feature to develop a rapid flow cytometric assay of differential detergent resistance based on immunocytochemical labeling of extracellular domain epitopes in membrane proteins. Data evaluation is based on comparative detection of their detergent solubility without and with cholesterol depletion of cell membranes, resolved by moderate concentrations of nonionic detergents. RESULTS: Nonionic detergents Triton X-100 and Nonidet-40 (0.05-0.1%) in cold or Brij-98 (0.1-0.5%) at 37 degrees C efficiently resolved detergent solubility or resistance of many lymphocyte cell surface proteins. Kinetic data revealed that a short (5-10 min) detergent treatment is sufficient for this assay. Comparison of detergent solubility in untreated and cholesterol-depleted cells differentiated membrane proteins associated with or excluded from raft microdomains, respectively. Confocal microscopy showed that this mild detergent treatment leaves the cytoskeleton of the cells intact, with a detectable expression of raft marker detergent-resistant proteins attached to it. An induced association with rafts of immunoglobulin E receptors upon antigen cross-linking was also easily detectable in rat mast cells by this approach. CONCLUSIONS: A protocol is proposed for a rapid (5-10 min) test of detergent resistance of membrane proteins in cells. The approach requires only a small amount of cells (10(4)/sample) and offers a good resolution of detergent solubility or resistance of membrane proteins, also in terms of the underlying mechanisms, with an advantage of applicability for all conventional bench-top flow cytometers.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cytometry. Part A. - 61A : 2 (2004), p. 117-126. -
További szerzők:Bacsó Zsolt (1963-) (biofizikus) Detre, Cynthia Nagy Henrietta Goda Katalin (1969-) (biofizikus) Andrásfalvy Márton Szabó Gábor (1953-) (biofizikus) Matkó János (1952-) (biológus)
Pályázati támogatás:T034393
OTKA
TS044711
OTKA
T032563
OTKA
T046945
OTKA
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