CCL

Összesen 15 találat.
#/oldal:
Részletezés:
Rendezés:

1.

001-es BibID:BIBFORM040913
Első szerző:Boratkó Anita (biokémikus, molekuláris biológus)
Cím:RACK1 is involved in endothelial barrier regulation via its two novel interacting partners / Boratkó Anita, Gergely Pál, Csortos Csilla
Dátum:2013
ISSN:1478-811X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cell Communication and Signaling. - 11 : 2 (2013), p. 1-14. -
További szerzők:Gergely Pál (1947-) (biokémikus) Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:CNK 80709
OTKA
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

2.

001-es BibID:BIBFORM033624
Első szerző:Boratkó Anita (biokémikus, molekuláris biológus)
Cím:Cell cycle dependent association of EBP50 with protein phosphatise 2A in endothelial cells / Boratkó A., Gergely P., Csortos Cs.
Dátum:2012
ISSN:1932-6203
Megjegyzések:Ezrin-radixin-moesin (ERM)-binding phosphoprotein 50 (EBP50) is a phosphorylatable PDZ domain-containing adaptor protein that is abundantly expressed in epithelium but was not yet studied in the endothelium. We report unusual nuclear localization of EBP50 in bovine pulmonary artery endothelial cells (BPAEC). Immunofluorescent staining and cellular fractionation demonstrated that EBP50 is present in the nuclear and perinuclear region in interphase cells. In the prophase of mitosis EBP50 redistributes to the cytoplasmic region in a phosphorylation dependent manner and during mitosis EBP50 co-localizes with protein phosphatase 2A (PP2A). Furthermore, in vitro wound healing of BPAEC expressing phospho-mimic mutant of EBP50 was accelerated indicating that EBP50 is involved in the regulation of the cell division. Cell cycle dependent specific interactions were detected between EBP50 and the subunits of PP2A (A, C, and Bα) with immunoprecipitation and pull-down experiments. The interaction of EBP50 with the Bα containing form of PP2A suggests that this holoenzyme of PP2A can be responsible for the dephosphorylation of EBP50 in cytokinesis. Moreover, the results underline the significance of EBP50 in cell division via reversible phosphorylation of the protein with cyclin dependent kinase and PP2A in normal cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Molekuláris Medicina
Megjelenés:Plos One. - 7 : 4 (2012), p. e35595. -
További szerzők:Gergely Pál (1947-) (biokémikus) Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
I. Protein foszfatázok szerepe az in vitro porcdifferenciációban és a mechano-transzdukcióban, II. Hypoglykaemiás szerek tervezése a glikogén foszforilázra (foszforilációval és defoszforilációval szabályozott kulcsenzim) ható molekulákkal
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

3.

001-es BibID:BIBFORM047051
035-os BibID:PMID:2157500
Első szerző:Csortos Csilla (biokémikus)
Cím:Phosphorylase phosphatase activities of rat liver in streptozotocin-diabetes / Csilla Csortos, Ilona Farkas, Lloyd Sparks, Tamás Bányász, Tibor Kovács, Pál Gergely
Dátum:1990
ISSN:0167-4889
Megjegyzések:Protein phosphatase-1 and 2A, accounting for all the hepatic activity regulating phosphorylase, were assayed in streptozotocin-induced (8 weeks) diabetic Wistar rats. Cytosolic protein phosphatase-1 and 2A were distinguished by chromatography on heparin-Sepharose and by inhibition with inhibitor-2. Approx. 25-35% increases in type-1 phosphorylase phosphatase activity measured in cytosols were registered in diabetic rats when compared with control and 24 h fasting animals. The enrichment of protein phosphatase-1 in the cytosol of streptozotocin-treated rat livers could not be attributed to the reduced glycogen content with the onset of diabetes, since this elevated level of type-1 phosphatase was not observed in fasting rats with low glycogen content. The translocation of type-1 phosphatase from the particulate fraction into the cytosol was also recorded in trypsin-treated samples of diabetic rat livers. The apparent molecular weight of type-1 phosphatase in the cytosol of control and fasted rats was 160,000 as judged by gel filtration. The type-1 phosphatase activity that was released from the particulate fraction by streptozotocin-induced diabetes identified a further enzyme species (Mr 110,000) in the cytosol. Our data imply that the higher levels of cytosolic protein phosphatase-1 in diabetic rat liver could be a consequence of the dissociation of the catalytic subunit of protein phosphatase-1 and the glycogen-binding subunit in rat livers.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Protein phosphatase
Hepatic metabolism
Diabetes
Fasting
Streptozotocin
Rat liver
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1052 : 1 (1990), p. 235-241. -
További szerzők:Farkas Ilona (1953-) (biokémikus) Sparks, Lloyd Bányász Tamás (1960-) (élettanász) Kovács Tibor (1929-1994) (élettanász) Gergely Pál (1947-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Szerző által megadott URL
Borító:

4.

001-es BibID:BIBFORM029041
Első szerző:Csortos Csilla (biokémikus)
Cím:Interaction of the catalytic subunits of protein phosphatase-1 and 2A with inhibitor-1 and 2 : a fluorescent study with sulfhydryl-specific pyrene maleimide / Csilla Csortos, János Matkó, Ferenc Erdődi, Pál Gergely
Dátum:1990
ISSN:0006-291X
Megjegyzések:The catalytic subunits of protein phosphatase-1 and 2A were covalently modified in their reactive sulfhydryl groups with N-(3-Pyrene) maleimide resulting in fluorescent labeling of the proteins to an extent of 0.85 and 0.9 mole dye/mole enzyme, respectively. The reaction of the sulfhydryl group led to the partial inactivation of both phosphatase-1 and 2A. Inhibitor-1 and inhibitor-2 increased markedly the fluorescence intensity of the dye-phosphatase-1 conjugate implying that the labeled enzyme retained its ability to bind these proteins. In contrast, inhibitor-1 or inhibitor-2 had no influence on the fluorescence of the dye-phosphatase-2A conjugate. No change in either the fluorescence intensity or polarization of labeled phosphatase-1 and 2A was observed in the presence of thiophosphorylase a, suggesting a lack of interaction of these enzyme forms with the substrate after modification of the reactive sulfhydryl group.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochemical and Biophysical Research Communications. - 169 : 2 (1990), p. 559-564. -
További szerzők:Matkó János (1952-) (biológus) Erdődi Ferenc (1953-) (biokémikus) Gergely Pál (1947-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

5.

001-es BibID:BIBFORM016824
Első szerző:Czikora István (vegyész, biokémikus)
Cím:Characterization of the effect of TIMAP phosphorylation on its interaction with protein phosphatase 1 / Czikora István, Kim Kyung-mi, Kása Anita, Bécsi Bálint, Verin Alexander D., Gergely Pál, Erdődi Ferenc, Csortos Csilla
Dátum:2011
ISSN:0300-9084
Megjegyzések:TIMAP, TGF-beta inhibited, membrane-associated protein, is highly abundant in endothelial cells (EC). We have shown earlier the involvement of TIMAP in PKA-mediated ERM (ezrin-radixin-moesin) dephosphorylation as part of EC barrier protection by TIMAP (Csortos et al., 2008). Emerging data demonstrate the regulatory role of TIMAP on protein phosphatase 1 (PP1) activity. We provide here evidence for specific interaction (Ka = 1.80 x 106 M-1) between non-phosphorylated TIMAP and the catalytic subunit of PP1 (PP1c) by surface plasmon resonance based binding studies. Thiophosphorylation of TIMAP by PKA, or sequential thiophosphorylation by PKA and GSK3β slightly modifies the association constant for the interaction of TIMAP with PP1c and decreases the rate of dissociation. However, dephosphorylation of phospho-moesin substrate by PP1cbeta is inhibited to different extent in the presence of non- (not, vert, similar60% inhibition), mono- (not, vert, similar50% inhibition) or double-thiophosphorylated (<10% inhibition) form of TIMAP. Our data suggest that double-thiophosphorylation of TIMAP has minor effect on its binding ability to PP1c, but considerably attenuates its inhibitory effect on the activity of PP1c. PKA activation by forskolin treatment of EC prevented thrombin evoked barrier dysfunction and ERM phosphorylation at the cell membrane (Csortos et al., 2008). With the employment of specific GSK3beta inhibitor it is shown here that PKA activation is followed by GSK3beta activation in bovine pulmonary EC and both of these activations are required for the rescuing effect of forskolin in thrombin treated EC. Our results suggest that the forskolin induced PKA/GSK3beta activation protects the EC barrier via TIMAP-mediated decreasing of the ERM phosphorylation level.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
TIMAP
Protein Phosphatase 1
Moesin
Surface Plasmon Resonance
Molekuláris Medicina
Megjelenés:Biochimie. - 93 : 7 (2011), p. 1139-1145. -
További szerzők:Kim, Kyung-mi Kovács-Kása Anita (1983-) Bécsi Bálint (1981-) (vegyészmérnök) Verin, Alexander Gergely Pál (1947-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus) Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
I. Protein foszfatázok szerepe az in vitro porcdifferenciációban és a mechano-transzdukcióban, II. Hypoglykaemiás szerek tervezése a glikogén foszforilázra (foszforilációval és defoszforilációval szabályozott kulcsenzim) ható molekulákkal
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Biomolekuláris interakciók jellemzőinek kvantitatív meghatározása
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

6.

001-es BibID:BIBFORM029057
Első szerző:Erdődi Ferenc (biokémikus)
Cím:Effects of acidic and basic macromolecules on the activity of protein phosphatase-1 / Ferenc Erdődi, Csilla Csortos, György Bot, Pál Gergely
Dátum:1985
ISSN:0167-4838
Megjegyzések:The dephosphorylation of phosphorylase a by the catalytic subunit of protein phosphatase-1 obtained from rabbit skeletal muscle is inhibited by heparin in a noncompetitive manner with respect to phosphorylase a (Ki = 8 micrograms/ml). The inhibitory effect of heparin is also observed in the presence of effectors (e.g., glucose and AMP) modifying the dephosphorylation of phosphorylase a. Heat-stable protein inhibitors of protein phosphatase-1 can develop their inhibitory effect of the activity of protein phosphatase-1 even in the presence of heparin. The inhibitory effect of heparin and the heat-stable inhibitor-2 of phosphatase is additive. Polybrene, a heparin antagonist, prevented phosphatase-1 from the inhibition caused by heparin or the inhibitors. Proteins with basic character, histone fractions (H1, H3) and protamine sulfate, can counteract with the inhibitory effect of heparin, but they cannot intercept the actions of inhibitor-1 or -2.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Protein phosphatase
Enzyme inhibitor
Polybrene
Rabbit skeletal muscle
Megjelenés:Biochimica et Biophysica Acta (BBA). Protein Structure and Molecular Enzymology. - 827 : 1 (1985), p. 23-29. -
További szerzők:Csortos Csilla (1956-) (biokémikus) Bot György (1917-1998) (biokémikus, vegyész) Gergely Pál (1947-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Szerző által megadott URL
Borító:

7.

001-es BibID:BIBFORM029054
Első szerző:Erdődi Ferenc (biokémikus)
Cím:Separation of rabbit liver latent and spontaneously active phosphorylase phosphatases by chromatography on heparin-sepharose / Ferenc Erdődi, Csilla Csortos, György Bot, Pál Gergely
Dátum:1985
ISSN:0006-291X
Megjegyzések:Latent and spontaneously active forms of phosphorylase phosphatase were separated by heparin-Sepharose chromatography of rabbit liver extract. The latent enzyme had an absolute polycation (histone H1, polybrene) requirement for the activity assayed with phosphorylase a and phosphorylase kinase substrates. Ethanol treatment resulted in the activation of both phosphatases by dissociating of 150-180 kDa holoenzymes to 33-38 kDa catalytic subunits as judged by gel filtration. The latent and spontaneously active phosphatases were differentiated according to their abilities to dephosphorylate the alpha and the beta subunits of phosphorylase kinase and sensitivities to inhibition by inhibitor-2 or heparin, and were classified as type-2A and type-1 phosphatases, respectively.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochemical and Biophysical Research Communications. - 128 : 2 (1985), p. 705-712. -
További szerzők:Csortos Csilla (1956-) (biokémikus) Bot György (1917-1998) (biokémikus, vegyész) Gergely Pál (1947-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

8.

001-es BibID:BIBFORM029040
Első szerző:Erdődi Ferenc (biokémikus)
Cím:Purification and characterization of three distinct types of protein phosphatase catalytic subunits in bovine platelets / Ferenc Erdődi, Csilla Csortos, Lloyd Sparks, Andrea Murányi, Pál Gergely
Dátum:1992
ISSN:0003-9861
Megjegyzések:The catalytic subunits of bovine platelet protein phosphatases were separated into three distinct forms by chromatography on heparin-Sepharose. Each phosphatase was further purified to apparent homogeneity as judged in sodium dodecyl sulfate-polyacrylamide gel yielding single protein bands of 37, 41, and 36 kDa. The 37-kDa phosphatase was excluded from heparin-Sepharose and preferentially dephosphorylated the alpha-subunit of phosphorylase kinase. It was stimulated by polycations (polybrene or histone H1) and was inhibited by okadaic acid (IC50 = 0.3 nM), but its activity was not influenced by inhibitor-2 or heparin. The 41-kDa phosphatase was eluted from heparin-Sepharose by 0.20-0.25 M NaCl and preferentially dephosphorylated the beta-subunit of phosphorylase kinase. It was stimulated by polycations and inhibited by okadaic acid (IC50 = 2 nM), but its activity was not affected by inhibitor-2 or heparin. The 36-kDa phosphatase was eluted from heparin-Sepharose by 0.45-0.50 M NaCl and preferentially dephosphorylated the beta-subunit of phosphorylase kinase. It was inhibited by inhibitor-2, heparin, histone H1, and okadaic acid (IC50 = 70 nM). The 37- and 36-kDa phosphatases can be classified as type-2A and type-1 enzymes, respectively. The 41-kDa phosphatase does not precisely fit the criteria of either type, showing only partial similarities to both type-1 and type-2A enzymes and it may represent a novel type of protein phosphatase in bovine platelets.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Archives of Biochemistry And Biophysics. - 298 : 2 (1992), p. 682-687. -
További szerzők:Sparks, Lloyd Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus) Murányi Andrea (1966-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

9.

001-es BibID:BIBFORM047052
035-os BibID:PMID:2854691
Első szerző:Farkas Ilona (biokémikus)
Cím:Activation/dephosphorylation of rabbit muscle glycogen synthase by the catalytic subunits of protein phosphatase-1 and 2A / Ilona Farkas, B. Tóth, Gy. Vereb, Csilla Csortos, P. Gergely
Dátum:1988
ISSN:0237-6261
Megjegyzések:Glycogen synthase a was purified from rabbit skeletal muscle by a procedure involving heparin-Sepharose chromatography. Glycogen synthase a was phosphorylated by the catalytic subunit of cAMP-dependent protein kinase to give synthase b1. Dephosphorylation and activation of synthase b1 was investigated using the catalytic subunits of protein phosphatase-1 and 2A. The dephosphorylation and activation of synthase b1 was biphasic with a larger rate constant for the initial phase. Analysis of tryptic phosphopeptides of glycogen synthase during the course of dephosphorylation revealed a faster initial phosphate release from site-2 by both phosphatases comparing to sites-1a and 1b. Ligand effects on synthase phosphatase reactions were also studied. Spermine was found to inhibit protein phosphatase-1 activity and to stimulate type-2A phosphatase using synthase b1 as substrate.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Acta Biochimica et Biophysica Hungarica. - 23 : 3-4 (1988), p. 231-246. -
További szerzők:Tóth Béla (1954-) (vegyész, biokémikus) Vereb György (1938-) (biokémikus, sejtbiológus) Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

10.

001-es BibID:BIBFORM028726
Első szerző:Kiss Enikő
Cím:Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton / Enikő Kiss, Andrea Murányi, Csilla Csortos, Pál Gergely, Masaaki Ito, David J. Hartshorne, Ferenc Erdődi
Dátum:2002
ISSN:0264-6021
Megjegyzések:The myosin phosphatase (MP) composed of the catalytic subunit of type 1 protein phosphatase and myosin phosphatase target subunit isoform 1 (MYPT1) was identified as the major serine/threonine phosphatase component in the platelet-cytoskeleton fraction. MYPT1 was phosphorylated by cytoskeletal kinase(s), but the identity of the kinase(s) and the effect of phosphorylation were not established. Incubation of platelet-cytoskeletal fraction with MgATP or MgATP[S] (magnesium adenosine 5'-[gamma-thio]triphosphate) caused a decrease in the 20 kDa light-chain of smooth-muscle myosin (MLC20) phosphatase and phosphorylase phosphatase activities. MYPT1 contains a phosphorylation site, Thr-695, involved in the inhibition of MP in a RhoA/Rho kinase-dependent manner. The cytoskeletal kinase(s) phosphorylated Thr-695 of glutathione S-transferase (GST)-MYPT1, as determined with an antibody specific for phosphorylated Thr-695. The level of Rho kinase was low in the cytoskeletal fraction and was detected primarily in the membrane and cytosolic fractions. The phosphorylation of Thr-695 by the cytoskeletal kinase(s) was not affected by Rho kinase inhibitor, Y-27632, suggesting that kinase(s) other than Rho kinase were involved. In-gel kinase assay identified a kinase at 54-59 kDa that phosphorylated the C-terminal fragment of MYPT1 (GST-MYPT1(667-1004)). Western blots detected both zipper-interacting protein kinase (ZIPK) and integrin-linked kinase (ILK) at 54-59 kDa in the cytoskeleton and membrane fractions. Cytoskeletal ZIPK and ILK were separated and partially purified by chromatography on SP-Sepharose and on MonoQ. ZIPK preferentially phosphorylated MLC20 and had low activity on MYPT1. ILK phosphorylated both MLC20 and MYPT1 and phosphorylation of MYPT1 occured on Thr-695. The above results raise the potential for regulation of MP activity in platelet cytoskeleton by ILK and suggest an alternative to the Rho-linked pathway.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochemical Journal. - 365 : 1 (2002), p. 79-87. -
További szerzők:Murányi Andrea (1966-) (biokémikus) Ito, Masaaki Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus) Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

11.

001-es BibID:BIBFORM047041
035-os BibID:PMID:23721711
Első szerző:Kovács-Kása Anita
Cím:Protein phosphatase 2A activity is required for functional adherent junctions in endothelial cells / Anita Kása, István Czikora, Alexander D. Verin, Pál Gergely, Csilla Csortos
Dátum:2013
ISSN:0026-2862
Megjegyzések:Reversible Ser/Thr phosphorylation of cytoskeletal and adherent junction (AJ) proteins has a critical role in the regulation of endothelial cell (EC) barrier function. We have demonstrated earlier that protein phosphatase 2A (PP2A) activity is important in EC barrier integrity. In the present work, macro- and microvascular EC were examined and we provided further evidence on the significance of PP2A in the maintenance of EC cytoskeleton and barrier function with special focus on the Bα (regulatory) subunit of PP2A. Immunofluorescent staining revealed that the inhibition of PP2A results in changes in the organization of EC cytoskeleton as microtubule dissolution and actin re-arrangement were detected. Depletion of Bα regulatory subunit of PP2A had similar effect on the cytoskeleton structure of the cells. Furthermore, transendothelial electric resistance measurements demonstrated significantly slower barrier recovery of Bα depleted EC after thrombin treatment. AJ proteins, VE-cadherin and β-catenin, were detected along with Bα in pull-down assay. Also, the inhibition of PP2A (by okadaic acid or fostriecin) or depletion of Bα caused β-catenin translocation from the membrane to the cytoplasm in parallel with its phosphorylation on Ser552. In conclusion, our data suggest that the A/Bα/C holoenzyme form of PP2A is essential in EC barrier integrity both in micro- and macrovascular EC.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Microvascular Research. - 89 (2013), p. 86-94. -
További szerzők:Czikora István (1979-) (vegyész, biokémikus) Verin, Alexander Gergely Pál (1947-) (biokémikus) Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

12.

001-es BibID:BIBFORM040525
035-os BibID:PMID:2907509
Első szerző:Sipos Adrien
Cím:The antigen/receptor specificity of antigranulocyte antibodies in patients with SLE / Adrien Sipos, Csilla Csortos, Sándor Sipka, Pál Gergely, Ildikó Sonkoly, Gyula Szegedi
Dátum:1988
Megjegyzések:The antigen/receptor specificity of antigranulocyte antibodies (AGAs) detected in the sera of patients with systemic lupus erythematosus (SLE) was investigated by inhibitory immunofluorescence test and Western immunoblotting technique. The interactions of AGAs with antigens of intact normal granulocytes were determined by inhibiting the binding of different myeloid monoclonal antibodies (mAbs). Seven of the studied 12 sera revealed binding to CD15 (X hapten) and/or to CD16 (FcR1o). The specificity investigation of AGAs was completed with Western immunoblotting technique. The binding of AGAs to bands with Mr of about 50-60 kDa and at 30 kDa on unstimulated granulocyte plasma membrane preparation could be demonstrated from 4 out of 6 AGA positive SLE sera. The cause of the disappearance of bands on the phorbol-myristate-acetate (PMA) activated membrane except those of the 50-60 kDa bands is still to be discovered.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Immunology Letters. - 19 : 4 (1988), p. 329-334. -
További szerzők:Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus) Sonkoly Ildikó Szegedi Gyula (1936-2013) (belgyógyász, immunológus) Sipka Sándor (1945-) (laboratóriumi szakorvos)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:
Rekordok letöltése1 2 
Corvina könyvtári katalógus v8.2.27 © 2023 Monguz kft. Minden jog fenntartva.