CCL

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001-es BibID:BIBFORM029089
Első szerző:Ádány Róza (megelőző orvostan és népegészségtan szakorvos)
Cím:Factor XIII of blood coagulation as a nuclear crosslinking enzyme / Ádány R., Bárdos H., Antal M., Módis L., Sárváry A., Szűcs S., Balogh I.
Dátum:2001
Megjegyzések:Intracellular localization and distribution of Factor XIII subunit A (FXIIIA) was investigated in association with monocyte-macrophage differentiation in a long term culture of human monocytes by light- and electron microscopical as well as biochemical and immunobiochemical techniques. To allow the detection of FXIIIA in cells with well-preserved ultrustructure, immunosera against glutaraldehyde-derivatized recombinant FXIIIA were developed in rabbits, then characterized and used in this study. In the early phase of macrophage differentiation intranuclear accumulation of FXIIIA was detected as a transient phenomenon in cells of the 2nd day culture by optical sectioning with 0,7 microm steps in laser scanning confocal microscopy and immunoblotting technique. FXIIIA could be detected by immunoelectron microscopic postembedding staining over electrodense DNA-containing areas. Fluoresceinated monodansylcadaverine incorporation assay was used to demonstrate that FXIIIA is not only present in the nuclei, but also expresses its transglutaminase activity. Our finding of the nuclear accumulation of FXIIIA in differentiating human macrophages is also unique in that a blood clotting factor has, for the first time, been localized in nuclei and has been shown to be an intracellular crosslinking enzyme. The possible role of nuclear FXIIIA in association with cellular processes involving chromatin structure remodeling, such as cell death, cell differentiation or cellular proliferation requires further in-depth investigation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Thrombosis and Haemostasis. - 85 : 5 (2001), p. 845-851. -
További szerzők:Bárdos Helga (1969-) (megelőző orvostan és népegészségtan szakorvos) Antal Miklós (1951-) (orvos, anatómus) Módis László (1939-) (anatómus, kötőszövetbiológus) Sárváry Attila (1971-) (népegészségtan szakorvos) Szűcs Sándor (1958-) (biokémikus, vegyész) Balogh Imre
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM015613
035-os BibID:11195086
Első szerző:Zákány Róza (anatómus-, kötőszövetbiológus)
Cím:Okadaic acid-induced inhibition of protein phosphatase 2A enhances chondrogenesisin chicken limb bud micromass cell cultures / Róza Zákány, Éva Bakó, Szabolcs Felszeghy, Krisztina Holló, Margit Balázs, Helga Bárdos, Pál Gergely, László Módis
Dátum:2001
ISSN:0340-2061 (Linking)
Megjegyzések:The role of major cellular serine/threonine-specific protein phosphatases,protein phosphatase 1 and 2A, was investigated during chicken cartilagedifferentiation under in vitro conditions. Activity of protein phosphatase 2Adecreased parallel to differentiation of chondrogenic cells, whereas activity ofprotein phosphatase 1 remained unchanged as assayed in the supernatants of thehomogenised chicken limb bud micromass cell cultures. When okadaic acid, a potentinhibitor of protein phosphatase 1 and 2A was applied in 20 nM concentration for4 h during the second and third culturing days, it significantly increased thesize of metachromatic cartilage areas measured in 6-day-old colonies. Followingokadaic acid treatments, a significant inhibition in the activity of proteinphosphatase 2A was found, while the activity of protein phosphatase 1 wasunaffected as measured an days 2 and 3. TRITC-phalloidin labelling demonstratedthat okadaic acid disorganised actin filaments and induced rounding ofchondrogenic cells. This deterioration of actin filaments was reversible.Electron microscopy and biochemical analysis of colonies revealed that theultrastructure and major components of cartilage matrix remained unchanged underthe effect of okadaic acid. Okadaic acid-treatment applied to cultures containingpredominantly differentiated chondrocytes (after day 4) did not influence thecartilage formation. 3H-thymidine and bromodeoxyuridine incorporation-assaysdemonstrated enhanced cell proliferation in the okadaic acid-treated coloniescompared to that of the untreated ones. Our results indicate, for the first time,that protein phosphatase 2A is involved in the regulation of chondrogenesis.Inhibition of protein phosphatase 2A with okadaic acid may result in increasedchondrogenesis via modulation of proliferation and cytoskeletal organisation, aswell as via alteration of protein kinase A-signaling pathway of the chondrogeniccells.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
78111-17-8 (Okadaic Acid)
EC 3.1.3.16 (Phosphoprotein Phosphatases)
EC 3.1.3.16 (Protein Phosphatase 1)
EC 3.1.3.16 (Protein Phosphatase 2)
Animals
Cartilage/*embryology/metabolism/ultrastructure
Cell Differentiation/drug effects/physiology
Cell Division/drug effects/physiology
Cells, Cultured/drug effects/metabolism/ultrastructure
Chick Embryo
Chondrocytes/drug effects/*metabolism/ultrastructure
Chondrogenesis/drug effects/*physiology
Cytoskeleton/drug effects/metabolism/ultrastructure
Dose-Response Relationship, Drug
Limb Buds/*embryology/metabolism/ultrastructure
Microfilaments/drug effects/metabolism/ultrastructure
Okadaic Acid/*pharmacology
Phosphoprotein Phosphatases/drug effects/*metabolism
Phosphorylation/drug effects
Protein Phosphatase 1
Protein Phosphatase 2
Signal Transduction/drug effects/physiology
egyetemen (Magyarországon) készült közlemény
Megjelenés:Anatomy and Embryology. - 203 : 1 (2001), p. 23-34. -
További szerzők:Bakó Éva (1958-) (biokémikus) Felszeghy Szabolcs Béla (1972-) (fogorvos, anatómus, kötőszövetbiológus) Holló Krisztina (1967-) (vegyész) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Bárdos Helga (1969-) (megelőző orvostan és népegészségtan szakorvos) Gergely Pál (1947-) (biokémikus) Módis László (1939-) (anatómus, kötőszövetbiológus)
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