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001-es BibID:	BIBFORM014363
Első szerző:	Zákány Róza (anatómus-, kötőszövetbiológus)
Cím:	Protein Phosphatase 2A Is Involved in the Regulation of Protein Kinase A Signaling Pathway during in Vitro Chondrogenesis / Róza Zákány, Kornélia Szűcs, Éva Bakó, Szabolcs Felszeghy, Gabriella Czifra, Tamás Bíró, László Módis, Pál Gergely
Dátum:	2002
ISSN:	0014-4827
Megjegyzések:	aWe have evaluated the importance of the Ser/Thr protein phosphorylation anddephosphorylation for chondrogenesis in high-density chicken limb bud mesenchymalcell cultures (HDCs) by using H89, a cell-permeable protein kinase inhibitor, andokadaic acid (OA), a phosphoprotein phosphatase (PP)-specific inhibitor molecule.When 20 nM OA was applied to the HDCs on Days 2 and 3 of culturing, itsignificantly inhibited protein phosphatase 2A (PP2A), enhanced cartilageformation, and elevated the activity of cAMP-dependent protein kinase (PKA).Application of 20 microM H89 significantly decreased the activity of PKA andblocked the chondrogenesis in HDCs. Furthermore, OA enhanced cartilage formationand elevated the suppressed activity of PKA even in the H89-pretreated HDCs.cGMP-dependent protein kinase was not detected in HDCs, while protein kinase Cmu(PKCmu), which is also inhibited by nanomolar concentrations of H89, was presentthroughout the culturing period. Neither OA nor H89 influenced the expression ofthe catalytic subunit of PKA or the cAMP response element binding protein, CREB.However, a significantly elevated amount of Ser-133-phosphorylated-CREB (P-CREB)was detected following addition of OA, while H89 treatment resulted in a decreaseof the amount of P-CREB. Our results demonstrate that PP2A plays a role in theregulation of the PKA signaling pathway and that the phosphorylation level ofCREB is influenced by the activity of both enzymes during in vitrochondrogenesis.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban a0 (Cyclic AMP Response Element-Binding Protein) 0 (Enzyme Inhibitors) 0 (Isoquinolines) 0 (Sulfonamides) 127243-85-0 (N-(2-(4-bromocinnamylamino)ethyl)-5-isoquinolinesulfonamide) 56-45-1 (Serine) 72-19-5 (Threonine) 78111-17-8 (Okadaic Acid) EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases) EC 3.1.3.16 (Phosphoprotein Phosphatases) EC 3.1.3.16 (Protein Phosphatase 2) Animals Cartilage/drug effects/embryology/metabolism Cell Differentiation/drug effects/physiology Cell Division/drug effects/physiology Cells, Cultured Chick Embryo Chondrocytes/drug effects/metabolism Chondrogenesis/drug effects/physiology Cyclic AMP Response Element-Binding Protein/metabolism Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors/metabolism Dose-Response Relationship, Drug Enzyme Inhibitors/pharmacology Isoquinolines/pharmacology Limb Buds/embryology/metabolism Okadaic Acid/pharmacology Phosphoprotein Phosphatases/drug effects/metabolism Phosphorylation Protein Phosphatase Serine/chemistrySignal Transduction Sulfonamides Threonine/chemistry Time Factors egyetemen (Magyarországon) készült közlemény
Megjelenés:	Experimental Cell Research. - 275 : 1 (2002), p. 1-8. -
További szerzők:	Szűcs Kornélia (1945-) (biokémikus) Bakó Éva (1958-) (biokémikus) Felszeghy Szabolcs Béla (1972-) (fogorvos, anatómus, kötőszövetbiológus) Czifra Gabriella (1975-) (élettanász) Bíró Tamás (1968-) (élettanász) Módis László (1939-) (anatómus, kötőszövetbiológus) Gergely Pál (1947-) (biokémikus)
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