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001-es BibID:	BIBFORM042355
035-os BibID:	PMID:11124542
Első szerző:	Muratoglu, S.
Cím:	Primary structure of human matrilin-2, chromosome location of the MATN2 gene and conservation of an AT-AC intron in matrilin genes / S. Muratoglu, K. Krysan, M. Balázs, H. Sheng, R. Zákány, L. Módis, I. Kiss, F. Deák
Dátum:	2000
ISSN:	0301-0171
Megjegyzések:	We isolated full-length cDNA clones for human matrilin-2, an oligomeric protein, which forms filamentous networks in the extracellular matrices of various tissues. The human matrilin-2 precursor is encoded by a 4.0-kb mRNA, it consists of 956 amino acids and shows 93% similarity to the mouse protein. Out of the two von Willebrand factor type A-like domains, the 10 epidermal growth factor-type modules, one unique sequence and the oligomerization module, the first A domain is the most conserved. RT-PCR demonstrated wide expression of the gene in human cell lines of fibroblastic or epithelial origin. Alternative splicing affected only 19 amino acids in a 75-moiety-long segment, unique to matrilin-2. Isolation and analysis of the 3' end of the gene revealed that the reason for alternative splicing is alternative 3' splice site selection. Further, we identified in the human matrilin-2 gene a U12 type AT-AC intron between the last two exons encoding the oligomerization domain. We mapped the matrilin-2 gene (MATN2) by fluorescence in situ hybridization at chromosome position 8q22.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban külföldön készült közlemény
Megjelenés:	Cytogenetics and Cell Genetics. - 90 : 3-4 (2000), p. 323-327. -
További szerzők:	Krysan, K. Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Sheng, H. Zákány Róza (1963-) (anatómus-, kötőszövetbiológus) Módis László (1939-) (anatómus, kötőszövetbiológus) Kiss I. Deák F.
Pályázati támogatás:	OTKA T29157 OTKA FKFP 1292/1997 Egyéb
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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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)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat elektronikus változat DOI
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