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001-es BibID:BIBFORM006656
Első szerző:Fodor János (élettanász, biotechnológus)
Cím:Ionotropic purinergic receptor P2X4 is involved in the regulation of chondrogenesis in chicken micromass cell cultures / Fodor J., Matta Cs., Juhász T., Oláh T., Gönczi M., Szíjgyártó Zs., Gergely P., Csernoch L., Zákány R.
Dátum:2009
Megjegyzések:We have previously demonstrated that elevation of free cytosolic Ca(2+) concentration at the time of differentiation of chondroblasts was mainly due to a Ca(2+) influx and it was indispensable to cartilage formation in chicken high density mesenchymal cell cultures (HDC) [C. Matta, J. Fodor, Z. Szijgyarto, T. Juhasz, P. Gergely, L. Csernoch, R. Zakany, Cytosolic free Ca(2+) concentration exhibits a characteristic temporal pattern during in vitro cartilage differentiation: a possible regulatory role of calcineurin in Ca-signalling of chondrogenic cells, Cell Calcium 44 (2008) 310-323]. Here, we report that chondrogenic cells secreted ATP and administration of ATP to the culture medium evoked Ca(2+) transients exclusively in the presence of extracellular Ca(2+) and only on day 3 of culturing, when the final commitment of chondroblasts occurs. Moreover, ATP caused elevated protein expression of the chondrogenic transcription factor Sox9 and stimulated cartilage matrix production. Expression pattern of different types of both ionotropic and metabotropic purinergic receptors was detected. Agonists of metabotropic receptors, ADP and UDP did not evoke any Ca(2+) transients and had no influence on cartilage formation, while UTP caused transient elevation of cytosolic Ca(2+) concentration in 3-day-old HDC without stimulating matrix production. Suramin, which blocks all P2X receptors but not P2X(4) did not impede the effects of ATP, furthermore, P2X(4) appeared in the plasma membrane fraction and gave signals with immunocytochemistry only from day 3. In summary, we suggest a role of ionotropic purinergic signalling of P2X(4) in the generation of ATP-dependent Ca(2+) transients of differentiating chondroblasts.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
in vitro cartilage formation
high density cell culture
Fura-2
single cell Ca measurement
P2X receptors
P2Y receptors
ATP secretion
immunocytochemistry
Megjelenés:Cell Calcium. - 45 : 5 (2009), p. 421-430. -
További szerzők:Matta Csaba (1980-) (molekuláris biológus, genetikus, angol szakfordító) Juhász Tamás (1976-) (biológus, orvosbiológus) Oláh Tamás (1983-) (élettanász) Gönczi Mónika (1974-) (élettanász) Szíjgyártó Zsolt (1978-) (vegyész) Gergely Pál (1947-) (biokémikus) Csernoch László (1961-) (élettanász) Zákány Róza (1963-) (anatómus-, kötőszövetbiológus)
Internet cím:DOI
elektronikus változat
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2.

001-es BibID:BIBFORM004124
Első szerző:Fodor János (élettanász, biotechnológus)
Cím:Altered expression of triadin 95 causes parallel changes in localized Ca2+ release events and global Ca2+ signals in skeletal muscle cells in culture / Janos Fodor, Monika Gonczi, Monika Sztretye, Beatrix Dienes, Tamas Olah, Laszlo Szabo, Eszter Csoma, Peter Szentesi, Gyula P. Szigeti, Isabelle Marty, Laszlo Csernoch
Dátum:2008
Megjegyzések:The 95 kDa triadin (Trisk 95), an integral protein of the sarcoplasmic reticular membrane in skeletal muscle, interacts with both the ryanodine receptor (RyR) and calsequestrin. While its role in the regulation of calcium homeostasis has been extensively studied, data are not available on whether the overexpression or the interference with the expression of Trisk 95 would affect calcium sparks the localized events of calcium release (LCRE). In the present study LCRE and calcium transients were studied using laser scanning confocal microscopy on C2C12 cells and on primary cultures of skeletal muscle. Liposome- or adenovirus-mediated Trisk 95 overexpression and shRNA interference with triadin translation were used to modify the level of the protein. Stable overexpression in C2C12 cells significantly decreased the amplitude and frequency of calcium sparks, and the frequency of embers. In line with these observations, depolarization-evoked calcium transients were also suppressed. Similarly, adenoviral transfection of Trisk 95 into cultured mouse skeletal muscle cells significantly decreased both the frequency and amplitude of spontaneous global calcium transients. Inhibition of endogenous triadin expression by RNA interference caused opposite effects. Primary cultures of rat skeletal muscle cells expressing endogenous Trisk 95 readily generated spontaneous calcium transients but rarely produced calcium sparks. Their transfection with specific shRNA sequence significantly reduced the triadin-specific immunoreactivity. Functional experiments on these cells revealed that while caffeine-evoked calcium transients were reduced, LCRE appeared with higher frequency. These results suggest that Trisk 95 negatively regulates RyR function by suppressing localized calcium release events and global calcium signals in cultured muscle cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:The Journal of Physiology (London). - 586 : 23 (2008), p. 5803-5818. -
További szerzők:Gönczi Mónika (1974-) (élettanász) Sztretye Mónika (1981-) (élettanász, elektrofiziológus) Dienes Beatrix (1972-) (élettanász, molekuláris biológus) Oláh Tamás (1983-) (élettanász) Szabó László (Románia) Csoma Eszter (1978-) (molekuláris biológus, mikrobiológus) Szentesi Péter (1967-) (élettanász) Szigeti Gyula (1969-) (élettanász, elektrofiziológus) Marty, Isabelle Csernoch László (1961-) (élettanász)
Internet cím:elektronikus változat
elektronikus változat
DOI
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3.

001-es BibID:BIBFORM083002
035-os BibID:(WOS)000680961800012 (Scopus)85078617993
Első szerző:Gönczi Mónika (élettanász)
Cím:Septins, a cytoskeletal protein family, with emerging role in striated muscle / Gönczi Mónika, Dienes Beatrix, Dobrosi Nóra, Fodor János, Balogh Norbert, Oláh Tamás, Csernoch László
Dátum:2021
ISSN:0142-4319
Megjegyzések:Appropriate organization of cytoskeletal components are required for normal distribution and intracellular localization of different ion channels and proteins involved in calcium homeostasis, signal transduction, and contractile function of striated muscle. Proteins of the contractile system are in direct or indirect connection with the extrasarcomeric cytoskeleton. A number of other molecules which have essential role in regulating stretch-, voltage-, and chemical signal transduction from the surface into the cytoplasm or other intracellular compartments are already well characterized. Sarcomere, the basic contractile unit, is comprised of a precisely organized system of thin (actin), and thick (myosin) filaments. Intermediate filaments connect the sarcomeres and other organelles (mitochondria and nucleus), and are responsible for the cellular integrity. Interacting proteins have a very diverse function in coupling of the intracellular assembly components and regulating the normal physiological function. Despite the more and more intense investigations of a new cytoskeletal protein family, the septins, only limited information is available regarding their expression and role in striated, especially in skeletal muscles. In this review we collected basic and specified knowledge regarding this protein group and emphasize the importance of this emerging field in skeletal muscle biology.
Helyes pályázati azonosító: GINOP-2.3.2-15-2016-00040
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Cellular function
Oligomer assembly
Septin
Striated muscle
Megjelenés:Journal Of Muscle Research And Cell Motility. - 42 : 2 (2021), p. 251-265. -
További szerzők:Dienes Beatrix (1972-) (élettanász, molekuláris biológus) Dobrosi Nóra (1981-) (molekuláris biológus) Fodor János (1973-) (élettanász, biotechnológus) Balogh Norbert (1988-) (molekuláris biológus) Oláh Tamás (1983-) (élettanász) Csernoch László (1961-) (élettanász)
Pályázati támogatás:GINOP-2.3.2-15-2016-0004
GINOP
GINOP-2.3.2-15-2016-0044
GINOP
EFOP-3.6.2-16-2017-00006
EFOP
NK-115461
OTKA
20428-3/2018/FEKUTSTRAT
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