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001-es BibID:BIBFORM064412
035-os BibID:(scopus)84976324555 (wos)000381535900025
Első szerző:Balogh Enikő (molekuláris biológus)
Cím:Osteogenic differentiation of human lens epithelial cells might contribute to lens calcification / Enikő Balogh, Andrea Tóth, Emese Tolnai, Tímea Bodó, Emese Bányai, Dóra Júlia Szabó, Goran Petrovski, Viktória Jeney
Dátum:2016
ISSN:0006-3002
Megjegyzések:Calcification of the human lens has been described in senile cataracts and in young patients with congenital cataractor chronic uveitis. Lens calcification is also a major complication of cataract surgery and plays a role in theopacification of intraocular lenses. A cell-mediated process has been suggested in the background of lens calcification,but so far the exact mechanism remained unexplored. Lens calcification shares remarkable similaritieswith vascular calcification; in both pathological processes hydroxyapatite accumulates in the soft tissue. Vascularcalcification is a regulated, cell-mediated process in which vascular cells undergo osteogenic differentiation. Ourobjective was to investigate whether human lens epithelial cells (HuLECs) can undergo osteogenic transitionin vitro, and whether this process contributes to lens calcification. We used inorganic phosphate (Pi) and Ca tostimulate osteogenic differentiation of HuLECs. Osteogenic stimuli (2.5 mmol/L Pi and 1.2 mmol/L Ca) inducedextracellular matrix mineralization and Ca deposition in HuLECswith the critical involvement of active Pi uptake.Osteogenic stimuli almost doubled mRNA expressions of osteo-/chondrogenic transcription factors Runx2 andSox9, which was accompanied by a 1.9-fold increase in Runx2 and a 5.5-fold increase in Sox9 protein expressions.Osteogenic stimuli induced mRNA and protein expressions of alkaline phosphatase and osteocalcin in HuLEC. Cacontentwas higher in human cataractous lenses, compared to non-cataractous controls (n=10). Osteocalcin, anosteoblast-specific protein, was expressed in 2 out of 10 cataractous lenses.We conclude that osteogenic stimuliinduce osteogenic differentiation of HuLECs and propose that this mechanism might play a role in lenscalcification.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Human lens epithelial cells
Osteogenic differentiation
Calcification
Cataract
Aging disease
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Basis of Disease. - 1862 : 9 (2016), p. 1724-1731. -
További szerzők:Tóth Andrea (1992-) (molekuláris biológus) Szilágyi-Tolnai Emese (1988-) (Molekuláris biológus) Bodó Timea Bányai Emese (1984-) (orvos) Szabó Dóra Júlia (1985-) (Ph.D hallgató) Petrovski, Goran (1975-) (orvos) Jeney Viktória (1971-) (vegyész, kémia tanár)
Pályázati támogatás:K116024
OTKA
RH/751-2/2015
Egyéb
4.2.2.A/2-11-1-2012-0001
TÁMOP
KTIA_NAP_12-A_III/9
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001-es BibID:BIBFORM072211
035-os BibID:(cikkazonosító)4310816 (PMID)29743981 (PMCID)PMC5883980
Első szerző:Erdei Judit Zsuzsa (vegyész)
Cím:Induction Of NLRP3 Inflammasome Activation By Heme In Human Endothelial Cells / Judit Erdei, Andrea Tóth, Enikő Balogh, Benard Bogonko Nyakundi, Emese Bányai, Bernhard Ryffel, György Paragh, Mario D. Cordero, Viktória Jeney
Dátum:2018
ISSN:1942-0994 1942-0900
Megjegyzések:Hemolytic or hemorrhagic episodes are often associated with inflammation even when infectious agents are absent suggesting that red blood cells (RBCs) release damage-associated molecular patterns (DAMPs). DAMPs activate immune and nonimmune cells through pattern recognition receptors. Heme, released from RBCs, is a DAMP and induces IL-1β production through the activation of the nucleotide-binding domain and leucine-rich repeat-containing family and pyrin domain containing 3 (NLRP3) in macrophages; however, other cellular targets of heme-mediated inflammasome activation were not investigated. Because of their location, endothelial cells can be largely exposed to RBC-derived DAMPs; therefore, we investigated whether heme and other hemoglobin- (Hb-) derived species induce NLRP3 inflammasome activation in these cells. We found that heme upregulated NLRP3 expression and induced active IL-1β production in human umbilical vein endothelial cells (HUVECs). LPS priming largely amplified the heme-mediated production of IL-1β. Heme administration into C57BL/6 mice induced caspase-1 activation and cleavage of IL-1β which was not observed in NLRP3?/? mice. Unfettered production of reactive oxygen species played a critical role in heme-mediated NLRP3 activation. Activation of NLRP3 by heme required structural integrity of the heme molecule, as neither protoporphyrin IX nor iron-induced IL-1β production. Neither naive nor oxidized forms of Hb were able to induce IL-1β production in HUVECs. Our results identified endothelial cells as a target of heme-mediated NLRP3 activation that can contribute to the inflammation triggered by sterile hemolysis. Thus, understanding the characteristics and cellular counterparts of RBC-derived DAMPs might allow us to identify new therapeutic targets for hemolytic diseases.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Heme
endothelial cells
hemolysis
hemoglobin
DAMP
NLRP3 inflammasome activation
IL-1?
ROS
Megjelenés:Oxidative Medicine and Cellular Longevity. - 2018 (2018), p. 1-14. -
További szerzők:Tóth Andrea (1992-) (molekuláris biológus) Balogh Enikő (1987-) (molekuláris biológus) Nyakundi, Benard Bogonko (1983-) (biokémikus) Bányai Emese (1984-) (orvos) Ryffel, Bernhard Paragh György (1953-) (belgyógyász) Cordero, Mario D. Jeney Viktória (1971-) (vegyész, kémia tanár)
Pályázati támogatás:NKFIH K116024
Egyéb
GINOP-2.3.2-15-2016-00005
GINOP
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