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001-es BibID:	BIBFORM096311
035-os BibID:	(cikkazonosító)427
Első szerző:	Balogh Enikő (molekuláris biológus)
Cím:	Heme-Mediated Activation of the Nrf2/HO-1 Axis Attenuates Calcification of Valve Interstitial Cells / Balogh Enikő, Chowdhury Arpan, Ababneh Haneen, Csiki Dávid Máté, Tóth Andrea, Jeney Viktória
Dátum:	2021
ISSN:	2227-9059
Megjegyzések:	Calcific aortic valve stenosis (CAVS) is a heart disease characterized by the progressive fibro-calcific remodeling of the aortic valves, an actively regulated process with the involvement of the reactive oxygen species-mediated differentiation of valvular interstitial cells (VICs) into osteoblast-like cells. Nuclear factor erythroid 2-related factor 2 (Nrf2) regulates the expression of a variety of antioxidant genes, and plays a protective role in valve calcification. Heme oxygenase-1 (HO-1), an Nrf2-target gene, is upregulated in human calcified aortic valves. Therefore, we investigated the effect of Nrf2/HO-1 axis in VIC calcification. We induced osteogenic differentiation of human VICs with elevated phosphate and calcium-containing osteogenic medium (OM) in the presence of heme. Heme inhibited Ca deposition and OM-induced increase in alkaline phosphatase and osteocalcin (OCN) expression. Heme induced Nrf2 and HO-1 expression in VICs. Heme lost its anti-calcification potential when we blocked transcriptional activity Nrf2 or enzyme activity of HO-1. The heme catabolism products bilirubin, carbon monoxide, and iron, and also ferritin inhibited OM-induced Ca deposition and OCN expression in VICs. This study suggests that heme-mediated activation of the Nrf2/HO-1 pathway inhibits the calcification of VICs. The anti-calcification effect of heme is attributed to the end products of HO-1-catalyzed heme degradation and ferritin.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Biomedicines. - 9 : 4 (2021), p. 1-17. -
További szerzők:	Chowdhury, Arpan (1996-) (molekuláris biológus) Ababneh, Haneen Muntasir (1992-) Csiki Dávid Máté (1993-) (biomérnök) Tóth Andrea (1992-) (molekuláris biológus) Jeney Viktória (1971-) (vegyész, kémia tanár)
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001-es BibID:	BIBFORM124399
Első szerző:	Tóth Andrea (molekuláris biológus)
Cím:	In Vitro Models of Cardiovascular Calcification / Tóth Andrea, Balogh Enikő, Jeney Viktória
Dátum:	2024
ISSN:	2227-9059
Megjegyzések:	Cardiovascular calcification, characterized by hydroxyapatite deposition in the arterial wall and heart valves, is associated with high cardiovascular morbidity and mortality. Cardiovascular calcification is a hallmark of aging but is frequently seen in association with chronic diseases, such as chronic kidney disease (CKD), diabetes, dyslipidemia, and hypertension in the younger population as well. Currently, there is no therapeutic approach to prevent or cure cardiovascular calcification. The pathophysiology of cardiovascular calcification is highly complex and involves osteogenic differentiation of various cell types of the cardiovascular system, such as vascular smooth muscle cells and valve interstitial cells. In vitro cellular and ex vivo tissue culture models are simple and useful tools in cardiovascular calcification research. These models contributed largely to the discoveries of the numerous calcification inducers, inhibitors, and molecular mechanisms. In this review, we provide an overview of the in vitro cell culture and the ex vivo tissue culture models applied in the research of cardiovascular calcification.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk vascular calcification valve calcification vascular smooth muscle cell calcification valve interstitial cell calcification calcification inducers calcification detection
Megjelenés:	Biomedicines. - 12 : 9 (2024), p. 1-15. -
További szerzők:	Balogh Enikő (1987-) (molekuláris biológus) Jeney Viktória (1971-) (vegyész, kémia tanár)
Pályázati támogatás:	NKFIH K146669 Egyéb MTA-DE Lendület 96050 Egyéb BO/00443/21 Egyéb ÚNKP-23-5-DE-499 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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