CCL

Összesen 2 találat.
#/oldal:
Részletezés:
Rendezés:

1.

001-es BibID:BIBFORM011383
Első szerző:Varga Zsuzsa (biokémikus, nephrológus)
Cím:Structural Prerequisite for Antioxidant Activity of Silybin in Different Biochemical Systems in Vitro / Zs. Varga, I. Seres, E. Nagy, L. Ujhelyi, G. Balla, J. Balla, S. Antus
Dátum:2006
Megjegyzések:Structural analogues (flavanone: 2-4 and flavone: 5 and 6, respectively) of silybin (1a) were synthesized and tested for inhibitory activity on O2_ release and PKC translocation in PMA-stimulated neutrophils as well as xanthine oxidase activity in order to identify the molecular structures responsible for the antioxidant property of silybin. Concerning the prevention of hem-mediated oxidative modification of LDL by silybin, the hydroxyl radical scavenging activity of its structural analogues was also determined. We demonstrated that the basic skeleton of 1a (4) is responsible for its inhibitory activity on O2_ release in PMA-stimulated neutrophils via inhibition of PKC translocation, since introduction of a double bound and hydroxyl groups at C-5 and C-7 position (5 and 6) did not result in further increase in inhibition of O2_ release. It has been shown that the presence of the phenolic hydroxyl group at C-5 and C-7 of 1a is essential for the inhibition of xanthine oxidase activity. Moreover, introduction of a double bond into the C-ring of 2 and 3, resulting in flavone derivatives (5 and 6), markedly enhanced the antioxidant effect in all the tested systems. Finally, silybin (1a) and its flavon derivatives (5 and 6) directly scavenged hydroxyl radicals as well. On the basis of these results it might be concluded that different moiety of silybin is responsible for inhibition of overproduction of O2_ in stimulated neutrophils, xanthine oxidase activity, and for prevention of hemmediated oxidative modification of LDL.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Silybin
Oxidative stress
Antioxidants
Protein kinase C
Xanthine oxidase
Low density lipoprotein
Megjelenés:Phytomedicine. - 13 : 1-2 (2006), p. 85-93. -
További szerzők:Seres Ildikó (1954-) (biokémikus) Nagy Emőke (neonatológus, gyermekgyógyász) Újhelyi László (1956-) (belgyógyász) Balla György (1953-) (csecsemő és gyermekgyógyász, neonatológus) Balla József (1959-) (belgyógyász, nephrológus) Antus Sándor (1944-2022) (vegyészmérnök)
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

2.

001-es BibID:BIBFORM022526
Első szerző:Varga Zsuzsa
Cím:Effect of silybin on phorobol myristate actetate-induced protein kinase C translocation, NADPH oxidase activity and apoptosis in human neutrophils / Zsuzsa Varga, László Ujhelyi, Attila Kiss, József Balla, Andrea Czompa, Sándor Antus
Dátum:2004
Megjegyzések:Mechanism of the action of silybin (1) and its derivatives (2-4), possessing different lipid solubility in PMA-stimulated neutrophils was evaluated. Silybin (1) inhibited the calcium, phosphatidylserine- and diacylglycerol-dependent protein kinase C translocation and the NADPH oxidase activity in PMA-stimulated neutrophils and resulted in decreased apoptosis. Furthermore, silybin (1) inhibited xanthine oxidase activity and hem-mediated oxidative degradation of low-density lipoprotein, as well. Its derivatives (2-4), possessing different lipid-solubility, affected all the studied parameters. The lipid solubility of silybin (1) was enhanced by methylation (5·7·4··trimethylsilybin: 2), whereas a decrease in lipid-solubility by acetylation of compound 2 (5·,7,·4··-trimethylsilybin-acetate: 3) or all the hydroxyl groups of silybin (peracetyl-silybin: 4) attenuated the antioxidant capacity by decreasing the inhibition in PKC translocation and NADPH oxidase activation. All the derivatives of silybin (2-4) showed no inhibition in cell free systems; e.g. did not alter the xanthine oxidase activity and the hem-mediated oxidative degradation of LDL. In conclusion, the antioxidant activity of (1) might be due to its ability to inhibit PKC translocation and NADPH oxidase activation in PMA-stimulated neutrophils. The increase of lipid solubility of silybin (1) supports its penetration through cell membrane and enhances its inhibitory effects. This structural modification of (1) might have pharmacological consequences.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
oxidative stress
silybin
antioxidants
protein kinase C
NADPH oxidase
apoptosis
neutrophil
Megjelenés:Phytomedicine. - 11 : 2-3 (2004), p. 206-212. -
További szerzők:Újhelyi László (1956-) (belgyógyász) Kiss Attila (1942-) (belgyógyász, haematológus) Balla József (1959-) (belgyógyász, nephrológus) Czompa Andrea (1970-) (kémia-fizika szakos tanár) Antus Sándor (1944-2022) (vegyészmérnök)
Pályázati támogatás:T 29090
OTKA
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Rekordok letöltése1