Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome c

Lajos Vodnyánszky; Attila Marton; István Venekei; Mikiós Végh; Anna Blázovits; Ágnes Kittel; István Horváth

doi:10.1016/0005-2760(85)90299-1

Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome c

Lajos Vodnyánszky, Attila Marton, István Venekei, Mikiós Végh, Anna Blázovits, Ágnes Kittel, István Horváth

Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review

11 Citations (Scopus)

Abstract

Heme-nonapeptide, derived from cytochrome c, inhibited both the NADPH- and NADH-dependent lipid peroxidation of brain microsomes but, in the case of liver microsomes, this inhibitory effect manifested itself in the presence of SKF-525A (a specific Mocker of cytochrome P-450) only. Heme-nonapeptide prevented the transient accumulation of lipid peroxides in microsomes during lipid peroxidation. The oxygen consumption of microsomes in the presence of NADPH or NADH was stimulated by heme-nonapeptide. From these results we concluded that, in vitro, there are two independent mechanisms of lipid peroxidation in liver microsomes. It is suggested that, in vivo, the heme-peptide-sensitive mechanism, observed in brain microsomes, is more important. © 1985.

Original language	English
Pages (from-to)	411-414
Journal	Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume	835
Issue number	2
DOIs	https://doi.org/10.1016/0005-2760(85)90299-1
Publication status	Published - 9 Jul 1985
Externally published	Yes

Research Keywords

(Brain and liver microsome)
Heme-nonapeptide inhibitor
Lipid peroxidation
SKF-525A

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10.1016/0005-2760(85)90299-1

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title = "Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome c",

abstract = "Heme-nonapeptide, derived from cytochrome c, inhibited both the NADPH- and NADH-dependent lipid peroxidation of brain microsomes but, in the case of liver microsomes, this inhibitory effect manifested itself in the presence of SKF-525A (a specific Mocker of cytochrome P-450) only. Heme-nonapeptide prevented the transient accumulation of lipid peroxides in microsomes during lipid peroxidation. The oxygen consumption of microsomes in the presence of NADPH or NADH was stimulated by heme-nonapeptide. From these results we concluded that, in vitro, there are two independent mechanisms of lipid peroxidation in liver microsomes. It is suggested that, in vivo, the heme-peptide-sensitive mechanism, observed in brain microsomes, is more important. {\textcopyright} 1985.",

keywords = "(Brain and liver microsome), Heme-nonapeptide inhibitor, Lipid peroxidation, SKF-525A",

author = "Lajos Vodny{\'a}nszky and Attila Marton and Istv{\'a}n Venekei and Miki{\'o}s V{\'e}gh and Anna Bl{\'a}zovits and {\'A}gnes Kittel and Istv{\'a}n Horv{\'a}th",

year = "1985",

month = jul,

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doi = "10.1016/0005-2760(85)90299-1",

language = "English",

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TY - JOUR

T1 - Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome c

AU - Vodnyánszky, Lajos

AU - Marton, Attila

AU - Venekei, István

AU - Végh, Mikiós

AU - Blázovits, Anna

AU - Kittel, Ágnes

AU - Horváth, István

PY - 1985/7/9

Y1 - 1985/7/9

N2 - Heme-nonapeptide, derived from cytochrome c, inhibited both the NADPH- and NADH-dependent lipid peroxidation of brain microsomes but, in the case of liver microsomes, this inhibitory effect manifested itself in the presence of SKF-525A (a specific Mocker of cytochrome P-450) only. Heme-nonapeptide prevented the transient accumulation of lipid peroxides in microsomes during lipid peroxidation. The oxygen consumption of microsomes in the presence of NADPH or NADH was stimulated by heme-nonapeptide. From these results we concluded that, in vitro, there are two independent mechanisms of lipid peroxidation in liver microsomes. It is suggested that, in vivo, the heme-peptide-sensitive mechanism, observed in brain microsomes, is more important. © 1985.

AB - Heme-nonapeptide, derived from cytochrome c, inhibited both the NADPH- and NADH-dependent lipid peroxidation of brain microsomes but, in the case of liver microsomes, this inhibitory effect manifested itself in the presence of SKF-525A (a specific Mocker of cytochrome P-450) only. Heme-nonapeptide prevented the transient accumulation of lipid peroxides in microsomes during lipid peroxidation. The oxygen consumption of microsomes in the presence of NADPH or NADH was stimulated by heme-nonapeptide. From these results we concluded that, in vitro, there are two independent mechanisms of lipid peroxidation in liver microsomes. It is suggested that, in vivo, the heme-peptide-sensitive mechanism, observed in brain microsomes, is more important. © 1985.

KW - (Brain and liver microsome)

KW - Heme-nonapeptide inhibitor

KW - Lipid peroxidation

KW - SKF-525A

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U2 - 10.1016/0005-2760(85)90299-1

DO - 10.1016/0005-2760(85)90299-1

M3 - RGC 21 - Publication in refereed journal

C2 - 2988642

SN - 0005-2760

VL - 835

SP - 411

EP - 414

JO - Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism

JF - Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism

IS - 2

ER -

Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome c

Abstract

Research Keywords

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