-
Je něco špatně v tomto záznamu ?
Idebenone-induced recovery of glycerol-3-phosphate and succinate oxidation inhibited by digitonin
H. Rauchová, M. Vokurková, Z. Drahota
Jazyk angličtina Země Česko
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Directory of Open Access Journals
od 1991
Free Medical Journals
od 1998
ProQuest Central
od 2005-01-01
Medline Complete (EBSCOhost)
od 2006-01-01
Nursing & Allied Health Database (ProQuest)
od 2005-01-01
Health & Medicine (ProQuest)
od 2005-01-01
ROAD: Directory of Open Access Scholarly Resources
od 1998
- MeSH
- cytochromy c metabolismus MeSH
- digitonin farmakologie MeSH
- glycerolfosfátdehydrogenasa metabolismus MeSH
- glycerolfosfáty metabolismus MeSH
- hypertyreóza metabolismus MeSH
- jaterní mitochondrie metabolismus účinky léků MeSH
- kinetika MeSH
- krysa rodu rattus MeSH
- kyselina jantarová metabolismus MeSH
- mitochondriální membrány metabolismus účinky léků MeSH
- modely nemocí na zvířatech MeSH
- obnova funkce MeSH
- oxidace-redukce MeSH
- potkani Wistar MeSH
- spotřeba kyslíku účinky léků MeSH
- sukcinátcytochrom c oxidoreduktasa metabolismus MeSH
- ubichinon analogy a deriváty metabolismus MeSH
- vztah mezi dávkou a účinkem léčiva MeSH
- zvířata MeSH
- Check Tag
- krysa rodu rattus MeSH
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Digitonin solubilizes mitochondrial membrane, breaks the integrity of the respiratory chain and releases two mobile redox-active components: coenzyme Q (CoQ) and cytochrome c (cyt c). In the present study we report the inhibition of glycerol-3-phosphate- and succinate-dependent oxygen consumption rates by digitonin treatment. Our results show that the inhibition of oxygen consumption rates is recovered by the addition of exogenous synthetic analog of CoQ idebenone (hydroxydecyl-ubiquinone; IDB) and cyt c. Glycerol-3-phosphate oxidation rate is recovered to 148 % of control values, whereas succinate-dependent oxidation rate only to 68 %. We find a similar effect on the activities of glycerol-3-phosphate and succinate cytochrome c oxidoreductase. Our results also indicate that succinate-dependent oxidation is less sensitive to digitonin treatment and less activated by IDB in comparison with glycerol-3-phosphate-dependent oxidation. These findings might indicate the different mechanism of the electron transfer from two flavoprotein-dependent dehydrogenases (glycerol-3-phosphate dehydrogenase and succinate dehydrogenase) localized on the outer and inner face of the inner mitochondrial membrane, respectively.
Center for Applied Genomics Prague Czech Republic
Centre for Cardiovascular Research Prague
Institute of Physiology Academy of Sciences of the Czech Republic Prague Czech Republic
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc12035271
- 003
- CZ-PrNML
- 005
- 20130122101441.0
- 007
- ta
- 008
- 121023s2012 xr d f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.33549/physiolres.932318 $2 doi
- 035 __
- $a (PubMed)22480420
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xr
- 100 1_
- $a Rauchová, Hana, $d 1950- $7 xx0074209 $u Institute of Physiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic; Centre for Cardiovascular Research, Prague
- 245 10
- $a Idebenone-induced recovery of glycerol-3-phosphate and succinate oxidation inhibited by digitonin / $c H. Rauchová, M. Vokurková, Z. Drahota
- 520 9_
- $a Digitonin solubilizes mitochondrial membrane, breaks the integrity of the respiratory chain and releases two mobile redox-active components: coenzyme Q (CoQ) and cytochrome c (cyt c). In the present study we report the inhibition of glycerol-3-phosphate- and succinate-dependent oxygen consumption rates by digitonin treatment. Our results show that the inhibition of oxygen consumption rates is recovered by the addition of exogenous synthetic analog of CoQ idebenone (hydroxydecyl-ubiquinone; IDB) and cyt c. Glycerol-3-phosphate oxidation rate is recovered to 148 % of control values, whereas succinate-dependent oxidation rate only to 68 %. We find a similar effect on the activities of glycerol-3-phosphate and succinate cytochrome c oxidoreductase. Our results also indicate that succinate-dependent oxidation is less sensitive to digitonin treatment and less activated by IDB in comparison with glycerol-3-phosphate-dependent oxidation. These findings might indicate the different mechanism of the electron transfer from two flavoprotein-dependent dehydrogenases (glycerol-3-phosphate dehydrogenase and succinate dehydrogenase) localized on the outer and inner face of the inner mitochondrial membrane, respectively.
- 650 _2
- $a zvířata $7 D000818
- 650 _2
- $a cytochromy c $x metabolismus $7 D045304
- 650 _2
- $a digitonin $x farmakologie $7 D004072
- 650 _2
- $a modely nemocí na zvířatech $7 D004195
- 650 _2
- $a vztah mezi dávkou a účinkem léčiva $7 D004305
- 650 _2
- $a glycerolfosfátdehydrogenasa $x metabolismus $7 D005993
- 650 _2
- $a glycerolfosfáty $x metabolismus $7 D005994
- 650 _2
- $a hypertyreóza $x metabolismus $7 D006980
- 650 _2
- $a kinetika $7 D007700
- 650 _2
- $a mužské pohlaví $7 D008297
- 650 _2
- $a jaterní mitochondrie $x metabolismus $x účinky léků $7 D008930
- 650 _2
- $a mitochondriální membrány $x metabolismus $x účinky léků $7 D051336
- 650 _2
- $a oxidace-redukce $7 D010084
- 650 _2
- $a spotřeba kyslíku $x účinky léků $7 D010101
- 650 _2
- $a potkani Wistar $7 D017208
- 650 _2
- $a obnova funkce $7 D020127
- 650 _2
- $a sukcinátcytochrom c oxidoreduktasa $x metabolismus $7 D013384
- 650 _2
- $a kyselina jantarová $x metabolismus $7 D019802
- 650 _2
- $a ubichinon $x analogy a deriváty $x metabolismus $7 D014451
- 650 _2
- $a krysa rodu Rattus $7 D051381
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Vokurková, Martina, $d 1973- $7 xx0037678 $u Institute of Physiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic; Centre for Cardiovascular Research, Prague
- 700 1_
- $a Drahota, Zdeněk, $d 1932- $7 jn20000400531 $u Institute of Physiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic; Center for Applied Genomics, Prague, Czech Republic
- 773 0_
- $w MED00003824 $t Physiological research $x 1802-9973 $g Roč. 61, č. 3 (2012), s. 259-265
- 856 41
- $u http://www.biomed.cas.cz/physiolres/archive.htm
- 910 __
- $a ABA008 $b A 4120 $c 266 $y 4
- 990 __
- $a 20121023 $b ABA008
- 991 __
- $a 20130122101559 $b ABA008
- 999 __
- $a ok $b bmc $g 960121 $s 792771
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2012 $b 61 $c 3 $d 259-265 $i 1802-9973 $m Physiological research $n Physiol. Res. (Print) $x MED00003824
- LZP __
- $a Pubmed-20121023-PhysRes1203BezM