Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) rats

Bibliographic Details
Main Author: Palmeira, Carlos M.
Publication Date: 1999
Other Authors: Ferreira, F. M. L., Santos, D. L., Ceiça, R., Suzuki, Ken-ichi, Santos, M. S.
Format: Article
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: https://hdl.handle.net/10316/5460
https://doi.org/10.1016/S0014-5793(99)01144-8
Summary: Liver mitochondrial bioenergetics of Goto-Kakizaki (GK) rats (a model of non-insulin dependent diabetes mellitus) reveals a [Delta][Psi] upon energization with succinate significantly increased relatively to control animals. The repolarization rate following ADP phosphorylation is also significantly increased in GK mitochondria in parallel with increased ATPase activity. The increase in the repolarization rate and ATPase activity is presumably related to an improved efficiency of F0F1-ATPase, either from a better phosphorylative energy coupling or as a consequence of an enlarged number of catalytic units. Titrations with oligomycin indicate that diabetic GK liver mitochondria require excess oligomycin pulses to completely abolish phosphorylation, relative to control mitochondria. Therefore, accepting that the number of operational ATP synthase units is inversely proportional to the amount of added oligomycin, it is concluded that liver mitochondria of diabetic GK rats are provided with extra catalytic units relative to control mitochondria of normal rats. Other tissues (kidney, brain and skeletal muscle) were evaluated for the same bioenergetic parameters, confirming that this feature is exclusive to liver from diabetic GK rats.
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spelling Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) ratsNon-insulin dependent diabetes mellitusMitochondrionOxidative phosphorylationGoto-Kakizaki ratLiver mitochondrial bioenergetics of Goto-Kakizaki (GK) rats (a model of non-insulin dependent diabetes mellitus) reveals a [Delta][Psi] upon energization with succinate significantly increased relatively to control animals. The repolarization rate following ADP phosphorylation is also significantly increased in GK mitochondria in parallel with increased ATPase activity. The increase in the repolarization rate and ATPase activity is presumably related to an improved efficiency of F0F1-ATPase, either from a better phosphorylative energy coupling or as a consequence of an enlarged number of catalytic units. Titrations with oligomycin indicate that diabetic GK liver mitochondria require excess oligomycin pulses to completely abolish phosphorylation, relative to control mitochondria. Therefore, accepting that the number of operational ATP synthase units is inversely proportional to the amount of added oligomycin, it is concluded that liver mitochondria of diabetic GK rats are provided with extra catalytic units relative to control mitochondria of normal rats. Other tissues (kidney, brain and skeletal muscle) were evaluated for the same bioenergetic parameters, confirming that this feature is exclusive to liver from diabetic GK rats.http://www.sciencedirect.com/science/article/B6T36-3XCF7ST-5/1/4b332e8be5488aa395f2b6473dc9a01a1999info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleaplication/PDFhttps://hdl.handle.net/10316/5460https://hdl.handle.net/10316/5460https://doi.org/10.1016/S0014-5793(99)01144-8engFEBS Letters. 458:2 (1999) 103-106Palmeira, Carlos M.Ferreira, F. M. L.Santos, D. L.Ceiça, R.Suzuki, Ken-ichiSantos, M. S.info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2021-10-07T10:32:20Zoai:estudogeral.uc.pt:10316/5460Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-29T05:14:29.345353Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
dc.title.none.fl_str_mv Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) rats
title Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) rats
spellingShingle Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) rats
Palmeira, Carlos M.
Non-insulin dependent diabetes mellitus
Mitochondrion
Oxidative phosphorylation
Goto-Kakizaki rat
title_short Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) rats
title_full Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) rats
title_fullStr Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) rats
title_full_unstemmed Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) rats
title_sort Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) rats
author Palmeira, Carlos M.
author_facet Palmeira, Carlos M.
Ferreira, F. M. L.
Santos, D. L.
Ceiça, R.
Suzuki, Ken-ichi
Santos, M. S.
author_role author
author2 Ferreira, F. M. L.
Santos, D. L.
Ceiça, R.
Suzuki, Ken-ichi
Santos, M. S.
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Palmeira, Carlos M.
Ferreira, F. M. L.
Santos, D. L.
Ceiça, R.
Suzuki, Ken-ichi
Santos, M. S.
dc.subject.por.fl_str_mv Non-insulin dependent diabetes mellitus
Mitochondrion
Oxidative phosphorylation
Goto-Kakizaki rat
topic Non-insulin dependent diabetes mellitus
Mitochondrion
Oxidative phosphorylation
Goto-Kakizaki rat
description Liver mitochondrial bioenergetics of Goto-Kakizaki (GK) rats (a model of non-insulin dependent diabetes mellitus) reveals a [Delta][Psi] upon energization with succinate significantly increased relatively to control animals. The repolarization rate following ADP phosphorylation is also significantly increased in GK mitochondria in parallel with increased ATPase activity. The increase in the repolarization rate and ATPase activity is presumably related to an improved efficiency of F0F1-ATPase, either from a better phosphorylative energy coupling or as a consequence of an enlarged number of catalytic units. Titrations with oligomycin indicate that diabetic GK liver mitochondria require excess oligomycin pulses to completely abolish phosphorylation, relative to control mitochondria. Therefore, accepting that the number of operational ATP synthase units is inversely proportional to the amount of added oligomycin, it is concluded that liver mitochondria of diabetic GK rats are provided with extra catalytic units relative to control mitochondria of normal rats. Other tissues (kidney, brain and skeletal muscle) were evaluated for the same bioenergetic parameters, confirming that this feature is exclusive to liver from diabetic GK rats.
publishDate 1999
dc.date.none.fl_str_mv 1999
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.uri.fl_str_mv https://hdl.handle.net/10316/5460
https://hdl.handle.net/10316/5460
https://doi.org/10.1016/S0014-5793(99)01144-8
url https://hdl.handle.net/10316/5460
https://doi.org/10.1016/S0014-5793(99)01144-8
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv FEBS Letters. 458:2 (1999) 103-106
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dc.format.none.fl_str_mv aplication/PDF
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