Higher efficiency of the liver phosphorylative system in diabetic Goto-Kakizaki (GK) rats
Main Author: | |
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Publication Date: | 1999 |
Other Authors: | , , , , |
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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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 |
format |
article |
status_str |
publishedVersion |
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 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
aplication/PDF |
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Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
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