II - Insulin processing in mitochondria
- Autores
- Camberos, Maria del Carmen; Perez, Adriana A.; Passicot, Gisel Anabel; Martucci, Lucia Camila; Wanderley, Maria; Udrisar, Daniel P.; Cresto, Juan Carlos
- Año de publicación
- 2016
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Our objective was to know how insulin is processing in mitochondria; if IDE is the only participant in mitochondrial insulin degradation and the role of insulin degradation on IDE accumulation in mitoplasts. Mitochondria and its fractions were isolated as described by Greenwalt. IDE was purified and detected in immunoblot with specific antibodies. High insulin degradation was obtained through addition to rat’s diet of 25�g/rat of apple and 10�g/rat of hard-boiled eggs, 3�days a week. Mitochondrial insulin degradation was assayed with 5�% TCA, insulin antibody or Sephadex G50 chromatography. Degradation was also assayed 60�min at 37��C in mitochondrial fractions (IMS and Mx) with diet or not and without IDE. Degradation in fractions precipitated with ammonium sulfates (60–80�%) were studied after mitochondrial insulin incubation (1�ng. insulin during 15�min, at 30��C) or with addition of 2.5�mM ATP. Supplementary diet increased insulin degradation. High insulin did not increase mitoplasts accumulation and did not decrease mitochondrial degradation. High insulin and inhibition of degradation evidence insulin competition for a putative transport system. Mitochondrial incubation with insulin increased IDE in matrix as observed in immunoblot. ATP decreased degradation in Mx and increased it in IMS. Chromatography of IMS demonstrated an ATP-dependent protease that degraded insulin, similar to described by Sitte et al. Mitochondria participate in insulin degradation and the diet increased it. High insulin did not accomplish mitochondrial decrease of degradation or its accumulation in mitoplasts. Mitochondrial incubation with insulin increased IDE in matrix. ATP suggested being a regulator of mitochondrial insulin degradation.
Fil: Camberos, Maria del Carmen. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; Argentina
Fil: Perez, Adriana A.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Ecología, Genética y Evolución; Argentina
Fil: Passicot, Gisel Anabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; Argentina
Fil: Martucci, Lucia Camila. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; Argentina
Fil: Wanderley, Maria. Universidade Federal de Pernambuco; Brasil
Fil: Udrisar, Daniel P.. Universidade Federal de Pernambuco; Brasil
Fil: Cresto, Juan Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; Argentina - Materia
-
Atp-Dependent Protease
Chromatography Studies
Ide Insulin Degradation
Mitochondrial Fractions
Supplementary Diet - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/54152
Ver los metadatos del registro completo
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II - Insulin processing in mitochondriaCamberos, Maria del CarmenPerez, Adriana A.Passicot, Gisel AnabelMartucci, Lucia CamilaWanderley, MariaUdrisar, Daniel P.Cresto, Juan CarlosAtp-Dependent ProteaseChromatography StudiesIde Insulin DegradationMitochondrial FractionsSupplementary Diethttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Our objective was to know how insulin is processing in mitochondria; if IDE is the only participant in mitochondrial insulin degradation and the role of insulin degradation on IDE accumulation in mitoplasts. Mitochondria and its fractions were isolated as described by Greenwalt. IDE was purified and detected in immunoblot with specific antibodies. High insulin degradation was obtained through addition to rat’s diet of 25�g/rat of apple and 10�g/rat of hard-boiled eggs, 3�days a week. Mitochondrial insulin degradation was assayed with 5�% TCA, insulin antibody or Sephadex G50 chromatography. Degradation was also assayed 60�min at 37��C in mitochondrial fractions (IMS and Mx) with diet or not and without IDE. Degradation in fractions precipitated with ammonium sulfates (60–80�%) were studied after mitochondrial insulin incubation (1�ng. insulin during 15�min, at 30��C) or with addition of 2.5�mM ATP. Supplementary diet increased insulin degradation. High insulin did not increase mitoplasts accumulation and did not decrease mitochondrial degradation. High insulin and inhibition of degradation evidence insulin competition for a putative transport system. Mitochondrial incubation with insulin increased IDE in matrix as observed in immunoblot. ATP decreased degradation in Mx and increased it in IMS. Chromatography of IMS demonstrated an ATP-dependent protease that degraded insulin, similar to described by Sitte et al. Mitochondria participate in insulin degradation and the diet increased it. High insulin did not accomplish mitochondrial decrease of degradation or its accumulation in mitoplasts. Mitochondrial incubation with insulin increased IDE in matrix. ATP suggested being a regulator of mitochondrial insulin degradation.Fil: Camberos, Maria del Carmen. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; ArgentinaFil: Perez, Adriana A.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Ecología, Genética y Evolución; ArgentinaFil: Passicot, Gisel Anabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; ArgentinaFil: Martucci, Lucia Camila. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; ArgentinaFil: Wanderley, Maria. Universidade Federal de Pernambuco; BrasilFil: Udrisar, Daniel P.. Universidade Federal de Pernambuco; BrasilFil: Cresto, Juan Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; ArgentinaSpringer/Plenum Publishers2016-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/54152Camberos, Maria del Carmen; Perez, Adriana A.; Passicot, Gisel Anabel; Martucci, Lucia Camila; Wanderley, Maria; et al.; II - Insulin processing in mitochondria; Springer/Plenum Publishers; Journal of Bioenergetics and Biomembranes; 48; 5; 10-2016; 469-4820145-479XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s10863-016-9682-8info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10863-016-9682-8info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-29T11:50:54Zoai:ri.conicet.gov.ar:11336/54152instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-29 11:50:55.106CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
II - Insulin processing in mitochondria |
| title |
II - Insulin processing in mitochondria |
| spellingShingle |
II - Insulin processing in mitochondria Camberos, Maria del Carmen Atp-Dependent Protease Chromatography Studies Ide Insulin Degradation Mitochondrial Fractions Supplementary Diet |
| title_short |
II - Insulin processing in mitochondria |
| title_full |
II - Insulin processing in mitochondria |
| title_fullStr |
II - Insulin processing in mitochondria |
| title_full_unstemmed |
II - Insulin processing in mitochondria |
| title_sort |
II - Insulin processing in mitochondria |
| dc.creator.none.fl_str_mv |
Camberos, Maria del Carmen Perez, Adriana A. Passicot, Gisel Anabel Martucci, Lucia Camila Wanderley, Maria Udrisar, Daniel P. Cresto, Juan Carlos |
| author |
Camberos, Maria del Carmen |
| author_facet |
Camberos, Maria del Carmen Perez, Adriana A. Passicot, Gisel Anabel Martucci, Lucia Camila Wanderley, Maria Udrisar, Daniel P. Cresto, Juan Carlos |
| author_role |
author |
| author2 |
Perez, Adriana A. Passicot, Gisel Anabel Martucci, Lucia Camila Wanderley, Maria Udrisar, Daniel P. Cresto, Juan Carlos |
| author2_role |
author author author author author author |
| dc.subject.none.fl_str_mv |
Atp-Dependent Protease Chromatography Studies Ide Insulin Degradation Mitochondrial Fractions Supplementary Diet |
| topic |
Atp-Dependent Protease Chromatography Studies Ide Insulin Degradation Mitochondrial Fractions Supplementary Diet |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
Our objective was to know how insulin is processing in mitochondria; if IDE is the only participant in mitochondrial insulin degradation and the role of insulin degradation on IDE accumulation in mitoplasts. Mitochondria and its fractions were isolated as described by Greenwalt. IDE was purified and detected in immunoblot with specific antibodies. High insulin degradation was obtained through addition to rat’s diet of 25�g/rat of apple and 10�g/rat of hard-boiled eggs, 3�days a week. Mitochondrial insulin degradation was assayed with 5�% TCA, insulin antibody or Sephadex G50 chromatography. Degradation was also assayed 60�min at 37��C in mitochondrial fractions (IMS and Mx) with diet or not and without IDE. Degradation in fractions precipitated with ammonium sulfates (60–80�%) were studied after mitochondrial insulin incubation (1�ng. insulin during 15�min, at 30��C) or with addition of 2.5�mM ATP. Supplementary diet increased insulin degradation. High insulin did not increase mitoplasts accumulation and did not decrease mitochondrial degradation. High insulin and inhibition of degradation evidence insulin competition for a putative transport system. Mitochondrial incubation with insulin increased IDE in matrix as observed in immunoblot. ATP decreased degradation in Mx and increased it in IMS. Chromatography of IMS demonstrated an ATP-dependent protease that degraded insulin, similar to described by Sitte et al. Mitochondria participate in insulin degradation and the diet increased it. High insulin did not accomplish mitochondrial decrease of degradation or its accumulation in mitoplasts. Mitochondrial incubation with insulin increased IDE in matrix. ATP suggested being a regulator of mitochondrial insulin degradation. Fil: Camberos, Maria del Carmen. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; Argentina Fil: Perez, Adriana A.. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Ecología, Genética y Evolución; Argentina Fil: Passicot, Gisel Anabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; Argentina Fil: Martucci, Lucia Camila. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; Argentina Fil: Wanderley, Maria. Universidade Federal de Pernambuco; Brasil Fil: Udrisar, Daniel P.. Universidade Federal de Pernambuco; Brasil Fil: Cresto, Juan Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones Endocrinológicas ; Argentina |
| description |
Our objective was to know how insulin is processing in mitochondria; if IDE is the only participant in mitochondrial insulin degradation and the role of insulin degradation on IDE accumulation in mitoplasts. Mitochondria and its fractions were isolated as described by Greenwalt. IDE was purified and detected in immunoblot with specific antibodies. High insulin degradation was obtained through addition to rat’s diet of 25�g/rat of apple and 10�g/rat of hard-boiled eggs, 3�days a week. Mitochondrial insulin degradation was assayed with 5�% TCA, insulin antibody or Sephadex G50 chromatography. Degradation was also assayed 60�min at 37��C in mitochondrial fractions (IMS and Mx) with diet or not and without IDE. Degradation in fractions precipitated with ammonium sulfates (60–80�%) were studied after mitochondrial insulin incubation (1�ng. insulin during 15�min, at 30��C) or with addition of 2.5�mM ATP. Supplementary diet increased insulin degradation. High insulin did not increase mitoplasts accumulation and did not decrease mitochondrial degradation. High insulin and inhibition of degradation evidence insulin competition for a putative transport system. Mitochondrial incubation with insulin increased IDE in matrix as observed in immunoblot. ATP decreased degradation in Mx and increased it in IMS. Chromatography of IMS demonstrated an ATP-dependent protease that degraded insulin, similar to described by Sitte et al. Mitochondria participate in insulin degradation and the diet increased it. High insulin did not accomplish mitochondrial decrease of degradation or its accumulation in mitoplasts. Mitochondrial incubation with insulin increased IDE in matrix. ATP suggested being a regulator of mitochondrial insulin degradation. |
| publishDate |
2016 |
| dc.date.none.fl_str_mv |
2016-10 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/54152 Camberos, Maria del Carmen; Perez, Adriana A.; Passicot, Gisel Anabel; Martucci, Lucia Camila; Wanderley, Maria; et al.; II - Insulin processing in mitochondria; Springer/Plenum Publishers; Journal of Bioenergetics and Biomembranes; 48; 5; 10-2016; 469-482 0145-479X CONICET Digital CONICET |
| url |
http://hdl.handle.net/11336/54152 |
| identifier_str_mv |
Camberos, Maria del Carmen; Perez, Adriana A.; Passicot, Gisel Anabel; Martucci, Lucia Camila; Wanderley, Maria; et al.; II - Insulin processing in mitochondria; Springer/Plenum Publishers; Journal of Bioenergetics and Biomembranes; 48; 5; 10-2016; 469-482 0145-479X CONICET Digital CONICET |
| dc.language.none.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1007/s10863-016-9682-8 info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10863-016-9682-8 |
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openAccess |
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application/pdf application/pdf |
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Springer/Plenum Publishers |
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Springer/Plenum Publishers |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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