1 resultado para Duodenal switch
em Brock University, Canada
Filtro por publicador
- JISC Information Environment Repository (1)
- University of Cagliari UniCA Eprints (1)
- Aberdeen University (2)
- Abertay Research Collections - Abertay University’s repository (1)
- Aberystwyth University Repository - Reino Unido (1)
- AMS Tesi di Laurea - Alm@DL - Università di Bologna (1)
- Applied Math and Science Education Repository - Washington - USA (1)
- Aquatic Commons (8)
- Archive of European Integration (2)
- Archivo Digital para la Docencia y la Investigación - Repositorio Institucional de la Universidad del País Vasco (3)
- Aston University Research Archive (6)
- B-Digital - Universidade Fernando Pessoa - Portugal (1)
- Biblioteca de Teses e Dissertações da USP (1)
- Biblioteca Digital da Câmara dos Deputados (1)
- Biblioteca Digital da Produção Intelectual da Universidade de São Paulo (5)
- Biblioteca Digital da Produção Intelectual da Universidade de São Paulo (BDPI/USP) (2)
- Biblioteca Digital de la Universidad Católica Argentina (1)
- Biblioteca Digital de Teses e Dissertações Eletrônicas da UERJ (11)
- Bioline International (2)
- BORIS: Bern Open Repository and Information System - Berna - Suiça (42)
- Boston University Digital Common (6)
- Brock University, Canada (1)
- CaltechTHESIS (3)
- Cambridge University Engineering Department Publications Database (167)
- CentAUR: Central Archive University of Reading - UK (8)
- Chinese Academy of Sciences Institutional Repositories Grid Portal (181)
- Cochin University of Science & Technology (CUSAT), India (1)
- CORA - Cork Open Research Archive - University College Cork - Ireland (9)
- Dalarna University College Electronic Archive (5)
- Deakin Research Online - Australia (37)
- DI-fusion - The institutional repository of Université Libre de Bruxelles (6)
- Digital Commons at Florida International University (5)
- DigitalCommons@The Texas Medical Center (4)
- DigitalCommons@University of Nebraska - Lincoln (1)
- DRUM (Digital Repository at the University of Maryland) (1)
- Duke University (19)
- eResearch Archive - Queensland Department of Agriculture; Fisheries and Forestry (5)
- FUNDAJ - Fundação Joaquim Nabuco (1)
- Greenwich Academic Literature Archive - UK (4)
- Helda - Digital Repository of University of Helsinki (24)
- Indian Institute of Science - Bangalore - Índia (111)
- INSTITUTO DE PESQUISAS ENERGÉTICAS E NUCLEARES (IPEN) - Repositório Digital da Produção Técnico Científica - BibliotecaTerezine Arantes Ferra (1)
- Instituto Gulbenkian de Ciência (1)
- Lume - Repositório Digital da Universidade Federal do Rio Grande do Sul (1)
- Massachusetts Institute of Technology (3)
- National Center for Biotechnology Information - NCBI (37)
- Plymouth Marine Science Electronic Archive (PlyMSEA) (8)
- QSpace: Queen's University - Canada (2)
- QUB Research Portal - Research Directory and Institutional Repository for Queen's University Belfast (38)
- Queensland University of Technology - ePrints Archive (122)
- Repositório Institucional da Universidade de Aveiro - Portugal (1)
- Repositório Institucional da Universidade Federal do Rio Grande do Norte (2)
- Repositório Institucional UNESP - Universidade Estadual Paulista "Julio de Mesquita Filho" (20)
- Scielo España (2)
- Scientific Open-access Literature Archive and Repository (3)
- Universidad del Rosario, Colombia (4)
- Universidad Politécnica de Madrid (2)
- Universidade Federal do Rio Grande do Norte (UFRN) (5)
- Universitätsbibliothek Kassel, Universität Kassel, Germany (1)
- Université de Lausanne, Switzerland (7)
- Université de Montréal, Canada (2)
- University of Michigan (8)
- University of Queensland eSpace - Australia (10)
- University of Washington (1)
- WestminsterResearch - UK (1)
Resumo:
The first and rate-limiting step of lipolysis is the removal of the first fatty acid from a triglyceride molecule; it is catalyzed by adipose triglyceride lipase (ATGL). ATGL is co-activated by comparative gene identification-58 (CGI-58) and inhibited by the G(0)/G(1) switch gene-2 protein (G0S2). G0S2 has also recently been identified as a positive regulator of oxidative phosphorylation within the mitochondria. Previous research has demonstrated in cell culture, a dose dependent mechanism for inhibition by G0S2 on ATGL. However our data is not consistent with this hypothesis. There was no change in G0S2 protein content during an acute lipolytic inducing set of contractions in both whole muscle, and isolated mitochondria yet both ATGL and G0S2 increase following endurance training, in spite of the fact that there should be increased reliance on intramuscular lipolysis. Therefore, inhibition of ATGL by G0S2 appears to be regulated through more complicated intracellular or post-translation regulation.