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Uncoupling Protein 1 of Brown Adipocytes, the Only Uncoupler: A Historical Perspective

Uncoupling protein 1 (UCP1), is a unique mitochondrial membranous protein devoted to adaptive thermogenesis, a specialized function performed by brown adipocytes. Whereas the family of mitochondrial metabolite carriers comprises ∼40 members, UCP1 is the only memberable to translocate protons through...

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Detalles Bibliográficos
Autor principal: Ricquier, Daniel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Research Foundation 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3355862/
https://www.ncbi.nlm.nih.gov/pubmed/22649389
http://dx.doi.org/10.3389/fendo.2011.00085
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author Ricquier, Daniel
author_facet Ricquier, Daniel
author_sort Ricquier, Daniel
collection PubMed
description Uncoupling protein 1 (UCP1), is a unique mitochondrial membranous protein devoted to adaptive thermogenesis, a specialized function performed by brown adipocytes. Whereas the family of mitochondrial metabolite carriers comprises ∼40 members, UCP1 is the only memberable to translocate protons through the inner membrane of brown adipocyte mitochondria. By this process, UCP1 uncouples respiration from ATP synthesis and therefore provokes energy dissipation in the form of heat while, also stimulating high levels of fatty acid oxidation. UCP1 homologs were identified but they are biochemically and physiologically different from UCP1. Thirty five years after its identification, UCP1 still appears as a fascinating component. The recent renewal of the interest in human brown adipose tissue makes UCP1 as a potential target for strategies of treatment of metabolic disorders.
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spelling pubmed-33558622012-05-30 Uncoupling Protein 1 of Brown Adipocytes, the Only Uncoupler: A Historical Perspective Ricquier, Daniel Front Endocrinol (Lausanne) Endocrinology Uncoupling protein 1 (UCP1), is a unique mitochondrial membranous protein devoted to adaptive thermogenesis, a specialized function performed by brown adipocytes. Whereas the family of mitochondrial metabolite carriers comprises ∼40 members, UCP1 is the only memberable to translocate protons through the inner membrane of brown adipocyte mitochondria. By this process, UCP1 uncouples respiration from ATP synthesis and therefore provokes energy dissipation in the form of heat while, also stimulating high levels of fatty acid oxidation. UCP1 homologs were identified but they are biochemically and physiologically different from UCP1. Thirty five years after its identification, UCP1 still appears as a fascinating component. The recent renewal of the interest in human brown adipose tissue makes UCP1 as a potential target for strategies of treatment of metabolic disorders. Frontiers Research Foundation 2011-12-28 /pmc/articles/PMC3355862/ /pubmed/22649389 http://dx.doi.org/10.3389/fendo.2011.00085 Text en Copyright © 2011 Ricquier. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution Non Commercial License, which permits non-commercial use, distribution, and reproduction in other forums, provided the original authors and source are credited.
spellingShingle Endocrinology
Ricquier, Daniel
Uncoupling Protein 1 of Brown Adipocytes, the Only Uncoupler: A Historical Perspective
title Uncoupling Protein 1 of Brown Adipocytes, the Only Uncoupler: A Historical Perspective
title_full Uncoupling Protein 1 of Brown Adipocytes, the Only Uncoupler: A Historical Perspective
title_fullStr Uncoupling Protein 1 of Brown Adipocytes, the Only Uncoupler: A Historical Perspective
title_full_unstemmed Uncoupling Protein 1 of Brown Adipocytes, the Only Uncoupler: A Historical Perspective
title_short Uncoupling Protein 1 of Brown Adipocytes, the Only Uncoupler: A Historical Perspective
title_sort uncoupling protein 1 of brown adipocytes, the only uncoupler: a historical perspective
topic Endocrinology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3355862/
https://www.ncbi.nlm.nih.gov/pubmed/22649389
http://dx.doi.org/10.3389/fendo.2011.00085
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