Thermal sensitivity of uncoupling proteins in polar and temperate fish

Uncoupling proteins (UCP), capable of increasing proton leakage across the inner mitochondrial membrane, may play a role in the temperature dependent setting of energy turnover in animals (and their mitochondria). Therefore, the genes and expression of fish UCP were investigated in the Antarctic eel...

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Published in:Comparative Biochemistry and Physiology Part D: Genomics and Proteomics
Main Authors: Mark, Felix Christopher, Lucassen, Magnus, Pörtner, Hans-Otto
Format: Article in Journal/Newspaper
Language:unknown
Published: 2006
Subjects:
Online Access:https://epic.awi.de/id/eprint/12010/
https://epic.awi.de/id/eprint/12010/1/Mar2004d.pdf
https://doi.org/10.1016/j.cbd.2006.08.004
https://hdl.handle.net/10013/epic.22446
https://hdl.handle.net/10013/epic.22446.d001
id ftawi:oai:epic.awi.de:12010
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spelling ftawi:oai:epic.awi.de:12010 2023-09-05T13:13:19+02:00 Thermal sensitivity of uncoupling proteins in polar and temperate fish Mark, Felix Christopher Lucassen, Magnus Pörtner, Hans-Otto 2006 application/pdf https://epic.awi.de/id/eprint/12010/ https://epic.awi.de/id/eprint/12010/1/Mar2004d.pdf https://doi.org/10.1016/j.cbd.2006.08.004 https://hdl.handle.net/10013/epic.22446 https://hdl.handle.net/10013/epic.22446.d001 unknown https://epic.awi.de/id/eprint/12010/1/Mar2004d.pdf https://hdl.handle.net/10013/epic.22446.d001 Mark, F. C. orcid:0000-0002-5586-6704 , Lucassen, M. orcid:0000-0003-4276-4781 and Pörtner, H. O. orcid:0000-0001-6535-6575 (2006) Thermal sensitivity of uncoupling proteins in polar and temperate fish , Comparative biochemistry and physiology d-genomics & proteomics, D1(3)374, 365 . doi:10.1016/j.cbd.2006.08.004 <https://doi.org/10.1016/j.cbd.2006.08.004> , hdl:10013/epic.22446 EPIC3Comparative biochemistry and physiology d-genomics & proteomics, D1(3)374, 365 Article isiRev 2006 ftawi https://doi.org/10.1016/j.cbd.2006.08.004 2023-08-22T19:49:40Z Uncoupling proteins (UCP), capable of increasing proton leakage across the inner mitochondrial membrane, may play a role in the temperature dependent setting of energy turnover in animals (and their mitochondria). Therefore, the genes and expression of fish UCP were investigated in the Antarctic eelpout Pachycara brachycephalum and a temperate confamilial species, the common eelpout Zoarces viviparus. UCP full-length cDNA was amplified from liver and muscle using RT-PCR and rapid amplification of cDNA ends (RACE). The fish UCP mRNA consists of 1906bp in P. brachycephalum and of 1876bp in Z. viviparus. Both zoarcid sequences contain open reading frames of 939bp, encoding 313 amino acids, with 98 and 99% identity, respectively. Protein sequences of zoarcid UCP are closest related to fish and mammalian UCP2. For analysis of temperature dependent expression common eelpouts were cold-acclimated from 10°C to 2°C and Antarctic eelpouts were warm-acclimated from 0°C to 5°C. Identical cDNA probes for both species were developed to investigate fish UCP mRNA expression, and protein expression levels were detected by Western Blot in the enriched membrane fraction. During cold-acclimation in Z. viviparus, mRNA levels increased by a factor up to 2.0, protein levels increased up to 1.5, in line with mitochondrial proliferation during cold-acclimation. Despite decreased mitochondrial protein content, in Antarctic eelpout UCP levels rose upon warm acclimation by a factor up to 2.0 (mRNA) and 1.6 (protein), respectively. Besides the ongoing discussion of UCP function in vertebrates, the data are indicative of a significant role of fish UCP in thermal adaptation of fish mitochondria. Article in Journal/Newspaper Antarc* Antarctic Alfred Wegener Institute for Polar- and Marine Research (AWI): ePIC (electronic Publication Information Center) Antarctic The Antarctic Comparative Biochemistry and Physiology Part D: Genomics and Proteomics 1 3 365 374
institution Open Polar
collection Alfred Wegener Institute for Polar- and Marine Research (AWI): ePIC (electronic Publication Information Center)
op_collection_id ftawi
language unknown
description Uncoupling proteins (UCP), capable of increasing proton leakage across the inner mitochondrial membrane, may play a role in the temperature dependent setting of energy turnover in animals (and their mitochondria). Therefore, the genes and expression of fish UCP were investigated in the Antarctic eelpout Pachycara brachycephalum and a temperate confamilial species, the common eelpout Zoarces viviparus. UCP full-length cDNA was amplified from liver and muscle using RT-PCR and rapid amplification of cDNA ends (RACE). The fish UCP mRNA consists of 1906bp in P. brachycephalum and of 1876bp in Z. viviparus. Both zoarcid sequences contain open reading frames of 939bp, encoding 313 amino acids, with 98 and 99% identity, respectively. Protein sequences of zoarcid UCP are closest related to fish and mammalian UCP2. For analysis of temperature dependent expression common eelpouts were cold-acclimated from 10°C to 2°C and Antarctic eelpouts were warm-acclimated from 0°C to 5°C. Identical cDNA probes for both species were developed to investigate fish UCP mRNA expression, and protein expression levels were detected by Western Blot in the enriched membrane fraction. During cold-acclimation in Z. viviparus, mRNA levels increased by a factor up to 2.0, protein levels increased up to 1.5, in line with mitochondrial proliferation during cold-acclimation. Despite decreased mitochondrial protein content, in Antarctic eelpout UCP levels rose upon warm acclimation by a factor up to 2.0 (mRNA) and 1.6 (protein), respectively. Besides the ongoing discussion of UCP function in vertebrates, the data are indicative of a significant role of fish UCP in thermal adaptation of fish mitochondria.
format Article in Journal/Newspaper
author Mark, Felix Christopher
Lucassen, Magnus
Pörtner, Hans-Otto
spellingShingle Mark, Felix Christopher
Lucassen, Magnus
Pörtner, Hans-Otto
Thermal sensitivity of uncoupling proteins in polar and temperate fish
author_facet Mark, Felix Christopher
Lucassen, Magnus
Pörtner, Hans-Otto
author_sort Mark, Felix Christopher
title Thermal sensitivity of uncoupling proteins in polar and temperate fish
title_short Thermal sensitivity of uncoupling proteins in polar and temperate fish
title_full Thermal sensitivity of uncoupling proteins in polar and temperate fish
title_fullStr Thermal sensitivity of uncoupling proteins in polar and temperate fish
title_full_unstemmed Thermal sensitivity of uncoupling proteins in polar and temperate fish
title_sort thermal sensitivity of uncoupling proteins in polar and temperate fish
publishDate 2006
url https://epic.awi.de/id/eprint/12010/
https://epic.awi.de/id/eprint/12010/1/Mar2004d.pdf
https://doi.org/10.1016/j.cbd.2006.08.004
https://hdl.handle.net/10013/epic.22446
https://hdl.handle.net/10013/epic.22446.d001
geographic Antarctic
The Antarctic
geographic_facet Antarctic
The Antarctic
genre Antarc*
Antarctic
genre_facet Antarc*
Antarctic
op_source EPIC3Comparative biochemistry and physiology d-genomics & proteomics, D1(3)374, 365
op_relation https://epic.awi.de/id/eprint/12010/1/Mar2004d.pdf
https://hdl.handle.net/10013/epic.22446.d001
Mark, F. C. orcid:0000-0002-5586-6704 , Lucassen, M. orcid:0000-0003-4276-4781 and Pörtner, H. O. orcid:0000-0001-6535-6575 (2006) Thermal sensitivity of uncoupling proteins in polar and temperate fish , Comparative biochemistry and physiology d-genomics & proteomics, D1(3)374, 365 . doi:10.1016/j.cbd.2006.08.004 <https://doi.org/10.1016/j.cbd.2006.08.004> , hdl:10013/epic.22446
op_doi https://doi.org/10.1016/j.cbd.2006.08.004
container_title Comparative Biochemistry and Physiology Part D: Genomics and Proteomics
container_volume 1
container_issue 3
container_start_page 365
op_container_end_page 374
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