The proteasomes of two marine decapod crustaceans, European lobster (Homarus gammarus) and Edible crab (Cancer pagurus), are differently impaired by heavy metals

The intracellular ubiquitin-proteasome system is a key regulator of cellular processes involved in the controlled degradation of short-living or malfunctioning proteins. Certain diseases and cellular dysfunctions are known to arise from the disruption of proteasome pathways. Trace metals are recogni...

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Published in:Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology
Main Authors: Götze, Sandra, Bose, Aneesh, Skolova, Inna M., Abele, Doris, Saborowski, Reinhard
Format: Article in Journal/Newspaper
Language:unknown
Published: ELSEVIER SCIENCE INC 2014
Subjects:
Online Access:https://epic.awi.de/id/eprint/35454/
https://epic.awi.de/id/eprint/35454/1/Goetzeetal2014b.pdf
https://hdl.handle.net/10013/epic.43434
https://hdl.handle.net/10013/epic.43434.d001
id ftawi:oai:epic.awi.de:35454
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spelling ftawi:oai:epic.awi.de:35454 2023-05-15T16:08:49+02:00 The proteasomes of two marine decapod crustaceans, European lobster (Homarus gammarus) and Edible crab (Cancer pagurus), are differently impaired by heavy metals Götze, Sandra Bose, Aneesh Skolova, Inna M. Abele, Doris Saborowski, Reinhard 2014-05 application/pdf https://epic.awi.de/id/eprint/35454/ https://epic.awi.de/id/eprint/35454/1/Goetzeetal2014b.pdf https://hdl.handle.net/10013/epic.43434 https://hdl.handle.net/10013/epic.43434.d001 unknown ELSEVIER SCIENCE INC https://epic.awi.de/id/eprint/35454/1/Goetzeetal2014b.pdf https://hdl.handle.net/10013/epic.43434.d001 Götze, S. , Bose, A. , Skolova, I. M. , Abele, D. orcid:0000-0002-5766-5017 and Saborowski, R. orcid:0000-0003-0289-6501 (2014) The proteasomes of two marine decapod crustaceans, European lobster (Homarus gammarus) and Edible crab (Cancer pagurus), are differently impaired by heavy metals , Comparative Biochemistry and Physiology C-Toxicology & Pharmacology, 162 , pp. 62-69 . doi:10.1016/j.cbpc.2014.03.012 <https://doi.org/10.1016/j.cbpc.2014.03.012> , hdl:10013/epic.43434 EPIC3Comparative Biochemistry and Physiology C-Toxicology & Pharmacology, ELSEVIER SCIENCE INC, 162, pp. 62-69, ISSN: 1532-0456 Article isiRev 2014 ftawi 2021-12-24T15:39:29Z The intracellular ubiquitin-proteasome system is a key regulator of cellular processes involved in the controlled degradation of short-living or malfunctioning proteins. Certain diseases and cellular dysfunctions are known to arise from the disruption of proteasome pathways. Trace metals are recognized stressors of the proteasome system in vertebrates and plants, but their effects on the proteasome of invertebrates are not well understood. Since marine invertebrates, and particularly benthic crustaceans, can be exposed to high metal levels, we studied the effects of in vitro exposure to Hg2 +, Zn2 +, Cu2 +, and Cd2 + on the activities of the proteasome from the claw muscles of lobsters (Homarus gammarus) and crabs (Cancer pagurus). The chymotrypsin like activity of the proteasome of these two species showed different sensitivity to metals. In lobsters the activity was significantly inhibited by all metals to a similar extent. In crabs the activities were severely suppressed only by Hg2 + and Cu2 + while Zn2 + had only a moderate effect and Cd2 + caused almost no inhibition of the crab proteasome. This indicates that the proteasomes of both species possess structural characteristics that determine different susceptibility to metals. Consequently, the proteasome-mediated protein degradation in crab C. pagurus may be less affected by metal pollution than that of the lobster H. gammarus. Article in Journal/Newspaper European lobster Homarus gammarus Alfred Wegener Institute for Polar- and Marine Research (AWI): ePIC (electronic Publication Information Center) Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 162 62 69
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 The intracellular ubiquitin-proteasome system is a key regulator of cellular processes involved in the controlled degradation of short-living or malfunctioning proteins. Certain diseases and cellular dysfunctions are known to arise from the disruption of proteasome pathways. Trace metals are recognized stressors of the proteasome system in vertebrates and plants, but their effects on the proteasome of invertebrates are not well understood. Since marine invertebrates, and particularly benthic crustaceans, can be exposed to high metal levels, we studied the effects of in vitro exposure to Hg2 +, Zn2 +, Cu2 +, and Cd2 + on the activities of the proteasome from the claw muscles of lobsters (Homarus gammarus) and crabs (Cancer pagurus). The chymotrypsin like activity of the proteasome of these two species showed different sensitivity to metals. In lobsters the activity was significantly inhibited by all metals to a similar extent. In crabs the activities were severely suppressed only by Hg2 + and Cu2 + while Zn2 + had only a moderate effect and Cd2 + caused almost no inhibition of the crab proteasome. This indicates that the proteasomes of both species possess structural characteristics that determine different susceptibility to metals. Consequently, the proteasome-mediated protein degradation in crab C. pagurus may be less affected by metal pollution than that of the lobster H. gammarus.
format Article in Journal/Newspaper
author Götze, Sandra
Bose, Aneesh
Skolova, Inna M.
Abele, Doris
Saborowski, Reinhard
spellingShingle Götze, Sandra
Bose, Aneesh
Skolova, Inna M.
Abele, Doris
Saborowski, Reinhard
The proteasomes of two marine decapod crustaceans, European lobster (Homarus gammarus) and Edible crab (Cancer pagurus), are differently impaired by heavy metals
author_facet Götze, Sandra
Bose, Aneesh
Skolova, Inna M.
Abele, Doris
Saborowski, Reinhard
author_sort Götze, Sandra
title The proteasomes of two marine decapod crustaceans, European lobster (Homarus gammarus) and Edible crab (Cancer pagurus), are differently impaired by heavy metals
title_short The proteasomes of two marine decapod crustaceans, European lobster (Homarus gammarus) and Edible crab (Cancer pagurus), are differently impaired by heavy metals
title_full The proteasomes of two marine decapod crustaceans, European lobster (Homarus gammarus) and Edible crab (Cancer pagurus), are differently impaired by heavy metals
title_fullStr The proteasomes of two marine decapod crustaceans, European lobster (Homarus gammarus) and Edible crab (Cancer pagurus), are differently impaired by heavy metals
title_full_unstemmed The proteasomes of two marine decapod crustaceans, European lobster (Homarus gammarus) and Edible crab (Cancer pagurus), are differently impaired by heavy metals
title_sort proteasomes of two marine decapod crustaceans, european lobster (homarus gammarus) and edible crab (cancer pagurus), are differently impaired by heavy metals
publisher ELSEVIER SCIENCE INC
publishDate 2014
url https://epic.awi.de/id/eprint/35454/
https://epic.awi.de/id/eprint/35454/1/Goetzeetal2014b.pdf
https://hdl.handle.net/10013/epic.43434
https://hdl.handle.net/10013/epic.43434.d001
genre European lobster
Homarus gammarus
genre_facet European lobster
Homarus gammarus
op_source EPIC3Comparative Biochemistry and Physiology C-Toxicology & Pharmacology, ELSEVIER SCIENCE INC, 162, pp. 62-69, ISSN: 1532-0456
op_relation https://epic.awi.de/id/eprint/35454/1/Goetzeetal2014b.pdf
https://hdl.handle.net/10013/epic.43434.d001
Götze, S. , Bose, A. , Skolova, I. M. , Abele, D. orcid:0000-0002-5766-5017 and Saborowski, R. orcid:0000-0003-0289-6501 (2014) The proteasomes of two marine decapod crustaceans, European lobster (Homarus gammarus) and Edible crab (Cancer pagurus), are differently impaired by heavy metals , Comparative Biochemistry and Physiology C-Toxicology & Pharmacology, 162 , pp. 62-69 . doi:10.1016/j.cbpc.2014.03.012 <https://doi.org/10.1016/j.cbpc.2014.03.012> , hdl:10013/epic.43434
container_title Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology
container_volume 162
container_start_page 62
op_container_end_page 69
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