First evidence of laccase activity in the Pacific oyster Crassostrea gigas
International audience Phenoloxidases (POs) are a family of enzymes including tyrosinases, catecholases and laccases, which play an important role in immune defence mechanisms in various invertebrates. The aim of this study was to thoroughly identify the PO-like activity present in the hemolymph of...
Published in: | Fish & Shellfish Immunology |
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ftunivrochelle:oai:HAL:hal-00477727v2 2024-02-11T10:03:10+01:00 First evidence of laccase activity in the Pacific oyster Crassostrea gigas Luna Acosta, Andrea Rosenfeld, Eric Amari, Myriam Fruitier-Arnaudin, Ingrid Bustamante, Paco Thomas-Guyon, Hélène LIttoral ENvironnement et Sociétés (LIENSs) La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) Département de la Charente-Maritime 2010-04-01 https://hal.science/hal-00477727 https://hal.science/hal-00477727v2/document https://hal.science/hal-00477727v2/file/Luna_Acosta_et_al_2010_FSIM.pdf https://doi.org/10.1016/j.fsi.2010.01.008 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fsi.2010.01.008 hal-00477727 https://hal.science/hal-00477727 https://hal.science/hal-00477727v2/document https://hal.science/hal-00477727v2/file/Luna_Acosta_et_al_2010_FSIM.pdf doi:10.1016/j.fsi.2010.01.008 info:eu-repo/semantics/OpenAccess ISSN: 1050-4648 EISSN: 1095-9947 Fish and Shellfish Immunology https://hal.science/hal-00477727 Fish and Shellfish Immunology, 2010, 28 (4), pp.719-726. ⟨10.1016/j.fsi.2010.01.008⟩ phenoloxidase catecholase melanin mollusc bivalve hemolymph hemocyte plasma [SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology info:eu-repo/semantics/article Journal articles 2010 ftunivrochelle https://doi.org/10.1016/j.fsi.2010.01.008 2024-01-23T23:33:59Z International audience Phenoloxidases (POs) are a family of enzymes including tyrosinases, catecholases and laccases, which play an important role in immune defence mechanisms in various invertebrates. The aim of this study was to thoroughly identify the PO-like activity present in the hemolymph of the Pacific oyster Crassostrea gigas, by using different substrates (i.e. dopamine and p-phenylenediamine, PPD) and different PO inhibitors. In order to go deeper in this analysis, we considered separately plasma and hemocyte lysate supernatant (HLS). In crude plasma, oxygraphic assays confirmed the presence of true oxidase activities. Moreover, the involvement of peroxidase(s) was excluded. In contrast to other molluscs, no tyrosinase-like activity was detected. With dopamine as substrate, PO-like activity was inhibited by the PO inhibitors tropolone, phenylthiourea (PTU), salicylhydroxamic acid and diethyldithio-carbamic acid, by a specific inhibitor of tyrosinases and catecholases, i.e. 4-hexylresorcinol (4-HR), and by a specific inhibitor of laccases, i.e. cetyltrimethylammonium bromide (CTAB). With PPD as substrate, PO-like activity was inhibited by PTU and CTAB. In precipitated protein fractions from plasma, and with dopamine and PPD as substrates, PTU and 4-HR, and PTU and CTAB inhibited PO-like activity, respectively. In precipitated protein fractions from hemocyte lysate supernatant, PTU and CTAB inhibited PO-like activity, independently of the substrate. Taken together, these results suggest the presence of both catecholase- and laccase-like activities in plasma, and the presence of a laccase-like activity in HLS. To the best of our knowledge, this is the first time that a laccase-like activity is identified in a mollusc by using specific substrates and inhibitors for laccase, opening new perspectives for studying the implication of this enzyme in immune defence mechanisms of molluscs of high economic value such as C. gigas. Article in Journal/Newspaper Crassostrea gigas Pacific oyster HAL - Université de La Rochelle Pacific Fish & Shellfish Immunology 28 4 719 726 |
institution |
Open Polar |
collection |
HAL - Université de La Rochelle |
op_collection_id |
ftunivrochelle |
language |
English |
topic |
phenoloxidase catecholase melanin mollusc bivalve hemolymph hemocyte plasma [SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology |
spellingShingle |
phenoloxidase catecholase melanin mollusc bivalve hemolymph hemocyte plasma [SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology Luna Acosta, Andrea Rosenfeld, Eric Amari, Myriam Fruitier-Arnaudin, Ingrid Bustamante, Paco Thomas-Guyon, Hélène First evidence of laccase activity in the Pacific oyster Crassostrea gigas |
topic_facet |
phenoloxidase catecholase melanin mollusc bivalve hemolymph hemocyte plasma [SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology |
description |
International audience Phenoloxidases (POs) are a family of enzymes including tyrosinases, catecholases and laccases, which play an important role in immune defence mechanisms in various invertebrates. The aim of this study was to thoroughly identify the PO-like activity present in the hemolymph of the Pacific oyster Crassostrea gigas, by using different substrates (i.e. dopamine and p-phenylenediamine, PPD) and different PO inhibitors. In order to go deeper in this analysis, we considered separately plasma and hemocyte lysate supernatant (HLS). In crude plasma, oxygraphic assays confirmed the presence of true oxidase activities. Moreover, the involvement of peroxidase(s) was excluded. In contrast to other molluscs, no tyrosinase-like activity was detected. With dopamine as substrate, PO-like activity was inhibited by the PO inhibitors tropolone, phenylthiourea (PTU), salicylhydroxamic acid and diethyldithio-carbamic acid, by a specific inhibitor of tyrosinases and catecholases, i.e. 4-hexylresorcinol (4-HR), and by a specific inhibitor of laccases, i.e. cetyltrimethylammonium bromide (CTAB). With PPD as substrate, PO-like activity was inhibited by PTU and CTAB. In precipitated protein fractions from plasma, and with dopamine and PPD as substrates, PTU and 4-HR, and PTU and CTAB inhibited PO-like activity, respectively. In precipitated protein fractions from hemocyte lysate supernatant, PTU and CTAB inhibited PO-like activity, independently of the substrate. Taken together, these results suggest the presence of both catecholase- and laccase-like activities in plasma, and the presence of a laccase-like activity in HLS. To the best of our knowledge, this is the first time that a laccase-like activity is identified in a mollusc by using specific substrates and inhibitors for laccase, opening new perspectives for studying the implication of this enzyme in immune defence mechanisms of molluscs of high economic value such as C. gigas. |
author2 |
LIttoral ENvironnement et Sociétés (LIENSs) La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) Département de la Charente-Maritime |
format |
Article in Journal/Newspaper |
author |
Luna Acosta, Andrea Rosenfeld, Eric Amari, Myriam Fruitier-Arnaudin, Ingrid Bustamante, Paco Thomas-Guyon, Hélène |
author_facet |
Luna Acosta, Andrea Rosenfeld, Eric Amari, Myriam Fruitier-Arnaudin, Ingrid Bustamante, Paco Thomas-Guyon, Hélène |
author_sort |
Luna Acosta, Andrea |
title |
First evidence of laccase activity in the Pacific oyster Crassostrea gigas |
title_short |
First evidence of laccase activity in the Pacific oyster Crassostrea gigas |
title_full |
First evidence of laccase activity in the Pacific oyster Crassostrea gigas |
title_fullStr |
First evidence of laccase activity in the Pacific oyster Crassostrea gigas |
title_full_unstemmed |
First evidence of laccase activity in the Pacific oyster Crassostrea gigas |
title_sort |
first evidence of laccase activity in the pacific oyster crassostrea gigas |
publisher |
HAL CCSD |
publishDate |
2010 |
url |
https://hal.science/hal-00477727 https://hal.science/hal-00477727v2/document https://hal.science/hal-00477727v2/file/Luna_Acosta_et_al_2010_FSIM.pdf https://doi.org/10.1016/j.fsi.2010.01.008 |
geographic |
Pacific |
geographic_facet |
Pacific |
genre |
Crassostrea gigas Pacific oyster |
genre_facet |
Crassostrea gigas Pacific oyster |
op_source |
ISSN: 1050-4648 EISSN: 1095-9947 Fish and Shellfish Immunology https://hal.science/hal-00477727 Fish and Shellfish Immunology, 2010, 28 (4), pp.719-726. ⟨10.1016/j.fsi.2010.01.008⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fsi.2010.01.008 hal-00477727 https://hal.science/hal-00477727 https://hal.science/hal-00477727v2/document https://hal.science/hal-00477727v2/file/Luna_Acosta_et_al_2010_FSIM.pdf doi:10.1016/j.fsi.2010.01.008 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.1016/j.fsi.2010.01.008 |
container_title |
Fish & Shellfish Immunology |
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28 |
container_issue |
4 |
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719 |
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726 |
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