Differential tissue distribution and specificity of phenoloxidases from the Pacific oyster Crassostrea gigas
International audience Phenoloxidases (POs) play a key role in melanin production, are involved in invertebrate immune mechanisms, and have been detected in different bivalves. Recently, we identified catecholase- and laccase-like PO activities in plasma and haemocyte lysate supernatant (HLS) of the...
Published in: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |
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Format: | Article in Journal/Newspaper |
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Online Access: | https://hal.science/hal-00616689 https://hal.science/hal-00616689/document https://hal.science/hal-00616689/file/Luna-Acosta_et_al_2011_CBP.pdf https://doi.org/10.1016/j.cbpb.2011.04.009 |
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ftunivnantes:oai:HAL:hal-00616689v1 2023-05-15T15:58:28+02:00 Differential tissue distribution and specificity of phenoloxidases from the Pacific oyster Crassostrea gigas Luna-Acosta, Andrea Thomas-Guyon, Hélène Amari, Myriam Rosenfeld, Eric Bustamante, Paco Fruitier-Arnaudin, Ingrid LIttoral ENvironnement et Sociétés (LIENSs) La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) 2011-08-01 https://hal.science/hal-00616689 https://hal.science/hal-00616689/document https://hal.science/hal-00616689/file/Luna-Acosta_et_al_2011_CBP.pdf https://doi.org/10.1016/j.cbpb.2011.04.009 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.cbpb.2011.04.009 hal-00616689 https://hal.science/hal-00616689 https://hal.science/hal-00616689/document https://hal.science/hal-00616689/file/Luna-Acosta_et_al_2011_CBP.pdf doi:10.1016/j.cbpb.2011.04.009 info:eu-repo/semantics/OpenAccess ISSN: 1096-4959 Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology https://hal.science/hal-00616689 Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology, 2011, 159 (4), pp.220-226. ⟨10.1016/j.cbpb.2011.04.009⟩ bivalve phenoloxidase laccase catecholase zymography [SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology info:eu-repo/semantics/article Journal articles 2011 ftunivnantes https://doi.org/10.1016/j.cbpb.2011.04.009 2023-03-08T00:18:06Z International audience Phenoloxidases (POs) play a key role in melanin production, are involved in invertebrate immune mechanisms, and have been detected in different bivalves. Recently, we identified catecholase- and laccase-like PO activities in plasma and haemocyte lysate supernatant (HLS) of the Pacific oyster Crassostrea gigas. To go further in our investigations, the aims of this study were (i) to determine the tissue distribution of PO activities in C. gigas, and (ii) to identify and characterise the different sub-classes of POs (i.e. tyrosinase, catecholase and/or laccase) involved in these oxido-reductase activities. With dopamine and p-phenylenediamine (PPD) but not with L-tyrosine used as substrates, PO-activities were detected by spectrophotometry in the gills, digestive gland, mantle, and muscle. These results suggest the presence of catecholase and laccase but not of tyrosinase activities in oyster tissues. The highest activity was recovered in the digestive gland. PO-like activities were all inhibited by 1-phenyl-2-thiourea (PTU) and by the specific laccase inhibitor, cethyltrimethylammonium bromide (CTAB). With dopamine as substrate, the catecholase inhibitor 4-hexylresorcinol (4-HR) only inhibited PO in the muscle. SDS-PAGE zymographic assays with dopamine and PPD elicited a unique ~40 kDa protein band in the muscle. In the other tissues, laccase-like activities could be related to ~10 kDa and/or ~200 kDa protein bands. The ~10 kDa protein band was also detected in plasma and HLS, confirming the presence of a laccase in the later compartments, and probably in most of the tissues of C.gigas. This is the first time to our knowledge that a ~10 kDa protein band is associated to a laccase-like activity in a mollusc species, contributing to the characterisation of phenoloxidase activities in marine bivalves. Article in Journal/Newspaper Crassostrea gigas Pacific oyster Université de Nantes: HAL-UNIV-NANTES Pacific Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 159 4 220 226 |
institution |
Open Polar |
collection |
Université de Nantes: HAL-UNIV-NANTES |
op_collection_id |
ftunivnantes |
language |
English |
topic |
bivalve phenoloxidase laccase catecholase zymography [SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology |
spellingShingle |
bivalve phenoloxidase laccase catecholase zymography [SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology Luna-Acosta, Andrea Thomas-Guyon, Hélène Amari, Myriam Rosenfeld, Eric Bustamante, Paco Fruitier-Arnaudin, Ingrid Differential tissue distribution and specificity of phenoloxidases from the Pacific oyster Crassostrea gigas |
topic_facet |
bivalve phenoloxidase laccase catecholase zymography [SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology |
description |
International audience Phenoloxidases (POs) play a key role in melanin production, are involved in invertebrate immune mechanisms, and have been detected in different bivalves. Recently, we identified catecholase- and laccase-like PO activities in plasma and haemocyte lysate supernatant (HLS) of the Pacific oyster Crassostrea gigas. To go further in our investigations, the aims of this study were (i) to determine the tissue distribution of PO activities in C. gigas, and (ii) to identify and characterise the different sub-classes of POs (i.e. tyrosinase, catecholase and/or laccase) involved in these oxido-reductase activities. With dopamine and p-phenylenediamine (PPD) but not with L-tyrosine used as substrates, PO-activities were detected by spectrophotometry in the gills, digestive gland, mantle, and muscle. These results suggest the presence of catecholase and laccase but not of tyrosinase activities in oyster tissues. The highest activity was recovered in the digestive gland. PO-like activities were all inhibited by 1-phenyl-2-thiourea (PTU) and by the specific laccase inhibitor, cethyltrimethylammonium bromide (CTAB). With dopamine as substrate, the catecholase inhibitor 4-hexylresorcinol (4-HR) only inhibited PO in the muscle. SDS-PAGE zymographic assays with dopamine and PPD elicited a unique ~40 kDa protein band in the muscle. In the other tissues, laccase-like activities could be related to ~10 kDa and/or ~200 kDa protein bands. The ~10 kDa protein band was also detected in plasma and HLS, confirming the presence of a laccase in the later compartments, and probably in most of the tissues of C.gigas. This is the first time to our knowledge that a ~10 kDa protein band is associated to a laccase-like activity in a mollusc species, contributing to the characterisation of phenoloxidase activities in marine bivalves. |
author2 |
LIttoral ENvironnement et Sociétés (LIENSs) La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) |
format |
Article in Journal/Newspaper |
author |
Luna-Acosta, Andrea Thomas-Guyon, Hélène Amari, Myriam Rosenfeld, Eric Bustamante, Paco Fruitier-Arnaudin, Ingrid |
author_facet |
Luna-Acosta, Andrea Thomas-Guyon, Hélène Amari, Myriam Rosenfeld, Eric Bustamante, Paco Fruitier-Arnaudin, Ingrid |
author_sort |
Luna-Acosta, Andrea |
title |
Differential tissue distribution and specificity of phenoloxidases from the Pacific oyster Crassostrea gigas |
title_short |
Differential tissue distribution and specificity of phenoloxidases from the Pacific oyster Crassostrea gigas |
title_full |
Differential tissue distribution and specificity of phenoloxidases from the Pacific oyster Crassostrea gigas |
title_fullStr |
Differential tissue distribution and specificity of phenoloxidases from the Pacific oyster Crassostrea gigas |
title_full_unstemmed |
Differential tissue distribution and specificity of phenoloxidases from the Pacific oyster Crassostrea gigas |
title_sort |
differential tissue distribution and specificity of phenoloxidases from the pacific oyster crassostrea gigas |
publisher |
HAL CCSD |
publishDate |
2011 |
url |
https://hal.science/hal-00616689 https://hal.science/hal-00616689/document https://hal.science/hal-00616689/file/Luna-Acosta_et_al_2011_CBP.pdf https://doi.org/10.1016/j.cbpb.2011.04.009 |
geographic |
Pacific |
geographic_facet |
Pacific |
genre |
Crassostrea gigas Pacific oyster |
genre_facet |
Crassostrea gigas Pacific oyster |
op_source |
ISSN: 1096-4959 Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology https://hal.science/hal-00616689 Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology, 2011, 159 (4), pp.220-226. ⟨10.1016/j.cbpb.2011.04.009⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.cbpb.2011.04.009 hal-00616689 https://hal.science/hal-00616689 https://hal.science/hal-00616689/document https://hal.science/hal-00616689/file/Luna-Acosta_et_al_2011_CBP.pdf doi:10.1016/j.cbpb.2011.04.009 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.1016/j.cbpb.2011.04.009 |
container_title |
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |
container_volume |
159 |
container_issue |
4 |
container_start_page |
220 |
op_container_end_page |
226 |
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