2-DE Mapping of the Blue Mussel Gill Proteome: The Usual Suspects Revisited
The Blue Mussel (Mytilus edulis, L. 1758) is an ecologically important and commercially relevant bivalve. Because of its ability to bioconcentrate xenobiotics, it is also a widespread sentinel species for environmental pollution, which has been used in ecotoxicological studies for biomarker assess...
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| Format: | Article |
| Language: | English |
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MDPI AG
2015-01-01
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| Series: | Proteomes |
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| Online Access: | http://www.mdpi.com/2227-7382/3/1/3 |
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| author | Béatrice Rocher Florence Bultelle Philippe Chan Frank Le Foll Julie Letendre Tiphaine Monsinjon Stéphanie Olivier Romain Péden Agnès Poret David Vaudry Thomas Knigge |
| author_facet | Béatrice Rocher Florence Bultelle Philippe Chan Frank Le Foll Julie Letendre Tiphaine Monsinjon Stéphanie Olivier Romain Péden Agnès Poret David Vaudry Thomas Knigge |
| author_sort | Béatrice Rocher |
| collection | DOAJ |
| description | The Blue Mussel (Mytilus edulis, L. 1758) is an ecologically important and commercially relevant bivalve. Because of its ability to bioconcentrate xenobiotics, it is also a widespread sentinel species for environmental pollution, which has been used in ecotoxicological studies for biomarker assessment. Consequently, numerous proteomics studies have been carried out in various research contexts using mussels of the genus Mytilus, which intended to improve our understanding of complex physiological processes related to reproduction, adaptation to physical stressors or shell formation and for biomarker discovery. Differential-display 2-DE proteomics relies on an extensive knowledge of the proteome with as many proteoforms identified as possible. To this end, extensive characterization of proteins was performed in order to increase our knowledge of the Mytilus gill proteome. On average, 700 spots were detected on 2-DE gels by colloidal blue staining, of which 122 different, non-redundant proteins comprising 203 proteoforms could be identified by tandem mass spectrometry. These proteins could be attributed to four major categories: (i) “metabolism”, including antioxidant defence and degradation of xenobiotics; (ii) “genetic information processing”, comprising transcription and translation as well as folding, sorting, repair and degradation; (iii) “cellular processes”, such as cell motility, transport and catabolism; (iv) “environmental information processing”, including signal transduction and signalling molecules and interaction. The role of cytoskeleton proteins, energetic metabolism, chaperones/stress proteins, protein trafficking and the proteasome are discussed in the light of the exigencies of the intertidal environment, leading to an enhanced stress response, as well as the structural and physiological particularities of the bivalve gill tissue. |
| first_indexed | 2024-12-10T07:14:26Z |
| format | Article |
| id | doaj.art-49959ec7b36d4953ad1935ff17580a03 |
| institution | Directory Open Access Journal |
| issn | 2227-7382 |
| language | English |
| last_indexed | 2024-12-10T07:14:26Z |
| publishDate | 2015-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Proteomes |
| spelling | doaj.art-49959ec7b36d4953ad1935ff17580a032022-12-22T01:57:59ZengMDPI AGProteomes2227-73822015-01-013134110.3390/proteomes3010003proteomes30100032-DE Mapping of the Blue Mussel Gill Proteome: The Usual Suspects RevisitedBéatrice Rocher0Florence Bultelle1Philippe Chan2Frank Le Foll3Julie Letendre4Tiphaine Monsinjon5Stéphanie Olivier6Romain Péden7Agnès Poret8David Vaudry9Thomas Knigge10Laboratory of Ecotoxicology—Aquatic Environments, UMR I-02 SEBIO, Le Havre University, 76063 Le Havre, FranceLaboratory of Ecotoxicology—Aquatic Environments, UMR I-02 SEBIO, Le Havre University, 76063 Le Havre, FrancePISSARO Proteomic Platform, Institute for Research and Innovation in Biomedicine, University of Rouen, 76821 Mont-Saint-Aignan, FranceLaboratory of Ecotoxicology—Aquatic Environments, UMR I-02 SEBIO, Le Havre University, 76063 Le Havre, FranceLaboratory of Ecotoxicology—Aquatic Environments, UMR I-02 SEBIO, Le Havre University, 76063 Le Havre, FranceLaboratory of Ecotoxicology—Aquatic Environments, UMR I-02 SEBIO, Le Havre University, 76063 Le Havre, FranceLaboratory of Ecotoxicology—Aquatic Environments, UMR I-02 SEBIO, Le Havre University, 76063 Le Havre, FranceLaboratory of Ecotoxicology—Aquatic Environments, UMR I-02 SEBIO, Le Havre University, 76063 Le Havre, FranceLaboratory of Ecotoxicology—Aquatic Environments, UMR I-02 SEBIO, Le Havre University, 76063 Le Havre, FranceNeuronal and Neuroendocrine Differentiation and Communication (DC2N), Inserm U982, University of Rouen, 76821 Mont-Saint-Aignan, FranceLaboratory of Ecotoxicology—Aquatic Environments, UMR I-02 SEBIO, Le Havre University, 76063 Le Havre, FranceThe Blue Mussel (Mytilus edulis, L. 1758) is an ecologically important and commercially relevant bivalve. Because of its ability to bioconcentrate xenobiotics, it is also a widespread sentinel species for environmental pollution, which has been used in ecotoxicological studies for biomarker assessment. Consequently, numerous proteomics studies have been carried out in various research contexts using mussels of the genus Mytilus, which intended to improve our understanding of complex physiological processes related to reproduction, adaptation to physical stressors or shell formation and for biomarker discovery. Differential-display 2-DE proteomics relies on an extensive knowledge of the proteome with as many proteoforms identified as possible. To this end, extensive characterization of proteins was performed in order to increase our knowledge of the Mytilus gill proteome. On average, 700 spots were detected on 2-DE gels by colloidal blue staining, of which 122 different, non-redundant proteins comprising 203 proteoforms could be identified by tandem mass spectrometry. These proteins could be attributed to four major categories: (i) “metabolism”, including antioxidant defence and degradation of xenobiotics; (ii) “genetic information processing”, comprising transcription and translation as well as folding, sorting, repair and degradation; (iii) “cellular processes”, such as cell motility, transport and catabolism; (iv) “environmental information processing”, including signal transduction and signalling molecules and interaction. The role of cytoskeleton proteins, energetic metabolism, chaperones/stress proteins, protein trafficking and the proteasome are discussed in the light of the exigencies of the intertidal environment, leading to an enhanced stress response, as well as the structural and physiological particularities of the bivalve gill tissue.http://www.mdpi.com/2227-7382/3/1/32-DEmass spectrometryproteoformspost-translational modificationsbivalve molluscenvironmental stressecotoxicology |
| spellingShingle | Béatrice Rocher Florence Bultelle Philippe Chan Frank Le Foll Julie Letendre Tiphaine Monsinjon Stéphanie Olivier Romain Péden Agnès Poret David Vaudry Thomas Knigge 2-DE Mapping of the Blue Mussel Gill Proteome: The Usual Suspects Revisited Proteomes 2-DE mass spectrometry proteoforms post-translational modifications bivalve mollusc environmental stress ecotoxicology |
| title | 2-DE Mapping of the Blue Mussel Gill Proteome: The Usual Suspects Revisited |
| title_full | 2-DE Mapping of the Blue Mussel Gill Proteome: The Usual Suspects Revisited |
| title_fullStr | 2-DE Mapping of the Blue Mussel Gill Proteome: The Usual Suspects Revisited |
| title_full_unstemmed | 2-DE Mapping of the Blue Mussel Gill Proteome: The Usual Suspects Revisited |
| title_short | 2-DE Mapping of the Blue Mussel Gill Proteome: The Usual Suspects Revisited |
| title_sort | 2 de mapping of the blue mussel gill proteome the usual suspects revisited |
| topic | 2-DE mass spectrometry proteoforms post-translational modifications bivalve mollusc environmental stress ecotoxicology |
| url | http://www.mdpi.com/2227-7382/3/1/3 |
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