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Physiological relevance and contribution to metal balance of specific and non-specific Metallothionein isoforms in the garden snail, Cantareus aspersus
- Source :
- BioMetals, BioMetals, Springer Verlag, 2011, 24 (6), pp.1079-92. 〈10.1007/s10534-011-9466-x〉, BioMetals, Springer Verlag, 2011, 24 (6), pp.1079-92. ⟨10.1007/s10534-011-9466-x⟩
- Publication Year :
- 2011
- Publisher :
- HAL CCSD, 2011.
-
Abstract
- International audience; Variable environmental availability of metal ions represents a constant challenge for most organisms, so that during evolution, they have optimised physiological and molecular mechanisms to cope with this particular requirement. Metallothioneins (MTs) are proteins that play a major role in metal homeostasis and as a reservoir. The MT gene/protein systems of terrestrial helicid snails are an invaluable model for the study of metal-binding features and MT isoform-specific functionality of these proteins. In the present study, we characterised three paralogous MT isogenes and their expressed products in the escargot (Cantareus aspersus). The metal-dependent transcriptional activation of the three isogenes was assessed using quantitative Real Time PCR. The metal-binding capacities of the three isoforms were studied by characterising the purified native complexes. All the data were analysed in relation to the trace element status of the animals after metal feeding. Two of the three C. aspersus MT (CaMT) isoforms appeared to be metal-specific, (CaCdMT and CaCuMT, for cadmium and copper respectively). A third isoform (CaCd/CuMT) was non-specific, since it was natively recovered as a mixed Cd/Cu complex. A specific role in Cd detoxification for CaCdMT was revealed, with a 80-90% contribution to the Cd balance in snails exposed to this metal. Conclusive data were also obtained for the CaCuMT isoform, which is involved in Cu homeostasis, sharing about 30-50% of the Cu balance of C. aspersus. No apparent metal-related physiological function was found for the third isoform (CaCd/CuMT), so its contribution to the metal balance of the escargot may be, if at all, of only marginal significance, but may enclose a major interest in evolutionary studies.
- Subjects :
- MESH : Molecular Sequence Data
Transcription, Genetic
[ SDV.TOX.ECO ] Life Sciences [q-bio]/Toxicology/Ecotoxicology
MESH: Amino Acid Sequence
MESH: Protein Isoforms
010501 environmental sciences
01 natural sciences
Mass Spectrometry
MESH: Recombinant Proteins
Transcription (biology)
MESH: Helix (Snails)
Metallothionein
Protein Isoforms
MESH: Animals
MESH : Copper
Peptide sequence
Chromatography, High Pressure Liquid
MESH : Cadmium
0303 health sciences
Cadmium
biology
Ecology
MESH : Amino Acid Sequence
MESH : Sequence Alignment
Metals and Alloys
Recombinant Proteins
MESH: Copper
Biochemistry
MESH : Helix (Snails)
[SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology
General Agricultural and Biological Sciences
Gene isoform
MESH : Recombinant Proteins
Molecular Sequence Data
MESH: Sequence Alignment
MESH: Cadmium
chemistry.chemical_element
Sequence alignment
Pulmonata
General Biochemistry, Genetics and Molecular Biology
Biomaterials
03 medical and health sciences
MESH : Chromatography, High Pressure Liquid
MESH : Mass Spectrometry
Animals
Amino Acid Sequence
MESH: Chromatography, High Pressure Liquid
Gene
030304 developmental biology
0105 earth and related environmental sciences
MESH: Mass Spectrometry
MESH: Molecular Sequence Data
MESH: Transcription, Genetic
Helix, Snails
MESH: Metallothionein
MESH : Transcription, Genetic
MESH : Protein Isoforms
biology.organism_classification
MESH : Metallothionein
chemistry
MESH : Animals
Sequence Alignment
Copper
Subjects
Details
- Language :
- English
- ISSN :
- 09660844 and 15728773
- Database :
- OpenAIRE
- Journal :
- BioMetals, BioMetals, Springer Verlag, 2011, 24 (6), pp.1079-92. 〈10.1007/s10534-011-9466-x〉, BioMetals, Springer Verlag, 2011, 24 (6), pp.1079-92. ⟨10.1007/s10534-011-9466-x⟩
- Accession number :
- edsair.doi.dedup.....ba06074afee8730c6daef5e288beaa17
- Full Text :
- https://doi.org/10.1007/s10534-011-9466-x〉