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M Carriere

Publications and source records attributed to M Carriere.

5 recordsLinked to original sources

Actinide speciation in relation to biological processes.

In case of accidental release of radionuclides into the environment, actinides represent a severe health risk to human beings following internal contamination (inhalation, ingestion or wound). For a better understanding of the actinide behaviour in man (in term of metabolism, retention, excretion) and in specific biological systems (organs, cells or biochemical pathways), it is of prime importance to have a good knowledge of the relevant actinide solution chemistry and biochemistry, in particular of the thermodynamic constants needed for computing actinide speciation. To a large extent, speciation governs bioavailability and toxicity of elements and has a significant impact on the mechanisms by which toxics accumulate in cell compartments and organs and by which elements are transferred and transported from cell to cell. From another viewpoint, speciation is the prerequisite for the design and success of potential decorporation therapies. The purpose of this review is to present the state of the art of actinide knowledge within biological media. It is also to discuss how actinide speciation can be determined or predicted and to highlight the areas where information is lacking with the aim to encourage new research efforts.

Actinoid Series Elements↗

Osmotic stress activated expression of an Arabidopsis plasma membrane-associated protein: sequence and predicted secondary structure.

A cDNA clone At.MAMI (Arabidopsis thaliana membrane-associated mannitol-induced) was isolated from an Arabidopsis cDNA expression library by immunoselection. The cDNA was full-length (1.18 kb) with an open reading frame of 798 nucleotides encoding a 265 amino acid protein. The sequence of At.MAMI did not show any significant identity with other genes, as well as the deduced amino acid sequence with other proteins. However, prediction methods for the secondary structure of MAMI-30, together with homologous domains revealed some identity with VAP-33, a protein involved in membrane trafficking in neuronal tissues. In contrast to VAP-33, MAMI-30 did not exhibit a transmembrane domain, but positively charged loop regions could be involved in membrane anchoring. Indeed, MAMI-30 was immunodetected in purified plasma membrane from Arabidopsis cells. The gene was responsive to low turgor in Arabidopsis and its expression regulated developmentally. In addition, reduction of turgor caused a higher accumulation of mRNAs.

Amino Acid Sequence↗