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Dubois Martine


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tél : 02.38.25.55.36 - fax : 02.38.25.55.83

Publications

2013   Références trouvées : 1

Mollet L., Robinet P., Dubois M., Aurouet A., Normand T., Charpentier S., Sureau A., Grandclement C., Garnache-Ottou F., Deconinck E., Brulé F., Rohrlich P.S. and Legrand A.  (2013)

Opposing Mcl-1, the GALIG proapoptotic gene is upregulated as neutrophils die and underexpressed in Acute Myeloid Leukemia cells

Molecular Immunology 56 (1-2) 123-128
GALIG gene expression induces apoptosis in cultured cells through a pathway still under investigation. It is highly expressed in leukocytes but weakly detectable in bone marrow, suggesting a role in the myeloid lineage homeostasis. We show here that GALIG-induced cell death is counteracted by the overexpression of MCL-1, a pro-survival member of the Bcl2 family. Moreover, during spontaneous neutrophil apoptosis, a substantial increase in GALIG gene expression is observed : GALIG still opposes MCL-1. Finally, in bone marrow and peripheral blood cells from patients with Acute Myeloid Leukemia type 2, the level of GALIG transcripts is massively down-regulated when compared to their normal counterparts, while MCL-1 is expressed to the same extent. These data suggest that GALIG could be a key player in the cell death pathway involved in leukocytes homeostasis and myeloid malignancies.

GALIG gene expression induces apoptosis in cultured cells through a pathway still under investigation. It is highly expressed in leukocytes but weakly detectable in bone marrow, suggesting a role in the myeloid lineage homeostasis. We show here that GALIG-induced cell death is counteracted by the overexpression of MCL-1, a pro-survival member of the Bcl2 family. Moreover, during spontaneous neutrophil apoptosis, a substantial increase in GALIG gene expression is observed : GALIG still opposes MCL-1. Finally, in bone marrow and peripheral blood cells from patients with Acute Myeloid Leukemia type 2, the level of GALIG transcripts is massively down-regulated when compared to their normal counterparts, while MCL-1 is expressed to the same extent. These data suggest that GALIG could be a key player in the cell death pathway involved in leukocytes homeostasis and myeloid malignancies.


2010   Références trouvées : 1

Robinet, P., Mollet, L., Gonzalez, P., Normand, T., Charpentier, S., Brule, F., Dubois, M. & Legrand, A.  (2010)

The mitogaligin protein is addressed to the nucleus via a non-classical localization signal.

Biochem. Biophys. Res. Commun. 392, 53-57.


2009   Références trouvées : 1

Gonzalez, P., Robinet, P., Charpentier, S., Mollet, L., Normand, T., Dubois, M. & Legrand, A.  (2009)

Apoptotic activity of a nuclear form of mitogaligin, a cell death protein.

Biochem. Biophys. Res. Commun. 378, 816-820.


2007   Références trouvées : 1

Gonzalez, P ; Duneau, M ; Charpentier, S ; Normand, T ; Mollet, L ; Dubois, M ; Legrand, A  (2007)

Destabilization of membranes containing cardiolipin or its precursors by peptides derived from mitogaligin, a cell death protein

Biochemistry 46 (25) 7374-7382
Galig, a gene embedded within the galectin-3 gene, induces cell death when transfected in human cells. This death is associated with cell shrinkage, nuclei condensation, and aggregation of mitochondria. Galig contains two different overlapping open reading frames encoding two unrelated proteins. Previous observations have shown that one of these proteins, named mitogaligin, binds to mitochondria and promotes the release of cytochrome c. However, the mechanism of action of this cytotoxic protein remains still obscure.

Galig, a gene embedded within the galectin-3 gene, induces cell death when transfected in human cells. This death is associated with cell shrinkage, nuclei condensation, and aggregation of mitochondria. Galig contains two different overlapping open reading frames encoding two unrelated proteins. Previous observations have shown that one of these proteins, named mitogaligin, binds to mitochondria and promotes the release of cytochrome c. However, the mechanism of action of this cytotoxic protein remains still obscure.


2005   Références trouvées : 1

Duneau, M ; Boyer-Guittaut, M ; Gonzalez, P ; Charpentier, S ; Normand, T ; Dubois, M ; Raimond, J ; Legrand, A  (2005)

Galig, a novel cell death gene that encodes a mitochondrial protein promoting cytochrome c release

Experimental Cell Research 302 (2) 194-205
Galectin-3 internal gene (Galig) was recently identified as an internal gene transcribed from the second intron of the human galectin-3 gene that is implicated in cell growth, cell differentiation, and cancer development. In this study, we show that galig expression causes morphological alterations in human cells, such as cell shrinkage, cytoplasm vacuolization, nuclei condensation, and ultimately cell death. These alterations were associated with extramitochondrial release of cytochrome c, a known cell death effector.

Galectin-3 internal gene (Galig) was recently identified as an internal gene transcribed from the second intron of the human galectin-3 gene that is implicated in cell growth, cell differentiation, and cancer development. In this study, we show that galig expression causes morphological alterations in human cells, such as cell shrinkage, cytoplasm vacuolization, nuclei condensation, and ultimately cell death. These alterations were associated with extramitochondrial release of cytochrome c, a known cell death effector.


2001   Références trouvées : 1

Guittaut, M ; Charpentier, S ; Normand, T ; Dubois, M ; Raimond, J ; Legrand, A  (2001)

Identification of an internal gene to the human galectin-3 gene with two different overlapping reading frames that do not encode galectin-3

Journal of Biological Chemistry 276 (4) 2652-2657
We previously reported that alternative transcripts were initiated within the second intron of the human Galectin-3 gene (LGALS3), We now demonstrate that these transcripts arise from an internal gene embedded within LGALS3 and named galig (Galectin-3 internal gene). Tissue-specific expression of galig was assayed by screening of several human tissues. Contrary to LGALS3, galig appears to be tightly regulated and principally activated in leukocytes from peripheral blood. Cloning and characterization of galig transcripts revealed that they contain two out-of-frame overlapping open-reading frames (ORFs). Transfection of expression vectors encoding enhanced green fluorescent protein (EGFP) chimeras indicated that both ORFs could be translated in proteins unrelated to Galectin-3. The ORF1 polypeptide targets EGFP to cytosol and nucleus whereas ORF2 targets EGFP to mitochondria. These results revealed the exceptional genetic organization of the LGALS3 locus.

We previously reported that alternative transcripts were initiated within the second intron of the human Galectin-3 gene (LGALS3), We now demonstrate that these transcripts arise from an internal gene embedded within LGALS3 and named galig (Galectin-3 internal gene). Tissue-specific expression of galig was assayed by screening of several human tissues. Contrary to LGALS3, galig appears to be tightly regulated and principally activated in leukocytes from peripheral blood. Cloning and characterization of galig transcripts revealed that they contain two out-of-frame overlapping open-reading frames (ORFs). Transfection of expression vectors encoding enhanced green fluorescent protein (EGFP) chimeras indicated that both ORFs could be translated in proteins unrelated to Galectin-3. The ORF1 polypeptide targets EGFP to cytosol and nucleus whereas ORF2 targets EGFP to mitochondria. These results revealed the exceptional genetic organization of the LGALS3 locus.


Mots-clés

Assistant-ingénieur , Mort cellulaire programmée