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6. Loss of the thyroid hormone-binding protein Crym renders striatal neurons more vulnerable to mutant huntingtin in Huntington's disease

Author

Francelle, Laetitia, Galvan, Laurie, Gaillard, Marie-Claude, Guillermier, Martine, Houitte, Diane, Bonvento, Gilles, Petit, Fanny, Jan, Caroline, Dufour, Noëlle, Hantraye, Philippe, Elalouf, Jean-Marc, De Chaldée, Michel, Déglon, Nicole, Brouillet, Emmanuel, Francelle, Laetitia, Galvan, Laurie, Gaillard, Marie-Claude, Guillermier, Martine, Houitte, Diane, Bonvento, Gilles, Petit, Fanny, Jan, Caroline, Dufour, Noëlle, Hantraye, Philippe, Elalouf, Jean-Marc, De Chaldée, Michel, Déglon, Nicole, and Brouillet, Emmanuel

Abstract

The mechanisms underlying preferential atrophy of the striatum in Huntington's disease (HD) are unknown. One hypothesis is that a set of gene products preferentially expressed in the striatum could determine the particular vulnerability of this brain region to mutant huntingtin (mHtt). Here, we studied the striatal protein µ-crystallin (Crym). Crym is the NADPH-dependent p38 cytosolic T3-binding protein (p38CTBP), a key regulator of thyroid hormone (TH) T3 (3,5,3′-triiodo-l-thyronine) transportation. It has been also recently identified as the enzyme that reduces the sulfur-containing cyclic ketimines, which are potential neurotransmitters. Here, we confirm the preferential expression of the Crym protein in the rodent and macaque striatum. Crym expression was found to be higher in the macaque caudate than in the putamen. Expression of Crym was reduced in the BACHD and Knock-in 140CAG mouse models of HD before onset of striatal atrophy. We show that overexpression of Crym in striatal medium-size spiny neurons using a lentiviral-based strategy in mice is neuroprotective against the neurotoxicity of an N-terminal fragment of mHtt in vivo. Thus, reduction of Crym expression in HD could render striatal neurons more susceptible to mHtt suggesting that Crym may be a key determinant of the vulnerability of the striatum. In addition our work points to Crym as a potential molecular link between striatal degeneration and the THs deregulation reported in HD patients

Published
2017

7. O2-07-04: Specific Inhibition of Astrocyte Reactivity Improves Some Disease Outcomes in Alzheimer's Disease Mice

Author

Ceyzeriat, Kelly, primary, Ben Haim, Lucile, additional, Saint-Georges, Thomas, additional, Petit, Fanny, additional, Houitte, Diane, additional, Guillermier, Martine, additional, Berniard, Aurelie, additional, Mitja, Julien, additional, Josephine, Charlene, additional, Hantraye, Philippe, additional, Brouillet, Emmanuel, additional, Cambon, Karine, additional, Dhenain, Marc, additional, Bonvento, Gilles, additional, and Escartin, Carole, additional

Published
2016
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8. The JAK/STAT3 Pathway Is a Common Inducer of Astrocyte Reactivity in Alzheimer's and Huntington's Diseases

Author

Ben Haim, Lucile, primary, Ceyzériat, Kelly, additional, Carrillo-de Sauvage, Maria Angeles, additional, Aubry, Fabien, additional, Auregan, Gwennaëlle, additional, Guillermier, Martine, additional, Ruiz, Marta, additional, Petit, Fanny, additional, Houitte, Diane, additional, Faivre, Emilie, additional, Vandesquille, Matthias, additional, Aron-Badin, Romina, additional, Dhenain, Marc, additional, Déglon, Nicole, additional, Hantraye, Philippe, additional, Brouillet, Emmanuel, additional, Bonvento, Gilles, additional, and Escartin, Carole, additional

Published
2015
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9. Loss of the thyroid hormone-binding protein Crym renders striatal neurons more vulnerable to mutant huntingtin in Huntington's disease

Author

Francelle, Laetitia, primary, Galvan, Laurie, additional, Gaillard, Marie-Claude, additional, Guillermier, Martine, additional, Houitte, Diane, additional, Bonvento, Gilles, additional, Petit, Fanny, additional, Jan, Caroline, additional, Dufour, Noëlle, additional, Hantraye, Philippe, additional, Elalouf, Jean-Marc, additional, De Chaldée, Michel, additional, Déglon, Nicole, additional, and Brouillet, Emmanuel, additional

Published
2014
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10. Intracellular metabolites in the primate brain are primarily localized in long fibers rather than in cell bodies, as shown by diffusion-weighted magnetic resonance spectroscopy

Author

Najac, Chloé, primary, Marchadour, Charlotte, additional, Guillermier, Martine, additional, Houitte, Diane, additional, Slavov, Velislav, additional, Brouillet, Emmanuel, additional, Hantraye, Philippe, additional, Lebon, Vincent, additional, and Valette, Julien, additional

Published
2014
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13. P2-002: In-vivo detection of age-related cerebral glucose uptake alterations by pet in microcebus murinus primates

Author

Daorieux, Ole ne, primary, Joseph-Mathurin, Nelly, additional, Chaigneau, Marion, additional, Guillermier, Martine, additional, Houitte, Diane, additional, Josephine, Charlene, additional, David Santin, Mathieu, additional, Kraska, Audrey, additional, Van-Camp, Nadja, additional, Phillippe, Hantraye, additional, Metzker, Friedrich, additional, Perret, Martine, additional, and Dhenain, Marc, additional

Published
2011
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14. IC-P-002: Invivo detection of age-related cerebral glucose uptake alterations by PET in microcebus murinus primates

Author

Dorieux, Olene, primary, Joseph-Mathurin, Nelly, additional, Chaigneau, Marion, additional, Guillermier, Martine, additional, Houitte, Diane, additional, Josephine, Charlène, additional, Santin, Mathieu, additional, Kraska, Audrey, additional, Van-Camp, Nadja, additional, Philippe, Hantraye, additional, Metzger, Friedrich, additional, Perret, Martine, additional, and Dhenain, Marc, additional

Published
2011
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15. O1-03-07: MRI evaluation of focal brain lesions in streptozotocin-treated animals: Comparison between rodents (rats) and primates (microcebus murinus)

Author

Kraska, Audrey, primary, Santin, Mathieu, additional, Dhenain, Marc, additional, Philippe, Hantraye, additional, Dorieux, Olene, additional, Chaigneau, Marion, additional, Guillermier, Martine, additional, Houitte, Diane, additional, Josephine, Charlène, additional, Perret, Martine, additional, Joseph-Mathurin, Nelly, additional, Aujard, Fabienne, additional, and Lestage, Pierre, additional

Published
2011
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19. The neuroprotective agent CNTF decreases neuronal metabolites in the rat striatum: an in vivo multimodal magnetic resonance imaging study.

Author

Carrillo-de Sauvage, Maria-Angeles, Flament, Julien, Bramoulle, Yann, Ben Haim, Lucile, Guillermier, Martine, Berniard, Aurélie, Aurégan, Gwennaëlle, Houitte, Diane, Brouillet, Emmanuel, Bonvento, Gilles, Hantraye, Philippe, Valette, Julien, and Escartin, Carole

Subjects
NEUROPROTECTIVE agents, MAGNETIC resonance imaging of the brain, CILIARY neurotrophic factor, LABORATORY rats, PATHOLOGICAL physiology, HIGH performance liquid chromatography
Abstract

Ciliary neurotrophic factor (CNTF) is neuroprotective against multiple pathologic conditions including metabolic impairment, but the mechanisms are still unclear. To delineate CNTF effects on brain energy homeostasis, we performed a multimodal imaging study, combining in vivo proton magnetic resonance spectroscopy, high-performance liquid chromatography analysis, and in situ glutamate imaging by chemical exchange saturation transfer. Unexpectedly, we found that CNTF expression through lentiviral gene transfer in the rat striatum significantly decreased the levels of neuronal metabolites (N-acetyl-aspartate, N-acetyl-aspartyl-glutamate, and glutamate). This preclinical study shows that CNTF remodels brain metabolism, and suggests that decreased levels of neuronal metabolites may occur in the absence of neuronal dysfunction. [ABSTRACT FROM AUTHOR]

Published
2015
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20. The JAK/STAT3 Pathway Is a Common Inducer of Astrocyte Reactivity in Alzheimer's and Huntington's Diseases.

Author

Haim, Lucile Ben, Ceyzériat, Kelly, Carrillo-de Sauvage, Maria Angeles, Aubry, Fabien, Auregan, Gwennaëlle, Guillermier, Martine, Ruiz, Marta, Petit, Fanny, Houitte, Diane, Faivre, Emilie, Vandesquille, Matthias, Aron-Badin, Romina, Dhenain, Marc, Déglon, Nicole, Hantraye, Philippe, Brouillet, Emmanuel, Bonvento, Gilles, and Escartin, Carole

Subjects
ANIMAL models of Alzheimer's disease, CELLULAR signal transduction, JANUS kinases, ANIMAL models in research, HUNTINGTON disease, ASTROCYTES, STAT proteins, DISEASE progression
Abstract

Astrocyte reactivity is a hallmark of neurodegenerative diseases (ND), but its effects on disease outcomes remain highly debated. Elucidation of the signaling cascades inducing reactivity in astrocytes during ND would help characterize the function of these cells and identify novel molecular targets to modulate disease progression. The Janus kinase/signal transducer and activator of transcription 3 (JAK/STAT3) pathway is associated with reactive astrocytes in models of acute injury, but it is unknown whether this pathway is directly responsible for astrocyte reactivity in progressive pathological conditions such as ND. In this study, we examined whether the JAK/STAT3 pathway promotes astrocyte reactivity in several animal models of ND. The JAK/STAT3 pathway was activated in reactive astrocytes in two transgenic mouse models of Alzheimer's disease and in a mouse and a nonhuman primate lentiviral vector-based model of Huntington's disease (HD). To determine whether this cascade was instrumental for astrocyte reactivity, we used a lentiviral vector that specifically targets astrocytes in vivo to overexpress the endogenous inhibitor of the JAK/STAT3 pathway [suppressor of cytokine signaling 3 (SOCS3)]. SOCS3 significantly inhibited this pathway in astrocytes, prevented astrocyte reactivity, and decreased microglial activation in models of both diseases. Inhibition of the JAK/STAT3 pathway within reactive astrocytes also increased the number of huntingtin aggregates, a neuropathological hallmark of HD, but did not influence neuronal death. Our data demonstrate that the JAK/STAT3 pathway is a common mediator of astrocyte reactivity that is highly conserved between disease states, species, and brain regions. This universal signaling cascade represents a potent target to study the role of reactive astrocytes in ND. [ABSTRACT FROM AUTHOR]

Published
2015
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25. Loss of the thyroid hormone-binding protein Crym renders striatal neurons more vulnerable to mutant huntingtin in Huntington's disease

Author

Francelle, Laetitia, Galvan, Laurie, Gaillard, Marie-Claude, Guillermier, Martine, Houitte, Diane, Bonvento, Gilles, Petit, Fanny, Jan, Caroline, Dufour, Noëlle, Hantraye, Philippe, Elalouf, Jean-Marc, De Chaldée, Michel, Déglon, Nicole, Brouillet, Emmanuel, Francelle, Laetitia, Galvan, Laurie, Gaillard, Marie-Claude, Guillermier, Martine, Houitte, Diane, Bonvento, Gilles, Petit, Fanny, Jan, Caroline, Dufour, Noëlle, Hantraye, Philippe, Elalouf, Jean-Marc, De Chaldée, Michel, Déglon, Nicole, and Brouillet, Emmanuel

Abstract

The mechanisms underlying preferential atrophy of the striatum in Huntington's disease (HD) are unknown. One hypothesis is that a set of gene products preferentially expressed in the striatum could determine the particular vulnerability of this brain region to mutant huntingtin (mHtt). Here, we studied the striatal protein µ-crystallin (Crym). Crym is the NADPH-dependent p38 cytosolic T3-binding protein (p38CTBP), a key regulator of thyroid hormone (TH) T3 (3,5,3′-triiodo-l-thyronine) transportation. It has been also recently identified as the enzyme that reduces the sulfur-containing cyclic ketimines, which are potential neurotransmitters. Here, we confirm the preferential expression of the Crym protein in the rodent and macaque striatum. Crym expression was found to be higher in the macaque caudate than in the putamen. Expression of Crym was reduced in the BACHD and Knock-in 140CAG mouse models of HD before onset of striatal atrophy. We show that overexpression of Crym in striatal medium-size spiny neurons using a lentiviral-based strategy in mice is neuroprotective against the neurotoxicity of an N-terminal fragment of mHtt in vivo. Thus, reduction of Crym expression in HD could render striatal neurons more susceptible to mHtt suggesting that Crym may be a key determinant of the vulnerability of the striatum. In addition our work points to Crym as a potential molecular link between striatal degeneration and the THs deregulation reported in HD patients

27. Immunoprevalence of the CD4+ T-cell response to HIV Tat and Vpr proteins is provided by clustered and disperse epitopes, respectively.

Author

Castelli FA, Houitte D, Munier G, Szely N, Lecoq A, Briand JP, Muller S, and Maillere B

Subjects
Cell Line, Dendritic Cells immunology, HIV Infections virology, HLA-DR Antigens immunology, Humans, Peptide Fragments immunology, Peptide Fragments metabolism, CD4-Positive T-Lymphocytes immunology, Epitopes, T-Lymphocyte immunology, Gene Products, tat immunology, HIV immunology, HIV Infections immunology, vpr Gene Products, Human Immunodeficiency Virus immunology
Abstract

Recent studies have suggested including nonstructural proteins as Tat and Vpr in HIV vaccines. However, little is known about the CD4+ T-cell response that these small proteins induce in humans. We have therefore evaluated these responses by in vitro priming experiments of CD4+ T lymphocytes harvested in healthy donors. In the Tat protein, only one peptide primed CD4+ T cells of eight HLA unrelated healthy donors. T cells induced by this peptide recognized immature DC loaded with the native Tat protein and are restricted by multiple HLA-DR molecules, in agreement with its binding capacity. This peptide was therefore processed in an appropriate manner and was highly immunoprevalent. CD4+ T-cell response to Vpr peptides was more disperse and involved six different peptides depending on the HLA-DR molecules of the donors. Two overlapping peptides were T-cell stimulating in at least half of the donors. T-cell response to Vpr in multiple donors is the result of a combination of several CD4+ T-cell epitopes with good to moderate immunoprevalence. Altogether, our results show that the frequency of responders to HIV Tat or Vpr proteins relies on one or multiple CD4+ T-cell epitopes, respectively.

Published
2008
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