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Article ; Online: Calcium Signalling in Alzheimer's Disease: From Pathophysiological Regulation to Therapeutic Approaches.

Chami, Mounia

2021 Volume 10, Issue 1

Abstract: Alzheimer's disease (AD) is a neurodegenerative pathology representing a socioeconomic challenge, however, the complex mechanism behind the disease is not yet fully understood [ ... ]. ...

Abstract	Alzheimer's disease (AD) is a neurodegenerative pathology representing a socioeconomic challenge, however, the complex mechanism behind the disease is not yet fully understood [...].
MeSH term(s)	Alzheimer Disease/physiopathology ; Alzheimer Disease/therapy ; Animals ; Calcium/metabolism ; Calcium Signaling ; Humans ; Neuronal Plasticity ; Neurons/metabolism
Chemical Substances	Calcium (SY7Q814VUP)
Language	English
Publishing date	2021-01-12
Publishing country	Switzerland
Document type	Editorial ; Introductory Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10010140
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Mitophagy in Alzheimer's disease: Molecular defects and therapeutic approaches.

Mary, Arnaud / Eysert, Fanny / Checler, Frédéric / Chami, Mounia

Molecular psychiatry

2022 Volume 28, Issue 1, Page(s) 202–216

Abstract: Mitochondrial dysfunctions are central players in Alzheimer's disease (AD). In addition, impairments in mitophagy, the process of selective mitochondrial degradation by autophagy leading to a gradual accumulation of defective mitochondria, have also been ...

Abstract	Mitochondrial dysfunctions are central players in Alzheimer's disease (AD). In addition, impairments in mitophagy, the process of selective mitochondrial degradation by autophagy leading to a gradual accumulation of defective mitochondria, have also been reported to occur in AD. We provide an updated overview of the recent discoveries and advancements on mitophagic molecular dysfunctions in AD-derived fluids and cells as well as in AD brains. We discuss studies using AD cellular and animal models that have unraveled the contribution of relevant AD-related proteins (Tau, Aβ, APP-derived fragments and APOE) in mitophagy failure. In accordance with the important role of impaired mitophagy in AD, we report on various therapeutic strategies aiming at stimulating mitophagy in AD and we summarize the benefits of these potential therapeutic strategies in human clinical trials.
MeSH term(s)	Animals ; Humans ; Alzheimer Disease/metabolism ; Mitophagy/physiology ; Autophagy/genetics ; Mitochondria/metabolism ; Disease Models, Animal ; Amyloid beta-Peptides/metabolism
Chemical Substances	Amyloid beta-Peptides
Language	English
Publishing date	2022-06-03
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	1330655-8
ISSN	1476-5578 ; 1359-4184
ISSN (online)	1476-5578
ISSN	1359-4184
DOI	10.1038/s41380-022-01631-6
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Article ; Online: Targeting Post-Translational Remodeling of Ryanodine Receptor: A New Track for Alzheimer's Disease Therapy?

Chami, Mounia / Checler, Frédéric

Current Alzheimer research

2020 Volume 17, Issue 4, Page(s) 313–323

Abstract: Pathologic calcium (Ca2+) signaling linked to Alzheimer's Disease (AD) involves the intracellular Ca2+ release channels/ryanodine receptors (RyRs). RyRs are macromolecular complexes where the protein-protein interactions between RyRs and several ... ...

Abstract	Pathologic calcium (Ca2+) signaling linked to Alzheimer's Disease (AD) involves the intracellular Ca2+ release channels/ryanodine receptors (RyRs). RyRs are macromolecular complexes where the protein-protein interactions between RyRs and several regulatory proteins impact the channel function. Pharmacological and genetic approaches link the destabilization of RyRs macromolecular complexes to several human pathologies including brain disorders. In this review, we discuss our recent data, which demonstrated that enhanced neuronal RyR2-mediated Ca2+ leak in AD is associated with posttranslational modifications (hyperphosphorylation, oxidation, and nitrosylation) leading to RyR2 macromolecular complex remodeling, and dissociation of the stabilizing protein Calstabin2 from the channel. We describe RyR macromolecular complex structure and discuss the molecular mechanisms and signaling cascade underlying neuronal RyR2 remodeling in AD. We provide evidence linking RyR2 dysfunction with β-adrenergic signaling cascade that is altered in AD. RyR2 remodeling in AD leads to histopathological lesions, alteration of synaptic plasticity, learning and memory deficits. Targeting RyR macromolecular complex remodeling should be considered as a new therapeutic window to treat/or prevent AD setting and/or progression.
MeSH term(s)	Alzheimer Disease/drug therapy ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Animals ; Calcium Channel Blockers/administration & dosage ; Calcium Channel Blockers/metabolism ; Calcium Signaling/drug effects ; Calcium Signaling/physiology ; Drug Delivery Systems/methods ; Drug Delivery Systems/trends ; Humans ; Protein Processing, Post-Translational/drug effects ; Protein Processing, Post-Translational/physiology ; Ryanodine Receptor Calcium Release Channel/genetics ; Ryanodine Receptor Calcium Release Channel/metabolism
Chemical Substances	Calcium Channel Blockers ; Ryanodine Receptor Calcium Release Channel
Language	English
Publishing date	2020-02-25
Publishing country	United Arab Emirates
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2205170-3
ISSN	1875-5828 ; 1567-2050
ISSN (online)	1875-5828
ISSN	1567-2050
DOI	10.2174/1567205017666200225102941
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Article ; Online: Alterations of the Endoplasmic Reticulum (ER) Calcium Signaling Molecular Components in Alzheimer's Disease.

Chami, Mounia / Checler, Frédéric

Cells

2020 Volume 9, Issue 12

Abstract: Sustained imbalance in intracellular calcium ( ... ...

Abstract	Sustained imbalance in intracellular calcium (Ca
MeSH term(s)	Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Animals ; Calcium/metabolism ; Calcium Signaling/physiology ; Cell Membrane/metabolism ; Endoplasmic Reticulum/metabolism ; Homeostasis/physiology ; Humans ; Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Ryanodine Receptor Calcium Release Channel/metabolism ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism
Chemical Substances	Amyloid beta-Peptides ; Inositol 1,4,5-Trisphosphate Receptors ; Ryanodine Receptor Calcium Release Channel ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2020-12-01
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells9122577
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Article ; Online: Dysfonction mitochondriale et défaillance de la mitophagie dans la maladie d’Alzheimer.

Mary, Arnaud / Vaillant-Beuchot, Loan / Checler, Frédéric / Chami, Mounia

Medecine sciences : M/S

2021 Volume 37, Issue 10, Page(s) 843–847

Title translation	Mitochondrial dysfunction and mitophagy failure in Alzheimer's disease.
MeSH term(s)	Alzheimer Disease ; Autophagy ; Humans ; Mitochondria ; Mitophagy
Language	French
Publishing date	2021-10-14
Publishing country	France
Document type	Journal Article
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2021133
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Article ; Online: The η-secretase-derived APP fragment ηCTF is localized in Golgi, endosomes and extracellular vesicles and contributes to Aβ production

Afram, Elissa / Lauritzen, Inger / Bourgeois, Alexandre / El Manaa, Wejdane / Duplan, Eric / Chami, Mounia / Valverde, Audrey / Charlotte, Bauer / Pardossi-Piquard, Raphaëlle / Checler, Frederic

Cell. Mol. Life Sci.. 2023 Apr., v. 80, no. 4 p.97-97

2023

Abstract: The processing of the amyloid precursor protein (APP) is one of the key events contributing to Alzheimer’s disease (AD) etiology. Canonical cleavages by β- and γ-secretases lead to Aβ production which accumulate in amyloid plaques. Recently, the matrix ... ...

Abstract	The processing of the amyloid precursor protein (APP) is one of the key events contributing to Alzheimer’s disease (AD) etiology. Canonical cleavages by β- and γ-secretases lead to Aβ production which accumulate in amyloid plaques. Recently, the matrix metalloprotease MT5-MMP, referred to as η-secretase, has been identified as a novel APP cleaving enzyme producing a transmembrane fragment, ηCTF that undergoes subsequent cleavages by α- and β-secretases yielding the Aηα and Aηβ peptides, respectively. The functions and contributions of ηCTF and its related fragments to AD pathology are poorly understood. In this study, we designed a novel immunological probe referred to as ηCTF-NTer antibody that specifically interacts with the N-terminal part of ηCTF targeting ηCTF, Aηα, Aηβ but not C99, C83 and Aβ. We examined the fate and localization of ηCTF fragment in various cell models and in mice. We found that overexpressed ηCTF undergoes degradation in the proteasomal and autophagic pathways and accumulates mainly in the Golgi and in endosomes. Moreover, we observed the presence of ηCTF in small extracellular vesicles purified from neuroblastoma cells or from mouse brains expressing ηCTF. Importantly, the expression of ηCTF in fibroblasts devoid on APP leads to Aβ production demonstrating its contribution to the amyloidogenic pathway. Finally, we observed an ηCTF-like immunoreactivity around amyloid plaques and an age-dependent accumulation of ηCTF in the triple-transgenic mouse AD model. Thus, our study suggests that the ηCTF fragment likely contributes to AD pathology by its exosomal spreading and involvement in Aβ production.
Keywords	amyloid ; antibodies ; endosomes ; etiology ; fibroblasts ; immune response ; metalloproteinases ; mice ; models ; peptides
Language	English
Dates of publication	2023-04
Size	p. 97.
Publishing place	Springer International Publishing
Document type	Article ; Online
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-023-04737-4
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Ryanodine receptors: dual contribution to Alzheimer disease?

Chami, Mounia / Checler, Frédéric

Channels (Austin, Tex.)

2014 Volume 8, Issue 3, Page(s) 168

MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Animals ; Humans ; Ryanodine Receptor Calcium Release Channel/genetics ; Ryanodine Receptor Calcium Release Channel/metabolism
Chemical Substances	Ryanodine Receptor Calcium Release Channel
Language	English
Publishing date	2014-09-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	2262854-X
ISSN	1933-6969 ; 1933-6969
ISSN (online)	1933-6969
ISSN	1933-6969
DOI	10.4161/chan.29000
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Article ; Online: Modifications of the endosomal compartment in fibroblasts from sporadic Alzheimer's disease patients are associated with cognitive impairment.

Xicota, Laura / Lagarde, Julien / Eysert, Fanny / Grenier-Boley, Benjamin / Rivals, Isabelle / Botté, Alexandra / Forlani, Sylvie / Landron, Sophie / Gautier, Clément / Gabriel, Cecilia / Bottlaender, Michel / Lambert, Jean-Charles / Chami, Mounia / Sarazin, Marie / Potier, Marie-Claude

Translational psychiatry

2023 Volume 13, Issue 1, Page(s) 54

Abstract: Morphological alterations of the endosomal compartment have been widely described in post-mortem brains from Alzheimer's disease (AD) patients and subjects with Down syndrome (DS) who are at high risk for AD. Immunostaining with antibodies against ... ...

Abstract	Morphological alterations of the endosomal compartment have been widely described in post-mortem brains from Alzheimer's disease (AD) patients and subjects with Down syndrome (DS) who are at high risk for AD. Immunostaining with antibodies against endosomal markers such as Early Endosome Antigen 1 (EEA1) revealed increased size of EEA1-positive puncta. In DS, peripheral cells such as peripheral blood mononuclear cells (PBMCs) and fibroblasts, share similar phenotype even in the absence of AD. We previously found that PBMCs from AD patients have larger EEA1-positive puncta, correlating with brain amyloid load. Here we analysed the endosomal compartment of fibroblasts from a very well characterised cohort of AD patients (IMABio3) who underwent thorough clinical, imaging and biomarkers assessments. Twenty-one subjects were included (7 AD with mild cognitive impairment (AD-MCI), 7 AD with dementia (AD-D) and 7 controls) who had amyloid-PET at baseline (PiB) and neuropsychological tests at baseline and close to skin biopsy. Fibroblasts isolated from skin biopsies were immunostained with anti-EEA1 antibody and imaged using a spinning disk microscope. Endosomal compartment ultrastructure was also analysed by electron microscopy. All fibroblast lines were genotyped and their AD risk factors identified. Our results show a trend to an increased EEA1-positive puncta volume in fibroblasts from AD-D as compared to controls (p.adj = 0.12) and reveal enhanced endosome area in fibroblasts from AD-MCI and AD-AD versus controls. Larger puncta size correlated with PiB retention in different brain areas and with worse cognitive scores at the time of biopsy as well as faster decline from baseline to the time of biopsy. Finally, we identified three genetic risk factors for AD (ABCA1, COX7C and MYO15A) that were associated with larger EEA1 puncta volume. In conclusion, the endosomal compartment in fibroblasts could be used as cellular peripheral biomarker for both amyloid deposition and cognitive decline in AD patients.
MeSH term(s)	Humans ; Alzheimer Disease ; Amyloid ; Amyloid beta-Peptides ; Cognitive Dysfunction ; Endosomes/pathology ; Fibroblasts ; Leukocytes, Mononuclear ; Positron-Emission Tomography
Chemical Substances	Amyloid ; Amyloid beta-Peptides
Language	English
Publishing date	2023-02-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2609311-X
ISSN	2158-3188 ; 2158-3188
ISSN (online)	2158-3188
ISSN	2158-3188
DOI	10.1038/s41398-023-02355-z
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Article ; Online: The η-secretase-derived APP fragment ηCTF is localized in Golgi, endosomes and extracellular vesicles and contributes to Aβ production.

Afram, Elissa / Lauritzen, Inger / Bourgeois, Alexandre / El Manaa, Wejdane / Duplan, Eric / Chami, Mounia / Valverde, Audrey / Charlotte, Bauer / Pardossi-Piquard, Raphaëlle / Checler, Frederic

Cellular and molecular life sciences : CMLS

2023 Volume 80, Issue 4, Page(s) 97

Abstract: The processing of the amyloid precursor protein (APP) is one of the key events contributing to Alzheimer's disease (AD) etiology. Canonical cleavages by β- and γ-secretases lead to Aβ production which accumulate in amyloid plaques. Recently, the matrix ... ...

Abstract	The processing of the amyloid precursor protein (APP) is one of the key events contributing to Alzheimer's disease (AD) etiology. Canonical cleavages by β- and γ-secretases lead to Aβ production which accumulate in amyloid plaques. Recently, the matrix metalloprotease MT5-MMP, referred to as η-secretase, has been identified as a novel APP cleaving enzyme producing a transmembrane fragment, ηCTF that undergoes subsequent cleavages by α- and β-secretases yielding the Aηα and Aηβ peptides, respectively. The functions and contributions of ηCTF and its related fragments to AD pathology are poorly understood. In this study, we designed a novel immunological probe referred to as ηCTF-NTer antibody that specifically interacts with the N-terminal part of ηCTF targeting ηCTF, Aηα, Aηβ but not C99, C83 and Aβ. We examined the fate and localization of ηCTF fragment in various cell models and in mice. We found that overexpressed ηCTF undergoes degradation in the proteasomal and autophagic pathways and accumulates mainly in the Golgi and in endosomes. Moreover, we observed the presence of ηCTF in small extracellular vesicles purified from neuroblastoma cells or from mouse brains expressing ηCTF. Importantly, the expression of ηCTF in fibroblasts devoid on APP leads to Aβ production demonstrating its contribution to the amyloidogenic pathway. Finally, we observed an ηCTF-like immunoreactivity around amyloid plaques and an age-dependent accumulation of ηCTF in the triple-transgenic mouse AD model. Thus, our study suggests that the ηCTF fragment likely contributes to AD pathology by its exosomal spreading and involvement in Aβ production.
MeSH term(s)	Mice ; Animals ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Amyloid Precursor Protein Secretases/genetics ; Amyloid Precursor Protein Secretases/metabolism ; Plaque, Amyloid ; Alzheimer Disease/metabolism ; Mice, Transgenic ; Endosomes/metabolism ; Extracellular Vesicles/metabolism ; Amyloid beta-Peptides/metabolism
Chemical Substances	Amyloid beta-Protein Precursor ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; Amyloid beta-Peptides
Language	English
Publishing date	2023-03-17
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-023-04737-4
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Article ; Online: Molecular Dysfunctions of Mitochondria-Associated Membranes (MAMs) in Alzheimer's Disease.

Eysert, Fanny / Kinoshita, Paula Fernanda / Mary, Arnaud / Vaillant-Beuchot, Loan / Checler, Frédéric / Chami, Mounia

International journal of molecular sciences

2020 Volume 21, Issue 24

Abstract: Alzheimer's disease (AD) is a multifactorial neurodegenerative pathology characterized by a progressive decline of cognitive functions. Alteration of various signaling cascades affecting distinct subcellular compartment functions and their communication ... ...

Abstract	Alzheimer's disease (AD) is a multifactorial neurodegenerative pathology characterized by a progressive decline of cognitive functions. Alteration of various signaling cascades affecting distinct subcellular compartment functions and their communication likely contribute to AD progression. Among others, the alteration of the physical association between the endoplasmic reticulum (ER) and mitochondria, also reffered as mitochondria-associated membranes (MAMs), impacts various cellular housekeeping functions such as phospholipids-, glucose-, cholesterol-, and fatty-acid-metabolism, as well as calcium signaling, which are all altered in AD. Our review describes the physical and functional proteome crosstalk between the ER and mitochondria and highlights the contribution of distinct molecular components of MAMs to mitochondrial and ER dysfunctions in AD progression. We also discuss potential strategies targeting MAMs to improve mitochondria and ER functions in AD.
MeSH term(s)	Alzheimer Disease/metabolism ; Animals ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress/physiology ; Humans ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism
Language	English
Publishing date	2020-12-14
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21249521
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