Sorcin is an early marker of neurodegeneration, Ca


Journal

Cell death & disease
ISSN: 2041-4889
Titre abrégé: Cell Death Dis
Pays: England
ID NLM: 101524092

Informations de publication

Date de publication:
15 10 2020
Historique:
received: 02 12 2019
accepted: 18 09 2020
revised: 16 09 2020
entrez: 16 10 2020
pubmed: 17 10 2020
medline: 14 5 2021
Statut: epublish

Résumé

Dysregulation of calcium signaling is emerging as a key feature in the pathogenesis of neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), and Huntington's disease (HD), and targeting this process may be therapeutically beneficial. Under this perspective, it is important to study proteins that regulate calcium homeostasis in the cell. Sorcin is one of the most expressed calcium-binding proteins in the human brain; its overexpression increases endoplasmic reticulum (ER) calcium concentration and decreases ER stress in the heart and in other cellular types. Sorcin has been hypothesized to be involved in neurodegenerative diseases, since it may counteract the increased cytosolic calcium levels associated with neurodegeneration. In the present work, we show that Sorcin expression levels are strongly increased in cellular, animal, and human models of AD, PD, and HD, vs. normal cells. Sorcin partially colocalizes with RyRs in neurons and microglia cells; functional experiments with microsomes containing high amounts of RyR2 and RyR3, respectively, show that Sorcin is able to regulate these ER calcium channels. The molecular basis of the interaction of Sorcin with RyR2 and RyR3 is demonstrated by SPR. Sorcin also interacts with other ER proteins as SERCA2 and Sigma-1 receptor in a calcium-dependent fashion. We also show that Sorcin regulates ER calcium transients: Sorcin increases the velocity of ER calcium uptake (increasing SERCA activity). The data presented here demonstrate that Sorcin may represent both a novel early marker of neurodegenerative diseases and a response to cellular stress dependent on neurodegeneration.

Identifiants

pubmed: 33060591
doi: 10.1038/s41419-020-03063-y
pii: 10.1038/s41419-020-03063-y
pmc: PMC7566454
doi:

Substances chimiques

Biomarkers, Tumor 0
Calcium-Binding Proteins 0
RYR1 protein, human 0
RYR3 protein, human 0
RyR2 protein, human 0
Ryanodine Receptor Calcium Release Channel 0
SRI protein, human 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

861

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Auteurs

Ilaria Genovese (I)

Department of Medical Sciences, Laboratory for Technology of Advanced Therapies (LTTA) University of Ferrara, Ferrara, Italy.

Flavia Giamogante (F)

Department of Biomedical Sciences, University of Padova, Padova, Italy.
Padova Neuroscience Center (PNC), University of Padova, Padova, Italy.

Lucia Barazzuol (L)

Department of Biomedical Sciences, University of Padova, Padova, Italy.
Padova Neuroscience Center (PNC), University of Padova, Padova, Italy.

Theo Battista (T)

Department of Biochemical Sciences "A. Rossi Fanelli", University Sapienza of Rome, Rome, Italy.

Annarita Fiorillo (A)

Department of Biochemical Sciences "A. Rossi Fanelli", University Sapienza of Rome, Rome, Italy.

Mattia Vicario (M)

Department of Biomedical Sciences, University of Padova, Padova, Italy.

Giuseppina D'Alessandro (G)

Department of Physiology and Pharmacology, University of Rome "Sapienza", Rome, Italy.
IRCCS Neuromed, Pozzilli, Isernia, Italy.

Raffaela Cipriani (R)

Department of Physiology and Pharmacology, University of Rome "Sapienza", Rome, Italy.

Cristina Limatola (C)

IRCCS Neuromed, Pozzilli, Isernia, Italy.
Department of Physiology and Pharmacology, Sapienza University, Laboratory Affiliated to Istituto Pasteur Italia - Rome, Rome, Italy.

Daniela Rossi (D)

Department of Molecular and Developmental Medicine, University of Siena, Siena, Italy.

Vincenzo Sorrentino (V)

Department of Molecular and Developmental Medicine, University of Siena, Siena, Italy.

Elena Poser (E)

Department of Biochemistry, University of Oxford, Oxford, UK.

Luciana Mosca (L)

Department of Biochemical Sciences "A. Rossi Fanelli", University Sapienza of Rome, Rome, Italy.

Ferdinando Squitieri (F)

Huntington's and Rare Diseases Unit, IRCCS Ospedale Casa Sollievo della Sofferenza, Rome, Italy.

Marzia Perluigi (M)

Department of Biochemical Sciences "A. Rossi Fanelli", University Sapienza of Rome, Rome, Italy.

Andrea Arena (A)

Department of Biochemical Sciences "A. Rossi Fanelli", University Sapienza of Rome, Rome, Italy.

Filip van Petegem (F)

Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of British Columbia, Vancouver, Canada.

Claudia Tito (C)

Department of Anatomical, Histological, Forensic & Orthopedic Sciences, Section of Histology & Medical Embryology, Sapienza University of Rome, Laboratory affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, Rome, Italy.

Francesco Fazi (F)

Department of Anatomical, Histological, Forensic & Orthopedic Sciences, Section of Histology & Medical Embryology, Sapienza University of Rome, Laboratory affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, Rome, Italy.

Carlotta Giorgi (C)

Department of Medical Sciences, Laboratory for Technology of Advanced Therapies (LTTA) University of Ferrara, Ferrara, Italy.

Tito Calì (T)

Department of Biomedical Sciences, University of Padova, Padova, Italy.
Padova Neuroscience Center (PNC), University of Padova, Padova, Italy.

Andrea Ilari (A)

Institute of Molecular Biology and Pathology, Italian National Research Council, IBPM-CNR, Rome, Italy. andrea.ilari@cnr.it.

Gianni Colotti (G)

Institute of Molecular Biology and Pathology, Italian National Research Council, IBPM-CNR, Rome, Italy. gianni.colotti@cnr.it.

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