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Synaptic mitochondrial dysfunction and septin accumulation are linked to complement-mediated synapse loss in an Alzheimer’s disease animal model
Györffy, B.A. [Györffy, Balázs (Neurobiológia), author] ELTE TTK BI Proteomikai Csoport (ELTE / ELU FoS / Bio_I); MTA-ELTE-NAP B Neuroimmunology Research Group (ELTE / ELU FoS / Bio_I)
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Tóth, V. [Tóth, Vilmos (Molekuláris biológia), author]
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Török, G. [Török, György (Biofizika, Sejt- ...), author] Departmnet of Biophysics and Radiation Biology (SU / FM / I); Enzim_412 (IMLS)
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Gulyássy, P.
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Kovács, Réka [Kovács, Réka (Neuroimmunológia), author]
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Vadászi, H. [Vadászi, Henrietta (kémia), author] Department of Biochemistry (ELTE / ELU FoS / Bio_I)
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Micsonai, András [Micsonai, András (biokémia), author] Department of Biochemistry (ELTE / ELU FoS / Bio_I); MTA-ELTE-NAP B Neuroimmunology Research Group (ELTE / ELU FoS / Bio_I)
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Tóth, M.E. [Tóth, Erzsébet Melinda (biokémia), author] Institute of Biochemistry
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Sántha, M. [Sántha, Miklós (Neurobiológia és ...), author] Institute of Biochemistry
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Homolya, L. [Homolya, László (Molekuláris sejtb...), author] Institute of Enzymology (RCNS); Enzim_412 (IMLS)
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Drahos, L. [Drahos, László (proteomika, tömeg...), author] Institute of Organic Chemistry (MTA TTK)
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Juhász, G. [Juhász, Gábor Dénes (Élettan, neurokém...), author] ELTE TTK BI Proteomikai Csoport (ELTE / ELU FoS / Bio_I)
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Kékesi, K.A.** [Kékesi, Adrienna Katalin (Élettan, neurokém...), author] Department of Physiology and Neurobiology (ELTE / ELU FoS / Bio_I); ELTE TTK BI Proteomikai Csoport (ELTE / ELU FoS / Bio_I)
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Kardos, J. ✉ [Kardos, József (Biológia), author] Department of Biochemistry (ELTE / ELU FoS / Bio_I); MTA-ELTE-NAP B Neuroimmunology Research Group (ELTE / ELU FoS / Bio_I)
English Article (Journal Article) Scientific
Published:
CELLULAR AND MOLECULAR LIFE SCIENCES 1420-682X 1420-9071
77
(24)
pp. 5243-5258
2020
SJR Scopus - Molecular Medicine: D1
Identifiers
MTMT: 31177389
DOI:
10.1007/s00018-020-03468-0
WoS:
000515946800001
REAL:
115004
Scopus:
85078960985
PubMed:
32034429
Fundings:
(FIEK_16-1-2016-0005)
Subjects:
Pharmaceutical chemistry
Synaptic functional disturbances with concomitant synapse loss represent central pathological hallmarks of Alzheimer’s disease. Excessive accumulation of cytotoxic amyloid oligomers is widely recognized as a key event that underlies neurodegeneration. Certain complement components are crucial instruments of widespread synapse loss because they can tag synapses with functional impairments leading to their engulfment by microglia. However, an exact understanding of the affected synaptic functions that predispose to complement-mediated synapse elimination is lacking. Therefore, we conducted systematic proteomic examinations on synaptosomes prepared from an amyloidogenic mouse model of Alzheimer’s disease (APP/PS1). Synaptic fractions were separated according to the presence of the C1q-tag using fluorescence-activated synaptosome sorting and subjected to proteomic comparisons. The results raised the decline of mitochondrial functions in the C1q-tagged synapses of APP/PS1 mice based on enrichment analyses, which was verified using flow cytometry. Additionally, proteomics results revealed extensive alterations in the level of septin protein family members, which are known to dynamically form highly organized pre- and postsynaptic supramolecular structures, thereby affecting synaptic transmission. High-resolution microscopy investigations demonstrated that synapses with considerable amounts of septin-3 and septin-5 show increased accumulation of C1q in APP/PS1 mice compared to the wild-type ones. Moreover, a strong positive correlation was apparent between synaptic septin-3 levels and C1q deposition as revealed via flow cytometry and confocal microscopy examinations. In sum, our results imply that deterioration of synaptic mitochondrial functions and alterations in the organization of synaptic septins are associated with complement-dependent synapse loss in Alzheimer’s disease. © 2020, The Author(s).
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2025-04-26 01:49
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