The Alzheimer's disease-linked protease BACE1 modulates neuronal IL-6 signaling through shedding of the receptor gp130.


Journal

Molecular neurodegeneration
ISSN: 1750-1326
Titre abrégé: Mol Neurodegener
Pays: England
ID NLM: 101266600

Informations de publication

Date de publication:
21 02 2023
Historique:
received: 09 08 2022
accepted: 11 01 2023
entrez: 22 2 2023
pubmed: 23 2 2023
medline: 25 2 2023
Statut: epublish

Résumé

The protease BACE1 is a major drug target for Alzheimer's disease, but chronic BACE1 inhibition is associated with non-progressive cognitive worsening that may be caused by modulation of unknown physiological BACE1 substrates. To identify in vivo-relevant BACE1 substrates, we applied pharmacoproteomics to non-human-primate cerebrospinal fluid (CSF) after acute treatment with BACE inhibitors. Besides SEZ6, the strongest, dose-dependent reduction was observed for the pro-inflammatory cytokine receptor gp130/IL6ST, which we establish as an in vivo BACE1 substrate. Gp130 was also reduced in human CSF from a clinical trial with a BACE inhibitor and in plasma of BACE1-deficient mice. Mechanistically, we demonstrate that BACE1 directly cleaves gp130, thereby attenuating membrane-bound gp130 and increasing soluble gp130 abundance and controlling gp130 function in neuronal IL-6 signaling and neuronal survival upon growth-factor withdrawal. BACE1 is a new modulator of gp130 function. The BACE1-cleaved, soluble gp130 may serve as a pharmacodynamic BACE1 activity marker to reduce the occurrence of side effects of chronic BACE1 inhibition in humans.

Sections du résumé

BACKGROUND
The protease BACE1 is a major drug target for Alzheimer's disease, but chronic BACE1 inhibition is associated with non-progressive cognitive worsening that may be caused by modulation of unknown physiological BACE1 substrates.
METHODS
To identify in vivo-relevant BACE1 substrates, we applied pharmacoproteomics to non-human-primate cerebrospinal fluid (CSF) after acute treatment with BACE inhibitors.
RESULTS
Besides SEZ6, the strongest, dose-dependent reduction was observed for the pro-inflammatory cytokine receptor gp130/IL6ST, which we establish as an in vivo BACE1 substrate. Gp130 was also reduced in human CSF from a clinical trial with a BACE inhibitor and in plasma of BACE1-deficient mice. Mechanistically, we demonstrate that BACE1 directly cleaves gp130, thereby attenuating membrane-bound gp130 and increasing soluble gp130 abundance and controlling gp130 function in neuronal IL-6 signaling and neuronal survival upon growth-factor withdrawal.
CONCLUSION
BACE1 is a new modulator of gp130 function. The BACE1-cleaved, soluble gp130 may serve as a pharmacodynamic BACE1 activity marker to reduce the occurrence of side effects of chronic BACE1 inhibition in humans.

Identifiants

pubmed: 36810097
doi: 10.1186/s13024-023-00596-6
pii: 10.1186/s13024-023-00596-6
pmc: PMC9942414
doi:

Substances chimiques

Amyloid Precursor Protein Secretases EC 3.4.-
Cytokine Receptor gp130 133483-10-0
Aspartic Acid Endopeptidases EC 3.4.23.-
Interleukin-6 0
BACE1 protein, human EC 3.4.23.46
Sez6 protein, mouse 0
Nerve Tissue Proteins 0
Bace1 protein, mouse EC 3.4.23.46

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

13

Informations de copyright

© 2023. The Author(s).

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Auteurs

Stephan A Müller (SA)

German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.
Neuroproteomics, School of Medicine, Klinikum rechts der Isar, Technical University of Munich, Munich, Germany.

Merav D Shmueli (MD)

German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.
Neuroproteomics, School of Medicine, Klinikum rechts der Isar, Technical University of Munich, Munich, Germany.

Xiao Feng (X)

German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.
Neuroproteomics, School of Medicine, Klinikum rechts der Isar, Technical University of Munich, Munich, Germany.

Johanna Tüshaus (J)

German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.
Neuroproteomics, School of Medicine, Klinikum rechts der Isar, Technical University of Munich, Munich, Germany.

Neele Schumacher (N)

Biochemical Institute, Kiel University, Kiel, Germany.

Ryan Clark (R)

Neuroscience, Merck & Co. Inc., Boston, MA, USA.

Brad E Smith (BE)

Laboratory Animal Resources, Merck & Co. Inc., West Point, PA, USA.

An Chi (A)

Chemical Biology, Merck & Co. Inc., Boston, MA, USA.

Stefan Rose-John (S)

Biochemical Institute, Kiel University, Kiel, Germany.

Matthew E Kennedy (ME)

Neuroscience, Merck & Co. Inc., Boston, MA, USA.

Stefan F Lichtenthaler (SF)

German Center for Neurodegenerative Diseases (DZNE), Munich, Germany. stefan.lichtenthaler@dzne.de.
Neuroproteomics, School of Medicine, Klinikum rechts der Isar, Technical University of Munich, Munich, Germany. stefan.lichtenthaler@dzne.de.
Munich Cluster for Systems Neurology (SyNergy), Munich, Germany. stefan.lichtenthaler@dzne.de.

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