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Record W3152885207 · doi:10.1101/2021.04.19.440495

Ligands binding to the cellular prion protein induce its protective proteolytic release with therapeutic potential in neurodegenerative proteinopathies

2021· preprint· en· W3152885207 on OpenAlexaff
Luise Linsenmeier, Behnam Mohammadi, Mohsin Shafiq, Karl Frontzek, Julia Bär, Amulya Nidhi Shrivastava, Markus Daμμe, Alexander Schwarz, Stefano Da Vela, Tania Massignan, Sebastian Jung, Angela da Silva Correia, Matthias Schmitz, Berta Puig, Simone Hornemann, Inga Zerr, Jörg Tatzelt, Emiliano Biasini, Paul Säftig, Michaela Schweizer, Dmitri I. Svergun, Ladan Amin, Federica Mazzola, Luca Varani, Simrika Thapa, Sabine Gilch, Hermann Schätzl, David A. Harris, Antoine Triller, Marina Mikhaylova, Adriano Aguzzi, Hermann C. Altmeppen, Markus Glatzel

Bibliographic record

VenuebioRxiv (Cold Spring Harbor Laboratory) · 2021
Typepreprint
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicPrion Diseases and Protein Misfolding
Canadian institutionsUniversity of Calgary
FundersUniversity of California, San FranciscoNational Institutes of HealthUniversità degli Studi di TrentoWerner Otto StiftungDeutsche ForschungsgemeinschaftLudwig-Maximilians-Universität MünchenAlzheimer Forschung InitiativeJoachim Herz Stiftung
KeywordsInternalizationNeuroprotectionCell biologyProteolysisNeurodegenerationMetalloproteinaseEndocytosisNeurotoxicityADAM10ChemistryBiologyAmyloid (mycology)CellBiochemistryMatrix metalloproteinaseNeuroscienceDiseaseDisintegrinMedicineEnzymePathologyToxicity

Abstract

fetched live from OpenAlex

Abstract The cellular prion protein (PrP C ) is a central player in neurodegenerative diseases caused by protein misfolding, such as prion diseases or Alzheimer’s disease (AD). Expression levels of this GPI-anchored glycoprotein, especially at the neuronal cell surface, critically correlate with various pathomechanistic aspects underlying these diseases, such as templated misfolding (in prion diseases) and neurotoxicity and, hence, with disease progression and severity. In stark contrast to cell-associated PrP C , soluble extracellular forms or fragments of PrP are linked with neuroprotective effects, which is likely due to their ability to interfere with neurotoxic disease-associated protein conformers in the interstitial fluid. Fittingly, the endogenous proteolytic release of PrP C by the metalloprotease ADAM10 (‘shedding’) was characterized as a protective mechanism. Here, using a recently generated cleavage-site specific antibody, we shed new light on earlier studies by demonstrating that shed PrP (sPrP) negatively correlates with conformational conversion (in prion disease) and is markedly redistributed in murine brain in the presence of prion deposits or AD-associated amyloid plaques indicating a blocking and sequestrating activity. Importantly, we reveal that administration of certain PrP-directed antibodies and other ligands results in increased PrP shedding in cells and organotypic brain slice cultures. We also provide mechanistic and structural insight into this shedding-stimulating effect. In addition, we identified a striking exception to this, as one particular neuroprotective antibody, due to its special binding characteristics, did not cause increased shedding but rather strong surface clustering followed by fast endocytosis and degradation of PrP C . Both mechanisms may contribute to the beneficial action described for some PrP-directed antibodies/ligands and pave the way for new therapeutic strategies against devastating and currently incurable neurodegenerative diseases.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame machine prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: metacan-v3-hybrid-931329e0061cValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.001
Threshold uncertainty score0.003

Distilled classifier scores by category (both heads)

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0010.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.009
GPT teacher head0.207
Teacher spread0.197 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations0
Published2021
Admission routes1
Has abstractyes

Explore more

Same venuebioRxiv (Cold Spring Harbor Laboratory)→Same topicPrion Diseases and Protein Misfolding→French-language works237,207→