Evidence map›Paper›PMID 30153561›Full record

ArticleBiomaterials2018

An engineered, quantifiable in vitro model for analysing the effect of proteostasis-targeting drugs on tissue physical properties.

Sandra Loaiza, Silvia A Ferreira, Tamara M Chinn, Alex Kirby, Elena Tsolaki, Camilla Dondi, Katarzyna Parzych, Adam P Strange, Laurent Bozec, Sergio Bertazzo and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Biomaterials, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 36% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Systems level profiling of chemotherapy-induced stress resolution in cancer cells reveals druggable trade-offs.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 4 institutions in 3 countries.

Sandra LoaizaCancer Cell Protein Metabolism Group, Department of Medicine, Imperial College London, London W12 0NN, UK.
Silvia A FerreiraCentre for Craniofacial and Regenerative Biology, King's College London, London SE1 9RT, UK.
Tamara M ChinnCancer Cell Protein Metabolism Group, Department of Medicine, Imperial College London, London W12 0NN, UK; Centre for Craniofacial and Regenerative Biology, King's College London, London SE1 9RT, UK.
Alex KirbyDepartment of Medical Physics and Biomedical Engineering, University College London, London WC1E 6BT, UK.
Elena TsolakiDepartment of Medical Physics and Biomedical Engineering, University College London, London WC1E 6BT, UK.
Camilla DondiCentre for Craniofacial and Regenerative Biology, King's College London, London SE1 9RT, UK.
Katarzyna ParzychCancer Cell Protein Metabolism Group, Department of Medicine, Imperial College London, London W12 0NN, UK.
Adam P StrangeBiomaterials and Tissue Engineering, Eastman Dental Institute, University College London, London WC1X 8LD, UK.
Laurent BozecBiomaterials and Tissue Engineering, Eastman Dental Institute, University College London, London WC1X 8LD, UK; Faculty of Dentistry, University of Toronto, 124 Edward Street, Toronto, ON M5G 1G6, Canada.
Sergio BertazzoDepartment of Medical Physics and Biomedical Engineering, University College London, London WC1E 6BT, UK.
Martin A B HedegaardDepartment of Chemical Engineering, Biotechnology and Environmental Technology, University of Southern Denmark, 5230 Odense M, Denmark.
Eileen GentlemanCentre for Craniofacial and Regenerative Biology, King's College London, London SE1 9RT, UK. Electronic address: eileen.gentleman@kcl.ac.uk.
Holger W AunerCancer Cell Protein Metabolism Group, Department of Medicine, Imperial College London, London W12 0NN, UK. Electronic address: holger.auner04@imperial.ac.uk.
University College London · GBImperial College London · GBKing's College London · GBUniversity of Southern Denmark · DK

Funding

Cancer Research UK 15448Wellcome Trust
6 · The paper itself

Abstract

Cellular function depends on the maintenance of protein homeostasis (proteostasis) by regulated protein degradation. Chronic dysregulation of proteostasis is associated with neurodegenerative and age-related diseases, and drugs targeting components of the protein degradation apparatus are increasingly used in cancer therapies. However, as chronic imbalances rather than loss of function mediate their pathogenesis, research models that allow for the study of the complex effects of drugs on tissue properties in proteostasis-associated diseases are almost completely lacking. Here, to determine the functional effects of impaired proteostatic fine-tuning, we applied a combination of materials science characterisation techniques to a cell-derived, in vitro model of bone-like tissue formation in which we pharmacologically perturbed protein degradation. We show that low-level inhibition of VCP/p97 and the proteasome, two major components of the degradation machinery, have remarkably different effects on the bone-like material that human bone-marrow derived mesenchymal stromal cells (hMSC) form in vitro. Specifically, whilst proteasome inhibition mildly enhances tissue formation, Raman spectroscopic, atomic force microscopy-based indentation, and electron microscopy imaging reveal that VCP/p97 inhibition induces the formation of bone-like tissue that is softer, contains less protein, appears to have more crystalline mineral, and may involve aberrant micro- and ultra-structural tissue organisation. These observations contrast with findings from conventional osteogenic assays that failed to identify any effect on mineralisation. Taken together, these data suggest that mild proteostatic impairment in hMSC alters the bone-like material they form in ways that could explain some pathologies associated with VCP/p97-related diseases. They also demonstrate the utility of quantitative materials science approaches for tackling long-standing questions in biology and medicine, and could form the basis for preclinical drug testing platforms to develop therapies for diseases stemming from perturbed proteostasis or for cancer therapies targeting protein degradation. Our findings may also have important implications for the field of tissue engineering, as the manufacture of cell-derived biomaterial scaffolds may need to consider proteostasis to effectively replicate native tissues.

Indexed as

Biophysical PhenomenaBone RegenerationCell Culture TechniquesCell DifferentiationCell Line, TumorDrug DevelopmentHumansMesenchymal Stem CellsOsteoblastsProteasome Endopeptidase ComplexProteolysisProteostasisTissue EngineeringTissue ScaffoldsValosin Containing ProteinProteasome Endopeptidase ComplexValosin Containing ProteinVCP protein, humanAtomic force microscopyCancer diagnosis and therapyProteasomeProteostasisRaman spectroscopyVCP/p97

Identifiers

PMID30153561
PMCPMC6145445
OpenAlexW2885220361

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.