Evidence map›Paper›PMID 23233448›Full record

ArticleMolecular & cellular proteomics : MCP2013

Deletion of cysteine cathepsins B or L yields differential impacts on murine skin proteome and degradome.

Stefan Tholen, Martin L Biniossek, Martina Gansz, Alejandro Gomez-Auli, Fee Bengsch, Agnes Noel, Jayachandran N Kizhakkedathu, Melanie Boerries, Hauke Busch, Thomas Reinheckel and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
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  9. Matrix metalloproteinases in emphysema.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Review
  10. Cathepsin B as a potential cystatin M/E target in the mouse hair follicle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017
    Article
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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

11 authors at 3 institutions in 3 countries.

Stefan TholenInstitute of Molecular Medicine and Cell Research, University of Freiburg, Freiburg, Germany.
Martin L Biniossek
Martina Gansz
Alejandro Gomez-Auli
Fee Bengsch
Agnes Noel
Jayachandran N Kizhakkedathu
Melanie Boerries
Hauke Busch
Thomas Reinheckel
Oliver Schilling
University of Freiburg · DEUniversity of British Columbia · CAUniversity of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Numerous studies highlight the fact that concerted proteolysis is essential for skin morphology and function. The cysteine protease cathepsin L (Ctsl) has been implicated in epidermal proliferation and desquamation, as well as in hair cycle regulation. In stark contrast, mice deficient in cathepsin B (Ctsb) do not display an overt skin phenotype. To understand the systematic consequences of deleting Ctsb or Ctsl, we determined the protein abundances of >1300 proteins and proteolytic cleavage events in skin samples of wild-type, Ctsb(-/-), and Ctsl(-/-) mice via mass-spectrometry-based proteomics. Both protease deficiencies revealed distinct quantitative changes in proteome composition. Ctsl(-/-) skin revealed increased levels of the cysteine protease inhibitors cystatin B and cystatin M/E, increased cathepsin D, and an accumulation of the extracellular glycoprotein periostin. Immunohistochemistry located periostin predominantly in the hypodermal connective tissue of Ctsl(-/-) skin. The proteomic identification of proteolytic cleavage sites within skin proteins revealed numerous processing sites that are underrepresented in Ctsl(-/-) or Ctsb(-/-) samples. Notably, few of the affected cleavage sites shared the canonical Ctsl or Ctsb specificity, providing further evidence of a complex proteolytic network in the skin. Novel processing sites in proteins such as dermokine and Notch-1 were detected. Simultaneous analysis of acetylated protein N termini showed prototypical mammalian N-alpha acetylation. These results illustrate an influence of both Ctsb and Ctsl on the murine skin proteome and degradome, with the phenotypic consequences of the absence of either protease differing considerably.

Indexed as

AnimalsBlotting, WesternCathepsin BCathepsin LCell Adhesion MoleculesCells, CulturedChromatography, LiquidCystatin BCystatin MImmunohistochemistryMiceMice, KnockoutPeptidesProteolysisProteomeProteomicsCathepsin BCathepsin LCell Adhesion MoleculesCtsb protein, mouseCtsl protein, mouseCystatin BCystatin MPeptidesPostn protein, mouseProteomeReceptor, Notch1Serpins

Identifiers

PMID23233448
PMCPMC3591655
OpenAlexW1978887710

What OpenQuestion holds

Textmetadata
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.