Evidence map›Paper›PMID 14638864›Full record

ArticleThe Journal of cell biology2003

Loss of proteolytically processed filaggrin caused by epidermal deletion of Matriptase/MT-SP1.

Karin List, Roman Szabo, Philip W Wertz, Julie Segre, Christian C Haudenschild, Soo-Youl Kim, Thomas H Bugge

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

93 citing papers in PubMed, 210 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Frontiers in molecular biosciences · 2023
    Article
  7. Article
  8. Revisiting the Roles of Filaggrin in Atopic Dermatitis.International journal of molecular sciences · 2022
    Review
  9. The Discovery and Function of Filaggrin.International journal of molecular sciences · 2022
    Review
  10. Cracking the Skin Barrier: Liquid-Liquid Phase Separation Shines under the Skin.JID innovations : skin science from molecules to population health · 2021
    Review
  11. Review
  12. Skin barrier dysfunction and filaggrin.Archives of pharmacal research · 2021
    Review
  13. Article
  14. Mutations in ASPRV1 Cause Dominantly Inherited Ichthyosis.American journal of human genetics · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

33 more citing papers are in PubMed but not listed here.

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

7 authors at 5 institutions in 1 country.

Karin ListProteases and Tissue Remodeling Unit, Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA.
Roman Szabo
Philip W Wertz
Julie Segre
Christian C Haudenschild
Soo-Youl Kim
Thomas H Bugge
National Institute of Dental and Craniofacial Research · USAmerican Red Cross · USBurke Medical Research Institute · USNational Human Genome Research Institute · USUniversity of Iowa · US

Funding

Cell surface serine proteases in development, tissue repair, and malignancyZIADE000699 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI BUGGE, THOMAS H · 2009 to 2025
$34.1M
Gene-Environment Interactions at the Skin SurfaceZIAHG000180 · NHGRI · NATIONAL HUMAN GENOME RESEARCH INSTITUTE · PI SEGRE, JULIA ANGELA · 2009 to 2025
$29.6M
Serine Proteases In Remodeling Of The Extracellular MatrZ01DE000699 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI BUGGE, THOMAS H · 2000 to 2008
$3.2M
Transcriptional Regulation of Epidermal DifferentiationZ01HG000180 · NHGRI · NATIONAL HUMAN GENOME RESEARCH INSTITUTE · PI SEGRE, JULIA ANGELA · 2001 to 2008
$2.4M
6 · The paper itself

Abstract

Profilaggrin is a large epidermal polyprotein that is proteolytically processed during keratinocyte differentiation to release multiple filaggrin monomer units as well as a calcium-binding regulatory NH2-terminal filaggrin S-100 protein. We show that epidermal deficiency of the transmembrane serine protease Matriptase/MT-SP1 perturbs lipid matrix formation, cornified envelope morphogenesis, and stratum corneum desquamation. Surprisingly, proteomic analysis of Matriptase/MT-SP1-deficient epidermis revealed the selective loss of both proteolytically processed filaggrin monomer units and the NH2-terminal filaggrin S-100 regulatory protein. This was associated with a profound accumulation of profilaggrin and aberrant profilaggrin-processing products in the stratum corneum. The data identify keratinocyte Matriptase/MT-SP1 as an essential component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation.

Indexed as

AnimalsCell DifferentiationDehydrationEpidermisExtracellular MatrixFilaggrin ProteinsIchthyosisIntermediate Filament ProteinsKeratinocytesLipid MetabolismMembrane ProteinsMiceMice, KnockoutMicroscopy, ElectronPeptide HydrolasesPermeabilityFilaggrin ProteinsIntermediate Filament ProteinsmatriptaseMembrane ProteinsPeptide HydrolasesProtein PrecursorsS100 ProteinsSerine EndopeptidasesSt14 protein, mouseTrypsin

Identifiers

PMID14638864
PMCPMC2173680
OpenAlexW1999561220

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.