Evidence map›Paper›PMID 12782676›Full record

ArticleThe Journal of clinical investigation2003

Thyroid functions of mouse cathepsins B, K, and L.

Bianca Friedrichs, Carmen Tepel, Thomas Reinheckel, Jan Deussing, Kurt von Figura, Volker Herzog, Christoph Peters, Paul Saftig, Klaudia Brix

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

81 citing papers in PubMed, 220 citations in OpenAlex.

  1. Article
  2. Review
  3. Substrate for Thyroid Hormone Synthesis: Biochemistry, Evolution, and Physiology.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. The role of primary cilia in thyroid diseases.Frontiers in endocrinology · 2023
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Structure determinants defining the specificity of papain-like cysteine proteases.Computational and structural biotechnology journal · 2022
    Review
  18. Review
  19. Article
  20. Article

21 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

9 authors at 5 institutions in 1 country.

Bianca FriedrichsInstitut für Zellbiologie and Bonner Forum Biomedizin, Universität Bonn, Bonn, Germany.
Carmen Tepel
Thomas Reinheckel
Jan Deussing
Kurt von Figura
Volker Herzog
Christoph Peters
Paul Saftig
Klaudia Brix
University Medical Center Freiburg · DEUniversity of Bonn · DEConstructor University · DEGTT-Technologies (Germany) · DEKiel University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thyroid function depends on processing of the prohormone thyroglobulin by sequential proteolytic events. From in vitro analysis it is known that cysteine proteinases mediate proteolytic processing of thyroglobulin. Here, we have analyzed mice with deficiencies in cathepsins B, K, L, B and K, or K and L in order to investigate which of the cysteine proteinases is most important for proteolytic processing of thyroglobulin in vivo. Immunolabeling demonstrated a rearrangement of the endocytic system and a redistribution of extracellularly located enzymes in thyroids of cathepsin-deficient mice. Cathepsin L was upregulated in thyroids of cathepsin K(-/-) or B(-/-)/K(-/-) mice, suggesting a compensation of cathepsin L for cathepsin K deficiency. Impaired proteolysis resulted in the persistence of thyroglobulin in the thyroids of mice with deficiencies in cathepsin B or L. The typical multilayered appearance of extracellularly stored thyroglobulin was retained in cathepsin K(-/-) mice only. These results suggest that cathepsins B and L are involved in the solubilization of thyroglobulin from its covalently cross-linked storage form. Cathepsin K(-/-)/L(-/-) mice had significantly reduced levels of free thyroxine, indicating that utilization of luminal thyroglobulin for thyroxine liberation is mediated by a combinatory action of cathepsins K and L.

Indexed as

AnimalsCathepsin BCathepsin KCathepsin LCathepsinsCysteine EndopeptidasesEndocytosisGenotypeMiceMice, Inbred C57BLMice, TransgenicMicroscopy, ConfocalModels, BiologicalMutationThyroglobulinThyroid GlandCathepsin BCathepsin KCathepsin LCathepsinsCtsk protein, mouseCtsl protein, mouseCysteine EndopeptidasesThyroglobulinThyroxine

Identifiers

PMID12782676
PMCPMC156100
OpenAlexW2083578935

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.