Evidence map›Paper›PMID 10993910›Full record

ArticleThe Journal of experimental medicine2000

Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages.

A Punturieri, S Filippov, E Allen, I Caras, R Murray, V Reddy, S J Weiss

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

68 citing papers in PubMed, 214 citations in OpenAlex.

  1. Trial
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  8. Reassessing enzyme kinetics: Considering protease-as-substrate interactions in proteolytic networks.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Review
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  12. Full-thickness rotator cuff tear in rat results in distinct temporal expression of multiple proteases in tendon, muscle, and cartilage.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2019
    Article
  13. Matrix metalloproteinases in emphysema.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Review
  14. Gadd153 deficiency attenuates abdominal aortic aneurysm formation in mice.International journal of clinical and experimental pathology · 2018
    Article
  15. Review
  16. Article
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  19. Article
  20. Article

8 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 1 institution in 1 country.

A PunturieriDepartment of Internal Medicine, University of Michigan, Ann Arbor, Michigan 48109, USA.
S Filippov
E Allen
I Caras
R Murray
V Reddy
S J Weiss
University of Michigan–Ann Arbor · US

Funding

HUMAN PHAGOCYTES, OXYGEN METABOLITES AND INFLAMMATIONR37AI021301 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WEISS, STEPHEN · 1993 to 2002
$758k
HUMAN PHAGOCYTES, OXYGEN METABOLITES, AND INFLAMMATIONR01AI021301 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WEISS, STEPHEN · 1985 to 1991
–
NIAID NIH HHS AI21301
6 · The paper itself

Abstract

Human macrophages mediate the dissolution of elastic lamina by mobilizing tissue-destructive cysteine proteinases. While macrophage-mediated elastin degradation has been linked to the expression of cathepsins L and S, these cells also express cathepsin K, a new member of the cysteine proteinase family whose elastinolytic potential exceeds that of all known elastases. To determine the relative role of cathepsin K in elastinolysis, monocytes were differentiated under conditions in which they recapitulated a gene expression profile similar to that observed at sites of tissue damage in vivo. After a 12-d culture period, monocyte-derived macrophages (MDMs) expressed cathepsin K in tandem with cathepsins L and S. Though cysteine proteinases are acidophilic and normally confined to the lysosomal network, MDMs secreted cathepsin K extracellularly in concert with cathepsins L and S. Simultaneously, MDMs increased the expression of vacuolar-type H(+)-ATPase components, acidified the pericellular milieu, and maintained extracellular cathepsin K in an active form. MDMs from a cathepsin K-deficient individual, however, retained the ability to express, process, and secrete cathepsins L and S, and displayed normal elastin-degrading activity. Thus, matrix-destructive MDMs exteriorize a complex mix of proteolytic cysteine proteinases, but maintain full elastinolytic potential in the absence of cathepsin K by mobilizing cathepsins L and S.

Indexed as

EndopeptidasesCathepsin BCathepsin DCathepsin KCathepsin LCathepsinsCell DifferentiationCells, CulturedCysteine EndopeptidasesGene Expression Regulation, EnzymologicHumansKineticsMacrophagesMonocytesProton-Translocating ATPasesTime FactorsCathepsin BCathepsin DCathepsin KCathepsin Lcathepsin SCathepsinsCTSK protein, humanCTSL protein, humanCysteine EndopeptidasesEndopeptidasesProton-Translocating ATPases

Identifiers

PMID10993910
PMCPMC2193285
OpenAlexW2118810030

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.