Evidence map›Paper›PMID 10390548›Full record

ArticleMolecular medicine (Cambridge, Mass.)1999

Inflammatory mediators regulate cathepsin S in macrophages and microglia: A role in attenuating heparan sulfate interactions.

J P Liuzzo, S S Petanceska, D Moscatelli, L A Devi

Open access · bronzeAbstract read
In one paragraph

Article in Molecular medicine (Cambridge, Mass.), 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

34 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Effects of Cathepsin S Inhibition in the Age-Related Dry Eye Phenotype.Investigative ophthalmology & visual science · 2023
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Observational
  12. Review
  13. Glycosaminoglycan Neutralization in Coagulation Control.Arteriosclerosis, thrombosis, and vascular biology · 2018
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article
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

4 authors at 2 institutions in 1 country.

J P LiuzzoDepartment of Pharmacology, Kaplan Cancer Center, New York University School of Medicine, New York, New York, USA.
S S Petanceska
D Moscatelli
L A Devi
New York University · USNathan Kline Institute for Psychiatric Research · US

Funding

NINDS NIH HHS NS 26880NINDS NIH HHS NS K04 1788
6 · The paper itself

Abstract

backgroundCathepsin S is a member of the family of cysteine lysosomal proteases. The distribution of cathepsin S is restricted to cells from the mononuclear lineage both in the brain and in the periphery. Also, its protease activity is uniquely stable at neutral pH. MATERIALS AND

methodsWe compared the expression of cathepsin S, B, and L mRNAs in various undifferentiated and differentiated cells of mononuclear origin, and examined the modulation of these mRNAs by inflammatory mediators (lipopolysaccharide and various cytokines). In addition, the effect of these agents on cathepsin S protein levels and protease activity was also determined. Lastly, the ability of cathepsin S to process basement membrane components such as heparan sulfate proteoglycans in vitro and in vivo was assessed.

resultsCathepsin S, B, and L mRNAs are expressed in mature macrophages and microglial cells and not in undifferentiated monocytes. Activators of macrophages negatively regulate all three transcripts. Consistent with this, treatment with these agents leads to a decrease in intracellular cathepsin S protein levels and activity. However, the same treatments result in stimulation of secreted cathepsin S activity. Cathepsin S is capable of degrading heparan sulfate proteoglycans in vitro. Also, when expressed in endothelial cells, cathepsin S autocrinely attenuates the basic fibroblast growth factor (bFGF)-mediated binding of FGF receptor containing cells to endothelial cells, by acting on basement membrane proteoglycans.

conclusionsTaken together, these data imply that cathepsin S is a regulatable cysteine protease that plays a role in the degradation of extracellular proteins, whose secretion from macrophages and microglia is increased by signals that lead to activation of these cells, and may be important in regulating extracellular matrix interactions. http://link.springer-ny. com/link/service/journals/00020/bibs/5n5p320.html

Indexed as

EndopeptidasesHeparan Sulfate ProteoglycansAnimalsBlotting, NorthernBlotting, WesternCathepsin BCathepsin LCathepsinsCell AdhesionCell LineCysteine EndopeptidasesCysteine Proteinase InhibitorsFibroblast Growth Factor 2Granulocyte-Macrophage Colony-Stimulating FactorHeparan SulfateInflammationCathepsin BCathepsin Lcathepsin SCathepsinsCtsl protein, mouseCysteine EndopeptidasesCysteine Proteinase InhibitorsE 64EndopeptidasesFibroblast Growth Factor 2Granulocyte-Macrophage Colony-Stimulating FactorHeparan SulfateHeparan Sulfate ProteoglycansInterferon-alphaInterferon-gammaInterleukin-1LeucineLipopolysaccharidesperlecanProteoglycansRNA, MessengerTumor Necrosis Factor-alpha

Identifiers

PMID10390548
PMCPMC2230418
OpenAlexW1573783797

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.