Evidence map›Paper›PMID 16436681›Full record

ArticleThe American journal of pathology2006

Localization of cysteine protease, cathepsin S, to the surface of vascular smooth muscle cells by association with integrin alphanubeta3.

Xian Wu Cheng, Masafumi Kuzuya, Kae Nakamura, Qun Di, Zexuan Liu, Takeshi Sasaki, Shigeru Kanda, Hai Jin, Guo-Ping Shi, Toyoaki Murohara and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The American journal of pathology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Rac1 inhibition protects the kidney against kidney ischemia/reperfusion through the inhibition of macrophage migration.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Cysteinyl cathepsins in cardiovascular diseases.Biochimica et biophysica acta. Proteins and proteomics · 2020
    Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Cysteine Protease Cathepsins in Atherosclerotic Cardiovascular Diseases.Journal of atherosclerosis and thrombosis · 2018
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

12 authors at 3 institutions in 3 countries.

Xian Wu ChengDepartment of Geriatrics, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan.
Masafumi Kuzuya
Kae Nakamura
Qun Di
Zexuan Liu
Takeshi Sasaki
Shigeru Kanda
Hai Jin
Guo-Ping Shi
Toyoaki Murohara
Mitsuhiro Yokota
Akihisa Iguchi
Nagoya University · JPYanbian University · CNHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Smooth muscle cell (SMC) migration from the tunica media to the intima, a key event in neointimal formation, requires proteolytic degradation of elastin-rich extracellular matrix barriers. Although cathepsin S (Cat S) is overexpressed in atherosclerotic and neointimal lesions, its exact role in SMC behavior remains primarily unresolved. We examined the involvement of Cat S on SMC migration through an extracellular matrix barrier and its localization in SMCs. A selective Cat S inhibitor and the endogenous inhibitor cystatin C significantly attenuated SMC invasion across elastin gel. Western blotting and cell surface biotinylation analysis demonstrated localization of the 28-kd active form of Cat S on the SMC surface, consistent with its role in the proteolysis of subcellular matrices. Treatment with interferon-gamma or interleukin-beta1 significantly augmented the ability of SMC membranes to degrade elastin along with a significant increase in the level of active Cat S compared with controls. Immunofluorescence and confocal microscopy showed a punctuated pattern of Cat S clusters at the periphery of SMCs; further studies demonstrated partial co-localization of Cat S and integrin alphanubeta3 at the cell surfaces. These findings demonstrate that active Cat S co-localizes with integrin alphanubeta3 as a receptor on the SMC surface, playing an important role in the invasive behavior of SMCs.

Indexed as

AnimalsAntineoplastic AgentsAortaBiotinylationBlotting, WesternCathepsinsCattleCell MembraneCell MovementCells, CulturedCystatin CCystatinsElastinExtracellular MatrixFluorescent Antibody TechniqueHumansAntineoplastic Agentscathepsin SCathepsinsCST3 protein, humanCst3 protein, ratCystatin CCystatinsElastinIntegrin alphaVbeta3Interferon-gammaInterleukin-1RNA, Messenger

Identifiers

PMID16436681
PMCPMC1606490
OpenAlexW2053681311

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.