Evidence map›Paper›PMID 15271946›Full record

ArticleInfection and immunity2004

Proapoptotic effect of proteolytic activation of matrix metalloproteinases by Streptococcus pyogenes thiol proteinase (Streptococcus pyrogenic exotoxin B).

Fumio Tamura, Rumiko Nakagawa, Teruo Akuta, Shigefumi Okamoto, Shigeyuki Hamada, Hiroshi Maeda, Shigetada Kawabata, Takaaki Akaike

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.3field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 59 citations in OpenAlex.

  1. Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  2. Article
  3. Article
  4. Playing With Fire: Proinflammatory Virulence Mechanisms of Group AFrontiers in cellular and infection microbiology · 2021
    Review
  5. Interaction ofMatrix biology plus · 2020
    Article
  6. The Pathogenic Factors from Oral Streptococci for Systemic Diseases.International journal of molecular sciences · 2019
    Review
  7. Review
  8. Article
  9. Molecular and genomic characterization of pathogenic traits of group A Streptococcus pyogenes.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2015
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Streptococcus adherence and colonization.Microbiology and molecular biology reviews : MMBR · 2009
    Review
  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

8 authors at 2 institutions in 1 country.

Fumio TamuraDepartment of Microbiology, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto 860-8556, Japan.
Rumiko Nakagawa
Teruo Akuta
Shigefumi Okamoto
Shigeyuki Hamada
Hiroshi Maeda
Shigetada Kawabata
Takaaki Akaike
Kumamoto University · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus pyogenes thiol proteinase, also known as streptococcal pyrogenic exotoxin B (SpeB), has been suggested to be a major virulence factor in S. pyogenes infection. SpeB was reported to induce apoptosis of host cells, but its mechanism of action is not yet fully understood. In this study, we examined the involvement of matrix metalloproteinases (MMPs) in SpeB-induced apoptosis. We first developed a large-scale preparation of recombinant SpeB and precursors of human MMP-9 and -2 (proMMPs) by using Escherichia coli Rosetta (DE3)pLysS and baculovirus-insect cell expression systems, respectively. Treatment with SpeB induced effective proteolytic activation of both proMMP-9 and -2. When RAW264 murine macrophages were incubated with SpeB-activated proMMP-9, the level of tumor necrosis factor alpha (TNF-alpha) in conditioned medium (CM), assessed by an enzyme immunoassay, was elevated. This increase was completely inhibited by addition of the MMP inhibitor SI-27 to the cell culture. The CM also produced marked induction of apoptosis of U937 human monocytic cells. Similarly, soluble Fas ligand (sFasL) was detected in CM of cultures of SW480 cells expressing FasL after treatment with SpeB-activated proMMPs; this CM also induced apoptosis in U937 cells. SpeB had a direct effect as well and caused the release of TNF-alpha and sFasL from the cells. SpeB-dependent production of MMP-9 and -2 and proapoptotic molecules (TNF-alpha and sFasL) was evident in a murine model of severe invasive S. pyogenes infection. These results suggest that SpeB or SpeB-activated MMPs contribute to tissue damage and streptococcal invasion in the host via extracellular release of TNF-alpha and sFasL.

Indexed as

ApoptosisAnimalsBacterial ProteinsCell LineCollagenasesEnzyme ActivationEnzyme PrecursorsExotoxinsFas Ligand ProteinGelatinasesGene Expression RegulationHumansMacrophagesMaleMatrix Metalloproteinase 2Matrix Metalloproteinase 9Bacterial ProteinsCollagenasesEnzyme Precursorserythrogenic toxinExotoxinsFASLG protein, humanFas Ligand ProteinFasl protein, mouseGelatinasesMatrix Metalloproteinase 2Matrix Metalloproteinase 9Membrane GlycoproteinsMetalloendopeptidasesprogelatinasepro-matrix metalloproteinase 9Tumor Necrosis Factor-alpha

Identifiers

PMID15271946
PMCPMC470685
OpenAlexW2116487830

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.