Evidence map›Paper›PMID 7532280›Full record

ArticleMolecular and cellular biology1995

Clustering of Syk is sufficient to induce tyrosine phosphorylation and release of allergic mediators from rat basophilic leukemia cells.

V M Rivera, J S Brugge

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

14 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. One lyn molecule is sufficient to initiate phosphorylation of aggregated high-affinity IgE receptors.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  6. Article
  7. Article
  8. Article
  9. Relation between effects of a set of anti-allergic drugs on calcium pathways and membrane structure in Fc epsilon RI activated signal transduction.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 1996
    Article
  10. Article
  11. Article
  12. Clustered syk tyrosine kinase domains trigger phagocytosis.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  13. Article
  14. 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

2 authors at 1 institution in 1 country.

V M RiveraARIAD Pharmaceuticals, Cambridge, Massachusetts 02139.
J S Brugge
Aridis Pharmaceuticals (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In mast cells, antigen-mediated aggregation of the high-affinity receptor for immunoglobulin E, Fc epsilon RI, stimulates tyrosine phosphorylation and activation of multiple signaling pathways leading to the release of several classes of mediators of the allergic response. Early events induced upon cross-linking of Fc epsilon RI include tyrosine phosphorylation of Fc epsilon RI subunits and activation of the tyrosine kinase p72syk (Syk), which binds to tyrosine-phosphorylated Fc epsilon RI. Clustering of Syk, as a result of its interaction with aggregated Fc epsilon RI, may play a role in activating one or more of the signaling pathways leading to mediator release. To test this possibility, Syk was introduced into a model mast cell line (rat basophilic leukemia cells) as part of a chimeric transmembrane protein containing the extracellular and transmembrane domains of CD16 and CD7, respectively. Clustering of the Syk chimera, using antibodies against CD16, was found to be sufficient to stimulate early and late events normally induced by clustering of Fc epsilon RI. Specifically, aggregation of Syk induced degranulation, leukotriene synthesis, and expression of cytokine genes. Induction of mediator release was dependent on the kinase activity of Syk. Consistent with this finding, clustering of Syk also induced the tyrosine phosphorylation of a profile of proteins, including phospholipase C-gamma 1 and mitogen-activated protein kinase, similar to that induced upon clustering of Fc epsilon RI. These results strongly suggest that Syk is an early and critical mediator of multiple signaling pathways that emanate from the Fc epsilon RI receptor and give rise to the allergic response.

Indexed as

AnimalsCell LineCell MembraneCytokinesEnzyme PrecursorsGenetic VectorsHumansInterleukinsIntracellular Signaling Peptides and ProteinsLeukemia, Basophilic, AcuteLeukotrienesMast CellsPhosphorylationPhosphotyrosineProtein-Tyrosine KinasesRatsCytokinesEnzyme PrecursorsInterleukinsIntracellular Signaling Peptides and ProteinsLeukotrienesPhosphotyrosineProtein-Tyrosine KinasesReceptors, IgERecombinant Fusion ProteinsSyk KinaseSYK protein, humanSyk protein, ratTyrosine

Identifiers

PMID7532280
PMCPMC230382
OpenAlexW2142482343

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.