Evidence map›Paper›PMID 7530449›Full record

ArticleThe Biochemical journal1995

Tyrosine phosphorylation and association of Syk with Fc gamma RII in monocytic THP-1 cells.

S Ghazizadeh, J B Bolen, H B Fleit

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.9field-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

22 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Equus β-Defensin-1 Regulates Innate IMMUNE Response inAnimals : an open access journal from MDPI · 2022
    Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. CD32 Ligation Promotes the Activation of CD4Frontiers in immunology · 2018
    Article
  8. Review
  9. FcγRIIa requires lipid rafts, but not co-localization into rafts, for effector function.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2013
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Fcgamma receptor signaling in phagocytes.International journal of hematology · 2006
    Review
  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

3 authors at 2 institutions in 1 country.

S GhazizadehDepartment of Pathology, State University of New York at Stony Brook 11794.
J B Bolen
H B Fleit
Stony Brook University · USBristol-Myers Squibb (United States) · US

Funding

FC RECEPTOR EXPRESSION DURING MYELOID DIFFERENTIATIONR01CA038055 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI FLEIT, HOWARD B · 1988 to 1992
–
FC RECEPTOR EXPRESSION DURING MYELOID DIFFERENTIATIONR23CA038055 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI FLEIT, HOWARD B · 1985 to 1986
–
NCI NIH HHS CA38055NCRR NIH HHS RR05736
6 · The paper itself

Abstract

Although the cytoplasmic portion of the low-affinity receptor for immunoglobulin G, Fc gamma RII, does not contain a kinase domain, rapid tyrosine phosphorylation of intracellular substrates occurs in response to aggregation of the receptor. The use of specific tyrosine kinase inhibitors has suggested that these phosphorylations are required for subsequent cellular responses. We previously demonstrated the coprecipitation of a tyrosine kinase activity with Fc gamma RII, suggesting that non-receptor tyrosine kinases might associate with the cytoplasmic domain of Fc gamma RII. Anti-receptor immune complex kinase assays revealed the coprecipitation of several phosphoproteins, most notably p56/53lyn, an Src-family protein tyrosine kinase (PTK), and a 72 kDa phosphoprotein. Here we identify the 72 kDa Fc gamma RII-associated protein as p72syk (Syk), a member of a newly described family of non-receptor PTKs. A rapid and transient tyrosine phosphorylation of Syk was observed following Fc gamma RII activation. Syk was also tyrosyl-phosphorylated following aggregation of the high-affinity Fc gamma receptor, Fc gamma RI. The Fc gamma RI activation did not result in association of Syk with Fc gamma RII, implying that distinct pools of Syk are activated upon aggregation of each receptor in a localized manner. These results demonstrate a physical association between Syk and Fc gamma RII and suggest that the molecules involved in Fc gamma RII signalling are very similar to the ones utilized by multichain immune recognition receptors such as the B-cell antigen receptor and the high-affinity IgE receptor.

Indexed as

Amino AcidsBlotting, WesternCells, CulturedEnzyme PrecursorsIntracellular Signaling Peptides and ProteinsMonocytesPhosphorylationPhosphotyrosinePrecipitin TestsProtein BindingProtein-Tyrosine KinasesReceptor AggregationReceptors, IgGSignal TransductionSyk KinaseTyrosineAmino AcidsEnzyme PrecursorsIntracellular Signaling Peptides and ProteinsPhosphotyrosineProtein-Tyrosine KinasesReceptors, IgGSyk KinaseTyrosine

Identifiers

PMID7530449
PMCPMC1136413
OpenAlexW106950157

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.