Evidence map›Paper›PMID 11986952›Full record

ArticleLeukemia2002

Expression of a mutated form of the p85alpha regulatory subunit of phosphatidylinositol 3-kinase in a Hodgkin's lymphoma-derived cell line (CO).

M Jücker, K Südel, S Horn, M Sickel, W Wegner, W Fiedler, R A Feldman

Abstract read
PubMed Publisher
In one paragraph

Article in Leukemia, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.3field-weighted citation impact, top 10% 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

43 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Cancer-AssociatedInternational journal of medical sciences · 2025
    Review
  3. Functional selection in SH3-mediated activation of the PI3 kinase.bioRxiv : the preprint server for biology · 2024
    Article
  4. Nanobodies and chemical cross-links advance the structural and functional analysis of PI3Kα.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Oncogenic activity of the regulatory subunit p85β of phosphatidylinositol 3-kinase (PI3K).Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Article
  14. Article
  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

7 authors at 3 institutions in 2 countries.

M JückerInstitut für Medizinische Biochemie und Molekularbiologie, Abteilung für Zelluläre Signaltransduktion, Universitätsklinikum Hamburg-Eppendorf, Universität Hamburg, Martinistrasse 52, 20246 Hamburg, Germany.
K Südel
S Horn
M Sickel
W Wegner
W Fiedler
R A Feldman
University Medical Center Hamburg-Eppendorf · DEUniversity of Maryland, Baltimore · USUniversität Hamburg · DE

Funding

ROLE OF FPS/FES PROTO-ONCOGENE IN MYELOID CELL FUNCTIONR01CA055293 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI FELDMAN, RICARDO A · 1998 to 2004
$822k
FPS/FES PROTO-ONCOGENE IN MYELOID CELL FUNCTIONR29CA055293 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI FELDMAN, RICARDO A · 1991 to 1997
–
NCI NIH HHS CA 55293
6 · The paper itself

Abstract

Phosphatidylinositol (PI) 3-kinase plays an important role in a variety of biological processes, including proliferation and apoptosis. PI3-kinase is a heterodimer consisting of an 85 kDa adapter protein (p85) containing one SH3 domain and two SH2 domains and a 110 kDa catalytic subunit (p110). Recently an oncogenic form of p85 named p65-PI3K lacking the C-terminal SH2 domain has been cloned from an irradiation-induced murine thymic lymphoma and transgenic mice expressing p65-PI3K in T lymphocytes develop a lymphoproliferative disorder. Here we describe the cloning of a C-terminal truncated form of p85 expressed in a human lymphoma cell line (CO) with a T cell phenotype derived from a patient with Hodgkin's disease. As a result of a frame-shift mutation at amino acid 636, p76 is lacking most of the C-terminal SH2 domain, but contains the inter-SH2 domain and is associated with an active form of PI3-kinase. A PI3-kinase-dependent constitutive activation of Akt was detected in CO cells which was only partially reduced after serum starvation. Treatment of CO cells with the PI3-kinase inhibitor wortmannin resulted in a concentration-dependent inhibition of cell proliferation associated with an increased number of apoptotic cells. This is the first detection of a mutated form of the p85 subunit of PI3-kinase in human hematopoietic cells further underlining a potential role of PI3-kinase/Akt signaling in human leukemogenesis.

Indexed as

Frameshift MutationProtein Serine-Threonine KinasesApoptosisCloning, MolecularDimerizationEnzyme ActivationHodgkin DiseaseHumansPhosphatidylinositol 3-KinasesProtein SubunitsProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSignal Transductionsrc Homology DomainsT-LymphocytesTumor Cells, CulturedAKT1 protein, humanPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesProtein SubunitsProto-Oncogene ProteinsProto-Oncogene Proteins c-akt

Identifiers

PMID11986952
OpenAlexW2321226355

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.