Evidence map›Paper›PMID 2825654›Full record

ArticleThe Biochemical journal1987

Evidence for two distinct phosphatidylinositol kinases in fibroblasts. Implications for cellular regulation.

M Whitman, D Kaplan, T Roberts, L Cantley

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
12.3field-weighted citation impact, top 1% 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

87 citing papers in PubMed, 304 citations in OpenAlex.

  1. Phosphatidylinositol 4-phosphate; A minor lipid with multiple personalities.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  2. Review
  3. Review
  4. Review
  5. A short history of inositol lipids.Journal of lipid research · 2016
    Review
  6. Article
  7. Review
  8. Article
  9. Targeting the PI3K pathway for cancer therapy.Future medicinal chemistry · 2012
    Review
  10. Lessons in signaling and tumorigenesis from polyomavirus middle T antigen.Microbiology and molecular biology reviews : MMBR · 2009
    Review
  11. Article
  12. Review
  13. Review
  14. PI3K signaling in glioma--animal models and therapeutic challenges.Brain pathology (Zurich, Switzerland) · 2009
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

27 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

M WhitmanDepartment of Physiology, Tufts University School of Medicine, Boston, MA 02111.
D Kaplan
T Roberts
L Cantley
Tufts University · US

Funding

MOLECULAR MECHANISMS OF POLYOMA INDUCED TRANSFORMATIONR01CA030002 · NCI · DANA-FARBER CANCER INSTITUTE · PI ROBERTS, THOMAS M · 1985 to 2014
$5.8M
PHOSPHATIDYLINOSITOL KINASESR01GM036624 · NIGMS · TUFTS UNIVERSITY BOSTON · PI CANTLEY, LEWIS C. · 1986 to 2008
$2.9M
MECHANISM OF CATION TRANSPORT REGULATIONR01GM036133 · NIGMS · TUFTS UNIVERSITY BOSTON · PI CANTLEY, LEWIS C · 1985 to 1993
–
MOLECULAR MECHANISMS OF POLYOMA-INDUCED TRANSFORMATIONR37CA030002 · NCI · DANA-FARBER CANCER INSTITUTE · PI ROBERTS, THOMAS M · 1993 to 1999
–
NCI NIH HHS CA30002NIGMS NIH HHS GM36133NIGMS NIH HHS GM36624
6 · The paper itself

Abstract

Phosphatidylinositol (PtdIns) kinase activities from non-transformed and polyoma-middle-T-transformed murine fibroblasts were examined. Both normal and transformed 3T3 fibroblasts have two PtdIns kinases, which can be separated by anion-exchange chromatography. One of these activities (Type I) has a Km for ATP of 10 microM, is resistant to inhibition by adenosine, AMP or ADP, and is inhibited by non-ionic detergents. The other activity (Type II) has a somewhat higher Km for ATP (35 microM) and is inhibited competitively by ADP, AMP and adenosine at concentrations suggesting regulation of this activity by the energy charge of the cell. The Type II PtdIns kinase is activated by non-ionic detergents. We have previously reported the specific association of a PtdIns kinase activity with polyoma-middle-T immunoprecipitates [Whitman, Kaplan, Schaffhausen, Cantley & Roberts (1985) Nature (London) 315, 239-242; Kaplan, Whitman, Schaffhausen, Raptis, Garcea, Pallas, Roberts & Cantley (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 3624-3628]. Comparison of the immunoprecipitated PtdIns kinase with the activities identified by ion-exchange chromatography indicates that it is the Type I enzyme which specifically associates with the middle-T/pp60c-src complex. This PtdIns kinase activity is separable from both middle T and pp60c-src. Type I PtdIns kinase also associates with pp60v-src immunoprecipitates from Rous-sarcoma-virus-transformed cells. Furthermore, this PtdIns kinase appears to co-precipitate with partially purified platelet derived growth factor (PDGF) receptor. The amount of this activity found in anti-phosphotyrosine immunoprecipitates or in wheat-germ-lectin-agarose precipitates is increased 50-fold by stimulation of quiescent Balb/C 3T3 fibroblasts with PDGF. These results suggest that the Type I PtdIns kinase is regulated by agents which affect cell growth and transformation, whereas the Type II PtdIns kinase may be regulated by the local [ATP]/[ADP] ratio.

Indexed as

1-Phosphatidylinositol 4-KinaseAdenosineAdenosine DiphosphateAnimalsCell LineCell Transformation, NeoplasticChemical PrecipitationChromatography, Ion ExchangeFibroblastsIsoenzymesMicePhosphotransferasesPlatelet-Derived Growth Factor1-Phosphatidylinositol 4-KinaseAdenosineAdenosine DiphosphateIsoenzymesPhosphotransferasesPlatelet-Derived Growth Factor

Identifiers

PMID2825654
PMCPMC1148384
OpenAlexW2260076009

What Socratic 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 Socratic graph.