Evidence map›Paper›PMID 24095926›Full record

ArticleThe American journal of pathology2013

Epithelial wounds induce differential phosphorylation changes in response to purinergic and EGF receptor activation.

Amanuel Kehasse, Celeste B Rich, Albert Lee, Mark E McComb, Catherine E Costello, Vickery Trinkaus-Randall

Open access · bronzeAbstract read
In one paragraph

Article in The American journal of pathology, 2013. 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
1.4field-weighted citation impact, top 19% 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, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Age Dependent Changes in Corneal Epithelial Cell Signaling.Frontiers in cell and developmental biology · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Purinergic Signalling: Therapeutic Developments.Frontiers in pharmacology · 2017
    Review
  9. Article
  10. Purinergic Signaling in Corneal Wound Healing: A Tale of 2 Receptors.Journal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics · 2016
    Review
  11. Article
  12. Article
  13. Review
  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

6 authors at 1 institution in 1 country.

Amanuel KehasseDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts; Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, Massachusetts.
Celeste B RichDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts.
Albert LeeDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts.
Mark E McCombCenter for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, Massachusetts.
Catherine E CostelloDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts; Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, Massachusetts. Electronic address: cecmsms@bu.edu.
Vickery Trinkaus-RandallDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts; Department of Ophthalmology, Boston University School of Medicine, Boston, Massachusetts. Electronic address: vickery@bu.edu.
Boston University · US

Funding

XI INTERNATIONAL SYMPOSIUM ON AMYLOIDOSISP41RR010888 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 1996 to 2011
$18.6M
Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
Molecular Mechanisms of corneal wound repairR01EY006000 · NEI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI TRINKAUS-RANDALL, VICKERY E · 1986 to 2018
$6.8M
LTQ MASS SPECTROMETER: STRUCTURAL BIOLOGYS10RR020946 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2006 to 2006
$497k
PURCHASE OF A NEW CONFOCAL ZEISS LSM 510 V32: LUNGS10RR017967 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI TRINKAUS-RANDALL, VICKERY E · 2005 to 2005
$425k
UV&IR MALDI REFLECTION TIME OF FLIGHT MASS SPECTROMETERS10RR015942 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2001 to 2001
$402k
NHLBI PROTEOMICS INITIATIVE-N01HV28178N01HV028178 · HV · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2002 to 2006
–
NCRR NIH HHS P41 RR010888NCRR NIH HHS P41 RR10888NCRR NIH HHS S10 RR017967NCRR NIH HHS S10 RR020946NCRR NIH HHS S10 RR15942NEI NIH HHS EY06000NEI NIH HHS EY06000SNEI NIH HHS R01 EY006000NHLBI NIH HHS HHSN268201000031CNHLBI NIH HHS N01 HV028178NIGMS NIH HHS P41 GM104603
6 · The paper itself

Abstract

Protein phosphorylation is a dynamic post-translational modification. Mass spectrometry-based quantitation was performed to determine the phosphoproteome profile of epithelial cells in response to injury, nucleotide, or epidermal growth factor. Phosphotyrosine enrichment used immunoprecipitation and immobilized metal affinity chromatography. Nucleotides released after scratch wounding activate purinergic receptors, leading to a distinct phosphorylation profile on epidermal growth factor receptor (EGFR) compared with its natural ligand. ATP induced a 2- to 15-fold phosphorylation increase over control on EGFR Y974, Y1086, and Y1148, with minimal phosphorylation intensity on EGFR Y1173 compared with the level measured in response to epidermal growth factor. Differential phosphorylation induced by epidermal growth factor or ATP was site specific on Src, Shc, phospholipase Cγ, protein kinase C, focal adhesion kinase, paxillin, and mitogen-activated protein kinases 1, 12, and 13. After wounding, the P2Y2 receptor mRNA expression increased, and after knockdown, migration and Ca(2+) mobilization were impaired. To examine phosphorylation mediated by P2Y2, cells were cultured in media containing stable isotope-labeled amino acids, the receptor was knocked down, and the cells were stimulated. Mass spectrometry-based comparison of the phosphorylation profiles of control versus transfected cells revealed a 50-fold decrease in phosphorylation of EGFR Y974 and 1086, with no decrease in Y1173 phosphorylation. A similarfold decrease in Src Y421 and Y446 and paxillin Y118 was detected, indicating the far-reaching importance of the P2Y2 receptor in mediating migration.

Indexed as

Calcium SignalingCell MovementAdenosine TriphosphateCells, CulturedErbB ReceptorsFocal Adhesion Kinase 1HumansPhospholipase C gammaPhosphorylationProtein Kinase CReceptors, Purinergic P2Y2src-Family KinasesWounds and InjuriesAdenosine TriphosphateEGFR protein, humanErbB ReceptorsFocal Adhesion Kinase 1Phospholipase C gammaProtein Kinase CPTK2 protein, humanReceptors, Purinergic P2Y2src-Family Kinases

Identifiers

PMID24095926
PMCPMC5745543
OpenAlexW1982931327

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.