Evidence map›Paper›PMID 25356505›Full record

ReviewInternational journal of molecular sciences2014

Cell-surface receptors transactivation mediated by g protein-coupled receptors.

Fabio Cattaneo, Germano Guerra, Melania Parisi, Marta De Marinis, Domenico Tafuri, Mariapia Cinelli, Rosario Ammendola

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

96 citing papers in PubMed, 180 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. GαInternational journal of molecular sciences · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Agonist-Induced CaCells · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. NOX Dependent ROS Generation and Cell Metabolism.International journal of molecular sciences · 2023
    Review
  18. Article
  19. Article
  20. Diversification of PAR signaling through receptor crosstalk.Cellular & molecular biology letters · 2022
    Review

36 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

7 authors at 4 institutions in 1 country.

Fabio CattaneoDepartment of Molecular Medicine and Medical Biotechnology, School of Medicine, University of Naples Federico II, Naples 80131, Italy. fabio.cattaneo@unina.it.
Germano GuerraDepartment of Medicine and Health Sciences, University of Molise, Campobasso 86100, Italy. germano.guerra@unimol.it.
Melania ParisiDepartment of Molecular Medicine and Medical Biotechnology, School of Medicine, University of Naples Federico II, Naples 80131, Italy. melania.parisi@unina.it.
Marta De MarinisDepartment of Molecular Medicine and Medical Biotechnology, School of Medicine, University of Naples Federico II, Naples 80131, Italy. mar.demarinis@studenti.unina.it.
Domenico TafuriDepartment of Sport Science and Wellness, University of Naples Parthenope, Naples 80133, Italy. tafuri@uniparthenope.it.
Mariapia CinelliDepartment of Public Health, School of Medicine, University of Naples Federico II, Naples 80131, Italy. mariapia.cinelli@unina.it.
Rosario AmmendolaDepartment of Molecular Medicine and Medical Biotechnology, School of Medicine, University of Naples Federico II, Naples 80131, Italy. rosario.ammendola@unina.it.
Federico II University Hospital · ITParthenope University of Naples · ITUniversity of Molise · ITUniversity of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are seven transmembrane-spanning proteins belonging to a large family of cell-surface receptors involved in many intracellular signaling cascades. Despite GPCRs lack intrinsic tyrosine kinase activity, tyrosine phosphorylation of a tyrosine kinase receptor (RTK) occurs in response to binding of specific agonists of several such receptors, triggering intracellular mitogenic cascades. This suggests that the notion that GPCRs are associated with the regulation of post-mitotic cell functions is no longer believable. Crosstalk between GPCR and RTK may occur by different molecular mechanism such as the activation of metalloproteases, which can induce the metalloprotease-dependent release of RTK ligands, or in a ligand-independent manner involving membrane associated non-receptor tyrosine kinases, such as c-Src. Reactive oxygen species (ROS) are also implicated as signaling intermediates in RTKs transactivation. Intracellular concentration of ROS increases transiently in cells stimulated with GPCR agonists and their deliberated and regulated generation is mainly catalyzed by enzymes that belong to nicotinamide adenine dinucleotide phosphate (NADPH) oxidase family. Oxidation and/or reduction of cysteine sulfhydryl groups of phosphatases tightly controls the activity of RTKs and ROS-mediated inhibition of cellular phosphatases results in an equilibrium shift from the non-phosphorylated to the phosphorylated state of RTKs. Many GPCR agonists activate phospholipase C, which catalyze the hydrolysis of phosphatidylinositol 4,5-bis-phosphate to produce inositol 1,4,5-triphosphate and diacylglicerol. The consequent mobilization of Ca2+ from endoplasmic reticulum leads to the activation of protein kinase C (PKC) isoforms. PKCα mediates feedback inhibition of RTK transactivation during GPCR stimulation. Recent data have expanded the coverage of transactivation to include Serine/Threonine kinase receptors and Toll-like receptors. Herein, we discuss the main mechanisms of GPCR-mediated cell-surface receptors transactivation and the pathways involved in intracellular responses induced by GPCR agonists. These studies may suggest the design of novel strategies for therapeutic interventions.

Indexed as

AnimalsArrestinsbeta-ArrestinsMetalloendopeptidasesReactive Oxygen SpeciesReceptor Protein-Tyrosine KinasesReceptors, Cell SurfaceReceptors, G-Protein-CoupledSignal TransductionToll-Like ReceptorsTranscriptional ActivationArrestinsbeta-ArrestinsMetalloendopeptidasesReactive Oxygen SpeciesReceptor Protein-Tyrosine KinasesReceptors, Cell SurfaceReceptors, G-Protein-CoupledToll-Like Receptors

Identifiers

PMID25356505
PMCPMC4264134
OpenAlexW2155976456

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.