Evidence map›Paper›PMID 9425001›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1998

Growth factor receptor tyrosine kinases acutely regulate neuronal sodium channels through the src signaling pathway.

M D Hilborn, R R Vaillancourt, S G Rane

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Src family tyrosine kinase inhibitors suppress Nav1.1 expression in cultured rat spiral ganglion neurons.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2016
    Article
  4. Blocking Infralimbic Basic Fibroblast Growth Factor (bFGF or FGF2) Facilitates Extinction of Drug Seeking After Cocaine Self-Administration.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2015
    Article
  5. Article
  6. Article
  7. Plasticity in the prefrontal cortex of adult rats.Frontiers in cellular neuroscience · 2015
    Review
  8. Article
  9. Regulation of sodium channel activity by phosphorylation.Seminars in cell & developmental biology · 2011
    Review
  10. Article
  11. Article
  12. Sites and molecular mechanisms of modulation of Na(v)1.2 channels by Fyn tyrosine kinase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  13. Regulation of Na(v)1.2 channels by brain-derived neurotrophic factor, TrkB, and associated Fyn kinase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

M D HilbornDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
R R Vaillancourt
S G Rane
Purdue University West Lafayette · USUniversity of Arizona · US

Funding

PC12 CELL DIFFERENTIATION FROM PDGF RECEPTOR ACTIVATIONF32DK008897 · NIDDK · NATIONAL JEWISH HEALTH · PI VAILLANCOURT, RICHARD R · 1993 to 1995
–
NIDDK NIH HHS DK 08897NIDDK NIH HHS F32 DK008897
6 · The paper itself

Abstract

Growth factor receptor tyrosine kinase (RTK)-activated signaling pathways are well established regulators of neuronal growth and development, but whether these signals provide mechanisms for acute modulation of neuronal activity is just beginning to be addressed. We show in pheochromocytoma (PC12) cells that acute application of ligands for both endogenous RTKs [trkA, basic FGF (bFGF) receptor, and epidermal growth factor (EGF) receptor] and ectopically expressed platelet-derived growth factor (PDGF) receptors rapidly inhibits whole-cell sodium channel currents, coincident with a hyperpolarizing shift in the voltage dependence of inactivation. Sodium channel inhibition by trkA and PDGF receptors is mutually occlusive, suggestive of a common signal transduction mechanism. Furthermore, specific inhibitors for trkA and PDGF RTK activities abrogate sodium channel inhibition in response to NGF and PDGF, respectively, showing that the intrinsic RTK activity of these receptors is necessary for sodium channel inhibition. Use of PDGF receptor mutants deficient for specific signaling activities demonstrated that this inhibition is dependent on RTK interaction with Src but not with other RTK-associated signaling molecules. Inhibition was also compromised in cells expressing dominant-negative Ras. These results suggest a possible mechanism for acute physiological actions of RTKs, and they indicate regulatory functions for Ras and Src that may complement the roles of these signaling proteins in long-term neuronal regulation.

Indexed as

Signal TransductionAnimalsCell DifferentiationNeuronsPC12 Cellsras ProteinsRatsReceptor Protein-Tyrosine KinasesReceptors, Fibroblast Growth FactorReceptors, Growth FactorReceptors, Nerve Growth FactorReceptors, Platelet-Derived Growth FactorReceptor, trkASodium Channelssrc Homology Domainsras ProteinsReceptor Protein-Tyrosine KinasesReceptors, Fibroblast Growth FactorReceptors, Growth FactorReceptors, Nerve Growth FactorReceptors, Platelet-Derived Growth FactorReceptor, trkASodium Channels

Identifiers

PMID9425001
PMCPMC6792527
OpenAlexW1563737837

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.