Evidence map›Paper›PMID 8818145›Full record

ReviewMolecular neurobiology1996

Role of laminin and integrin interactions in growth cone guidance.

L McKerracher, M Chamoux, C O Arregui

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Nongenomic actions of thyroid hormone.Nature reviews. Endocrinology · 2016
    Review
  6. Article
  7. Article
  8. Article
  9. Cellular strategies of axonal pathfinding.Cold Spring Harbor perspectives in biology · 2010
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Myelin proteolipid protein forms a complex with integrins and may participate in integrin receptor signaling in oligodendrocytes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
    Article
  15. Integrins regulate responsiveness to slit repellent signals.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
    Article
  16. Rapid neuromodulatory actions of integrin ligands.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
    Article
  17. Plasma membrane ganglioside sialidase regulates axonal growth and regeneration in hippocampal neurons in culture.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    Article
  18. Article
  19. Local presentation of substrate molecules directs axon specification by cultured hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999
    Article
  20. Bradykinin-induced collapse of rat pheochromocytoma (PC12) cell growth cones: a role for tyrosine kinase activity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997
    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

3 authors at 2 institutions in 2 countries.

L McKerracherDépartement de Pathologie, Université de Montréal, Quebec, Canada.
M Chamoux
C O Arregui
Université de Montréal · CAUniversidad Nacional de Córdoba · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Laminin is well known to promote neuronal adhesion and axonal growth, but recent experiments suggest laminin has a wider role in guiding axons, both in development and regeneration. In vitro experiments demonstrate that laminin can alter the rate and direction of axonal growth, even when growth cone contact with laminin is transient. Investigations focused on a single neuronal type, such as retinal ganglion cells (RGCs), strongly implicate laminin as an important guidance molecule in development and suggest the involvement of integrins. Integrins are receptors for laminin, and neurons express multiple types of integrins that bind laminin. Morphologically, integrins cluster in point contacts, specialized regions of the growth cone that may coordinately regulate adhesion and motility. Recent evidence suggests that the structure and regulation of point contacts may differ from that of their nonneuronal counterpart, focal contacts. In part, this may be because the interaction of the cytoplasmic domain of integrin with the cytoskeleton is different in point contacts and focal contracts. Mutational studies where the cytoplasmic domain is truncated or altered are leading to a better understanding of the role of the alpha and beta subunit in regulating integrin clustering and binding to the cytoskeleton. In addition, whereas integrins may regulate motility through direct physical linkages to the growth cone cytoskeleton, an equally important role is their ability to elicit signaling, both through protein tyrosine phosphorylation and modulating calcium levels. Through such mechanisms integrins likely regulate the dynamic attachment and detachment of the growth cone as it moves on laminin substrates.

Indexed as

AnimalsAxonsCell AdhesionCell CommunicationCell DivisionHumansIntegrinsLamininNerve RegenerationNeuronsReceptors, LamininRetinal Ganglion CellsIntegrinsLamininReceptors, Laminin

Identifiers

PMID8818145
OpenAlexW1999385601

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.