Evidence map›Paper›PMID 19773554›Full record

ArticleThe Journal of biological chemistry2009

Identification of a novel family of laminin N-terminal alternate splice isoforms: structural and functional characterization.

Kevin J Hamill, Lutz Langbein, Jonathan C R Jones, W H Irwin McLean

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
0.7field-weighted citation impact, top 32% 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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 29 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Laminin N-terminus α31 expression during development is lethal and causes widespread tissue-specific defects in a transgenic mouse model.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
  6. Article
  7. Organization of the laminin polymer node.Matrix biology : journal of the International Society for Matrix Biology · 2021
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Laminins: Roles and Utility in Wound Repair.Advances in wound care · 2015
    Review
  13. Article
  14. Article
  15. Article
  16. 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

4 authors at 4 institutions in 3 countries.

Kevin J HamillEpithelial Genetics Group, Human Genetics Unit, Division of Pathology and Neuroscience, Ninewells Hospital and Medical School, University of Dundee, Dundee DD1 9SY, Scotland, United Kingdom. k-hamill@northwestern.edu
Lutz Langbein
Jonathan C R Jones
W H Irwin McLean
Heidelberg University · DENinewells Hospital · GBNorthwestern University · USUniversity of Dundee · GB

Funding

Keratinocyte Migration and Wound HealingR01AR054184 · NIAMS · WASHINGTON STATE UNIVERSITY · PI JONES, JONATHAN C. · 2006 to 2015
$3.3M
Medical Research Council G0700314NIAMS NIH HHS R01 AR054184
6 · The paper itself

Abstract

The laminins are a family of heterotrimeric basement membrane proteins that play roles in cellular adhesion, migration, and tissue morphogenesis. Through in silico analysis of the laminin-encoding genes, we identified a novel family of alternate splice isoforms derived from the 5'-end of the LAMA3 and LAMA5 genes. These isoforms resemble the netrins in that they contain a laminin N-terminal domain followed by a short stretch of laminin-type epidermal growth factor-like repeats. We suggest the terms LaNt (laminin N terminus) alpha3 and LaNt alpha5, for the predicted protein products of these mRNAs. RT-PCR confirmed the presence of these transcripts at the mRNA level. Moreover, they exhibit differential, tissue-specific, expression profiles. To confirm the existence of LaNt alpha3 protein, we generated an antibody to a unique domain within the putative polypeptide. This antibody recognizes a protein at the predicted molecular mass of 64 kDa by immunoblotting. Furthermore, immunofluorescence analyses revealed a basement membrane staining in epithelial tissue for LaNt alpha3 and LaNt alpha3 localized along the substratum-associated surface of cultured keratinocytes. We have also tested the functionality LaNt alpha3 through RNAi-mediated knockdown. Keratinocytes exhibiting specific knockdown of LaNt alpha3 displayed impaired adhesion, stress resistance, and reduced ability to close scratch wounds in vitro.

Indexed as

Alternative SplicingAnimalsAntibodies, MonoclonalCell AdhesionHeLa CellsHumansKeratinocytesLamininMiceOrgan SpecificityProtein IsoformsProtein Structure, TertiaryReverse Transcriptase Polymerase Chain ReactionRNA, MessengerWound HealingAntibodies, MonoclonalLamininlaminin alpha 3laminin alpha5Protein IsoformsRNA, Messenger

Identifiers

PMID19773554
PMCPMC2790989
OpenAlexW2077058377

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.