Evidence map›Paper›PMID 20566382›Full record

ArticleMatrix biology : journal of the International Society for Matrix Biology2010

Laminin-121--recombinant expression and interactions with integrins.

Takako Sasaki, Junichi Takagi, Camilla Giudici, Yoshihiko Yamada, Eri Arikawa-Hirasawa, Rainer Deutzmann, Rupert Timpl, Arnoud Sonnenberg, Hans Peter Bächinger, David Tonge

Abstract readComparative Study
In one paragraph

Article in Matrix biology : journal of the International Society for Matrix Biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

11 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Bone marrow laminins influence hematopoietic stem and progenitor cell cycling and homing to the bone marrow.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Article
  7. Review
  8. Proregenerative properties of ECM molecules.BioMed research international · 2013
    Review
  9. Article
  10. Article
  11. The laminin family.Cell adhesion & migration
    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

10 authors at 7 institutions in 5 countries.

Takako SasakiMax-Planck-Institut für Biochemie, Martinsried, Germany. tsasaki@molmed.uni-erlangen.de
Junichi Takagi
Camilla Giudici
Yoshihiko Yamada
Eri Arikawa-Hirasawa
Rainer Deutzmann
Rupert Timpl
Arnoud Sonnenberg
Hans Peter Bächinger
David Tonge
Max Planck Society · DENational Institute of Dental and Craniofacial Research · USKing's College London · GBProtein Research Foundation · JPShriners Hospitals for Children - Portland · USThe Netherlands Cancer Institute · NLUniversity of Regensburg · DE

Funding

Basement Membranes and Associated Protein Factors In Development and DiseaseZIADE000485 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI YAMADA, YOSHIHIKO · 2009 to 2017
$5.9M
Intramural NIH HHS ZIA DE000485
6 · The paper itself

Abstract

Laminin-121, previously referred as to laminin-3, was expressed recombinantly in human embryonic kidney (HEK) 293 cells by triple transfection of full-length cDNAs encoding mouse laminin α1, β2 and γ1 chains. The recombinant laminin-121 was purified using Heparin-Sepharose followed by molecular sieve chromatography and shown to be correctly folded by electron microscopy and circular dichroism (CD). The CD spectra of recombinant laminin-121 were very similar to those of laminin-111 isolated from Engelbreth-Holm-Swarm tumor (EHS-laminin) but its T(m) value was smaller than EHS-laminin and recombinant lamnin-111 suggesting that the replacement of the β chain reduced the stability of the coiled-coil structure of laminin-121. Its binding to integrins was compared with EHS-laminin, laminin-3A32 purified from murine epidermal cell line and recombinantly expressed laminins-111, -211 and -221. Laminin-121 showed the highest affinity to α6β1 and α7β1 integrins and furthermore, laminin-121 most effectively supported neurite outgrowth. Together, this suggests that the β2 laminins have higher affinity for integrins than the β1 laminins.

Indexed as

AnimalsCell LineChromatography, GelCircular DichroismHEK293 CellsHumansIntegrinsIn Vitro TechniquesKidneyLamininMiceRecombinant ProteinsSepharoseTransfectionheparin-sepharoseintegrin alpha7beta1IntegrinsLamininlaminin Alaminin beta2Recombinant ProteinsSepharose

Identifiers

PMID20566382
PMCPMC2939186
OpenAlexW2012114008

What OpenQuestion holds

Textmetadata
LicenceTDM
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.