Evidence map›Paper›PMID 18697739›Full record

ArticleThe Journal of biological chemistry2008

Laminin isoforms containing the gamma3 chain are unable to bind to integrins due to the absence of the glutamic acid residue conserved in the C-terminal regions of the gamma1 and gamma2 chains.

Hiroyuki Ido, Shunsuke Ito, Yukimasa Taniguchi, Maria Hayashi, Ryoko Sato-Nishiuchi, Noriko Sanzen, Yoshitaka Hayashi, Sugiko Futaki, Kiyotoshi Sekiguchi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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
  5. Zebrafish Models ofFrontiers in molecular neuroscience · 2020
    Article
  6. Article
  7. Article
  8. Laminin-dystroglycan signaling regulates retinal arteriogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Basement membranes: cell scaffoldings and signaling platforms.Cold Spring Harbor perspectives in biology · 2011
    Review
  19. Article
  20. 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

9 authors at 2 institutions in 1 country.

Hiroyuki IdoLaboratory of Extracellular Matrix Biochemistry, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Shunsuke Ito
Yukimasa Taniguchi
Maria Hayashi
Ryoko Sato-Nishiuchi
Noriko Sanzen
Yoshitaka Hayashi
Sugiko Futaki
Kiyotoshi Sekiguchi
Osaka University · JPNagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Laminins are the major cell adhesive proteins in basement membranes, and consist of three subunits termed alpha, beta, and gamma. Recently, we found that the Glu residue at the third position from the C termini of the gamma1 and gamma2 chains is critically involved in integrin binding by laminins. However, the gamma3 chain lacks this Glu residue, suggesting that laminin isoforms containing the gamma3 chain may be unable to bind to integrins. To address this possibility, we expressed the E8 fragment of laminin-213 and found that it was incapable of binding to integrins. Similarly, the E8 fragment of laminin-113 was expressed and also found to be inactive in binding to integrins, confirming the distinction between the integrin binding activities of gamma3 chain-containing isoforms and those containing the gamma1 or gamma2 chain. To further address the importance of the Glu residue, we swapped the C-terminal four amino acids of the gamma3 chain with the C-terminal nine amino acids of the gamma1 chain, which contain the Glu residue. The resulting chimeric E8 fragment of laminin-213 became fully active in integrin binding, whereas replacement with the nine amino acids of the gamma1 chain after substitution of Gln for the conserved Glu residue failed to restore the integrin binding activity. These results provide both loss-of-function and gain-of-function evidence that laminin isoforms containing the gamma3 chain are unable to bind to integrins due to the absence of the conserved Glu residue, which should play a critical role in integrin binding by laminins.

Indexed as

Amino Acid SequenceCell AdhesionDose-Response Relationship, DrugGlutamic AcidHumansK562 CellsLamininModels, BiologicalMolecular Sequence DataProtein BindingProtein IsoformsProtein Structure, TertiaryGlutamic AcidLAMC2 protein, humanLAMC3 protein, humanLamininlaminin gamma 1Protein Isoforms

Identifiers

PMID18697739
PMCPMC2661386
OpenAlexW2073256831

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.