Evidence map›Paper›PMID 12400007›Full record

ArticleOncogene2002

Involvement of nectin in the localization of junctional adhesion molecule at tight junctions.

Atsunori Fukuhara, Kenji Irie, Hiroyuki Nakanishi, Kyoji Takekuni, Tomomi Kawakatsu, Wataru Ikeda, Akio Yamada, Tatsuo Katata, Tomoyuki Honda, Tatsuhiro Sato and 5 more

Abstract read
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In one paragraph

Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
10.9field-weighted citation impact, top 1% 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

36 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Implications of AMPK in the Formation of Epithelial Tight Junctions.International journal of molecular sciences · 2018
    Review
  8. Afadin Downregulation byFrontiers in microbiology · 2018
    Article
  9. Article
  10. Article
  11. Review
  12. Serum nectin-2 levels are diagnostic and prognostic in patients with colorectal carcinoma.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2016
    Article
  13. Inhibition of Notch Signaling During Mouse Incisor Renewal Leads to Enamel Defects.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2016
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

15 authors at 2 institutions in 1 country.

Atsunori FukuharaDepartment of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Japan.
Kenji Irie
Hiroyuki Nakanishi
Kyoji Takekuni
Tomomi Kawakatsu
Wataru Ikeda
Akio Yamada
Tatsuo Katata
Tomoyuki Honda
Tatsuhiro Sato
Kazuya Shimizu
Harunobu Ozaki
Hisanori Horiuchi
Toru Kita
Yoshimi Takai
Osaka University · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Junctional adhesion molecule (JAM) is a Ca2+-independent immunoglobulin-like cell-cell adhesion molecule which localizes at tight junctions (TJs). Claudin is a key cell-cell adhesion molecule that forms TJ strands at TJs. JAM is associated with claudin through their cytoplasmic tail-binding protein, ZO-1. JAM is furthermore associated with Par-3, a cell polarity protein which forms a ternary complex with Par-6 and atypical protein kinase C. Nectin is another Ca2+-independent immunoglobulin-like cell-cell adhesion molecule which localizes at adherens junctions (AJs). Nectin is associated with E-cadherin through their respective cytoplasmic tail-binding proteins, afadin and catenins, and involved in the formation of AJs cooperatively with E-cadherin. We show here that nectin is furthermore involved in the localization of JAM at TJs. During the formation of the junctional complex consisting of AJs and TJs in Madin-Darby canine kidney (MDCK) cells, JAM was recruited to the nectin-based cell-cell adhesion sites. This recruitment of JAM was inhibited by nectin inhibitors, which inhibited the trans-interaction of nectin. Microbeads coated with the extracellular fragment of nectin, that interacted with cellular nectin, also recruited JAM to the bead-MDCK cell contact sites. Furthermore, when cadherin-deficient L fibroblasts stably expressing both exogenous JAM and nectin (nectin-JAM-L cells) were co-cultured with L fibroblasts expressing only nectin (nectin-L cells), JAM was concentrated at the cell-cell adhesion sites between nectin-JAM-L and nectin-L cells without the trans-interaction of JAM. Analyses of the localization and immunoprecipitation of JAM revealed that it was associated with nectin through afadin and ZO-1. These results suggest that nectin has a role in the localization of JAM at TJs in the process of the formation of the junctional complex in epithelial cells.

Indexed as

AnimalsCadherinsCalciumCell AdhesionCell Adhesion MoleculesCells, CulturedCoculture TechniquesDogsEpithelial CellsFibroblastsIntercellular JunctionsJunctional Adhesion MoleculesKidneyMembrane ProteinsMicrofilament ProteinsNectinsafadinCadherinsCalciumCell Adhesion MoleculesJunctional Adhesion MoleculesMembrane ProteinsMicrofilament ProteinsNectinsPhosphoproteinsRecombinant ProteinsTetradecanoylphorbol AcetateZonula Occludens-1 Protein

Identifiers

PMID12400007
OpenAlexW2329282236

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.