Evidence map›Paper›PMID 28325833›Full record

ArticleThe Journal of biological chemistry2017

The unique prodomain of T-cadherin plays a key role in adiponectin binding with the essential extracellular cadherin repeats 1 and 2.

Shiro Fukuda, Shunbun Kita, Yoshinari Obata, Yuya Fujishima, Hirofumi Nagao, Shigeki Masuda, Yoshimitsu Tanaka, Hitoshi Nishizawa, Tohru Funahashi, Junichi Takagi and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. CaAntibodies (Basel, Switzerland) · 2026
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  3. Article
  4. Article
  5. Review
  6. Observational
  7. T-cadherin, a major adiponectin binding partner, suppresses ERK signaling in metabolic tissues.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Review
  9. Article
  10. Article
  11. A Novel ELISA System for Measuring Modified LDL-Adiponectin Complex.Journal of atherosclerosis and thrombosis · 2025
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Observational
  20. 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

12 authors at 2 institutions in 1 country.

Shiro FukudaFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Shunbun KitaFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan, shunkita@endmet.med.osaka-u.ac.jp.
Yoshinari ObataFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Yuya FujishimaFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Hirofumi NagaoFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Shigeki MasudaFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Yoshimitsu TanakaFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Hitoshi NishizawaFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Tohru FunahashiFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Junichi Takagithe Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.
Norikazu MaedaFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Iichiro ShimomuraFrom the Department of Metabolic Medicine, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Osaka University · JPProtein Research Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adiponectin, an adipocyte-derived circulating protein, accumulates in the heart, vascular endothelium, and skeletal muscles through an interaction with T-cadherin (T-cad), a unique glycosylphosphatidylinositol-anchored cadherin. Recent studies have suggested that this interaction is essential for adiponectin-mediated cardiovascular protection. However, the precise protein-protein interaction between adiponectin and T-cad remains poorly characterized. Using ELISA-based and surface plasmon analyses, we report here that T-cad fused with IgG Fc as a fusion tag by replacing its glycosylphosphatidylinositol-anchor specifically bound both hexameric and larger multimeric adiponectin with a dissociation constant of ∼1.0 nm and without any contribution from other cellular or serum factors. The extracellular T-cad repeats 1 and 2 were critical for the observed adiponectin binding, which is required for classical cadherin-mediated cell-to-cell adhesion. Moreover, the 130-kDa prodomain-bearing T-cad, uniquely expressed on the cell surface among members of the cadherin family and predominantly increased by adiponectin, contributed significantly to adiponectin binding. Inhibition of prodomain-processing by a prohormone convertase inhibitor increased 130-kDa T-cad levels and also enhanced adiponectin binding to endothelial cells both by more preferential cell-surface localization and by higher adiponectin-binding affinity of 130-kDa T-cad relative to 100-kDa T-cad. The preferential cell-surface localization of 130-kDa T-cad relative to 100-kDa T-cad was also observed in normal mice aorta

Indexed as

AdiponectinAnimalsCadherinsCalciumCell AdhesionCell MembraneCHO CellsCricetinaeCricetulusDisulfidesEndothelial CellsEnzyme-Linked Immunosorbent AssayGlycosylphosphatidylinositolsHEK293 CellsHumansImmunoglobulin GAdiponectinCadherinsCalciumDisulfidesGlycosylphosphatidylinositolsH-cadherinImmunoglobulin Gadipokineadiponectincadherincell surface proteinglycosylphosphatidylinositol (GPI anchor)protein domainprotein-protein interaction

Identifiers

PMID28325833
PMCPMC5427265
OpenAlexW2602367518

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.