Evidence map›Paper›PMID 25514086›Full record

ArticleEndocrinology2015

Positive feedback regulation between adiponectin and T-cadherin impacts adiponectin levels in tissue and plasma of male mice.

Keisuke Matsuda, Yuya Fujishima, Norikazu Maeda, Takuya Mori, Ayumu Hirata, Ryohei Sekimoto, Yu Tsushima, Shigeki Masuda, Masaya Yamaoka, Kana Inoue and 5 more

Abstract read
In one paragraph

Article in Endocrinology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
–field-weighted citation impact
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

60 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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
  5. Article
  6. Review
  7. Article
  8. A Novel ELISA System for Measuring Modified LDL-Adiponectin Complex.Journal of atherosclerosis and thrombosis · 2025
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Adiponectin suppresses stiffness-dependent, profibrotic activation of lung fibroblasts.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Observational
  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.

Keisuke MatsudaDepartments of Metabolic Medicine (K.M., Y.F., N.M., T.M., A.H., R.S., Y.T., S.M., M.Y., K.I., H.N., S.K., T.F., I.S.) and Metabolism and Atherosclerosis (A.H., S.K., T.F.), Graduate School of Medicine, Osaka University, Suita, Osaka 565-0871, Japan; and 3Sanford-Burnham Medical Research Institute (B.R.), National Institutes of Health-Designated Cancer Center, Development, Aging, and Regeneration Program, La Jolla, California 92037.
Yuya Fujishima
Norikazu Maeda
Takuya Mori
Ayumu Hirata
Ryohei Sekimoto
Yu Tsushima
Shigeki Masuda
Masaya Yamaoka
Kana Inoue
Hitoshi Nishizawa
Shunbun Kita
Barbara Ranscht
Tohru Funahashi
Iichiro Shimomura

Funding

Adiponectin Functions in HippocampusR21MH103861 · NIMH · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI RANSCHT, BARBARA · 2014 to 2015
$536k
NIMH NIH HHS MH103861NIMH NIH HHS R21 MH103861
6 · The paper itself

Abstract

Adiponectin (Adipo), a multimeric adipocyte-secreted protein abundant in the circulation, is implicated in cardiovascular protective functions. Recent work documented that Adipo locally associates with responsive tissues through interactions with T-cadherin (Tcad), an atypical, glycosylphosphatidylinositol (GPI)-anchored cadherin cell surface glycoprotein. Mice deficient for Tcad lack tissue-associated Adipo, accumulate Adipo in the circulation, and mimic the Adipo knockout (KO) cardiovascular phenotype. In reverse, Tcad protein is visibly reduced from cardiac tissue in Adipo-KO mice, suggesting interdependent regulation of the 2 proteins. Here, we evaluate the effect of Adipo on Tcad protein expression. Adipo and Tcad proteins were colocalized in aorta, heart, and skeletal muscle. Adipo positively regulated levels of Tcad protein in vivo and in endothelial cell (EC) cultures. In Tcad-KO mice, binding of endogenous and exogenously administered Adipo to cardiovascular tissues was dramatically reduced. Consistently, knockdown of Tcad in cultured murine vascular ECs significantly diminished Adipo binding. In search for a possible mechanism, we found that enzymatic cleavage of Tcad with phosphatidylinositol-specific phospholipase C increases plasma Adipo while decreasing tissue-bound levels. Similarly, pretreatment of cultured ECs with serum containing Adipo attenuated phosphatidylinositol-specific phospholipase C-mediated Tcad cleavage. In vivo administration of adenovirus producing Adipo suppressed plasma levels of GPI phospholipase D, the endogenous cleavage enzyme for GPI-anchored proteins. In conclusion, our data show that both circulating and tissue-bound Adipo levels are dependent on Tcad and, in reverse, regulate tissue Tcad levels through a positive feedback loop that operates by suppressing phospholipase-mediated Tcad release from the cell surface.

Indexed as

Feedback, PhysiologicalAdiponectinAnimalsCadherinsCells, CulturedEndothelial CellsEpitopesHumansMaleMiceMice, KnockoutPhosphoinositide Phospholipase CAdiponectinCadherinsEpitopesH-cadherinPhosphoinositide Phospholipase C

Identifiers

PMID25514086
PMCPMC4330303

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.