Evidence map›Paper›PMID 19112104›Full record

ArticleThe Journal of biological chemistry2009

Secreted cyclophilin A, a peptidylprolyl cis-trans isomerase, mediates matrix assembly of hensin, a protein implicated in epithelial differentiation.

Hu Peng, Soundarapandian Vijayakumar, Cordelia Schiene-Fischer, Hui Li, Jeffrey M Purkerson, Miroslav Malesevic, Jürgen Liebscher, Qais Al-Awqati, George J Schwartz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Peptidyl prolylCommunications biology · 2019
    Article
  5. Review
  6. Renal acid-base regulation: new insights from animal models.Pflugers Archiv : European journal of physiology · 2015
    Review
  7. Collecting duct intercalated cell function and regulation.Clinical journal of the American Society of Nephrology : CJASN · 2015
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Deletion of hensin/DMBT1 blocks conversion of beta- to alpha-intercalated cells and induces distal renal tubular acidosis.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Regulated acid-base transport in the collecting duct.Pflugers Archiv : European journal of physiology · 2009
    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

9 authors at 4 institutions in 2 countries.

Hu PengDepartment of Pediatrics, University of Rochester School of Medicine, Rochester, New York 14642, USA.
Soundarapandian Vijayakumar
Cordelia Schiene-Fischer
Hui Li
Jeffrey M Purkerson
Miroslav Malesevic
Jürgen Liebscher
Qais Al-Awqati
George J Schwartz
University of Rochester · USMax Planck Research Unit for Enzymology of Protein Folding · DEColumbia University · USHumboldt-Universität zu Berlin · DE

Funding

BICARBONATE TRANSPORT BY THE MATURING RENAL TUBULER01DK050603 · NIDDK · UNIVERSITY OF ROCHESTER · PI SCHWARTZ, GEORGE J · 1995 to 2014
$4.8M
ACTIVE H+ TRANSPORT IN URINARY ACIDIFICATIONR01DK020999 · NIDDK · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI AL-AWQATI, QAIS · 1994 to 2006
$2.8M
ACTIVE H+ TRANSPORT IN URINARY ACIDIFICATIONR37DK020999 · NIDDK · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI AL-AWQATI, QAIS · 1986 to 1993
–
NIDDK NIH HHS DK-20999NIDDK NIH HHS DK-50603NIDDK NIH HHS R01 DK020999
6 · The paper itself

Abstract

Hensin is a rabbit ortholog of DMBT1, a multifunctional, multidomain protein implicated in the regulation of epithelial differentiation, innate immunity, and tumorigenesis. Hensin in the extracellular matrix (ECM) induced morphological changes characteristic of terminal differentiation in a clonal cell line (clone C) of rabbit kidney intercalated cells. Although hensin is secreted in monomeric and various oligomeric forms, only the polymerized ECM form is able to induce these phenotypic changes. Here we report that hensin secretion and matrix assembly were inhibited by the peptidylprolyl cis-trans isomerase (PPIase) inhibitors cyclosporin A (CsA) and a derivative of cyclosporin A with modifications in the d-Ser side chain (Cs9) but not by the calcineurin pathway inhibitor FK506. PPIase inhibition led to failure of hensin polymerization in the medium and ECM, plus the loss of apical cytoskeleton, apical microvilli, and the columnar epithelial shape of clone C cells. Cyclophilin A was produced and secreted into the media to a much greater extent than cyclophilins B and C. Our results also identified the direct CsA-sensitive interaction of cyclophilin A with hensin, suggesting that cyclophilin A is the PPIase that mediates the polymerization and matrix assembly of hensin. These results are significant because this is the first time a direct role of peptidylprolyl cis-trans isomerase activity has been implicated in the process of epithelial differentiation.

Indexed as

AnimalsCell LineCyclophilin ACyclosporineCytoskeletonEnzyme InhibitorsEpithelial CellsExtracellular MatrixExtracellular Matrix ProteinsImmunosuppressive AgentsKidneyRabbitsReceptors, ScavengerTacrolimusCyclophilin ACyclosporineEnzyme InhibitorsExtracellular Matrix Proteinshensin protein, rabbitImmunosuppressive AgentsReceptors, ScavengerTacrolimus

Identifiers

PMID19112104
PMCPMC2649100
OpenAlexW2092951247

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.