Evidence map›Paper›PMID 14633607›Full record

ArticleThe American journal of pathology2003

Nephrin promotes cell-cell adhesion through homophilic interactions.

Jamshid Khoshnoodi, Kristmundur Sigmundsson, Lars-Göran Ofverstedt, Ulf Skoglund, Björn Obrink, Jorma Wartiovaara, Karl Tryggvason

Open access · greenAbstract read
In one paragraph

Article in The American journal of pathology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

50 citing papers in PubMed, 147 citations in OpenAlex.

  1. Podocin oligomers regulate the ordering of nephrin chains, providing the molecular basis ofProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Interactions between Phase-Separated Liquids and Membrane Surfaces.Applied sciences (Basel, Switzerland) · 2021
    Article
  8. Article
  9. Review
  10. Kirrel3-Mediated Synapse Formation Is Attenuated by Disease-Associated Missense Variants.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Avian Podocytes, Which Lack Nephrin, Use Adherens Junction Proteins at Intercellular Junctions.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2016
    Article
  18. Role of Neuropilin-1 in Diabetic Nephropathy.Journal of clinical medicine · 2015
    Review
  19. Review series: The cell biology of renal filtration.The Journal of cell biology · 2015
    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

7 authors at 2 institutions in 2 countries.

Jamshid KhoshnoodiDepartments of Medical Biochemistry and Biophysics and Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.
Kristmundur Sigmundsson
Lars-Göran Ofverstedt
Ulf Skoglund
Björn Obrink
Jorma Wartiovaara
Karl Tryggvason
Karolinska Institutet · SEUniversity of Helsinki · FI

Funding

NEPHRIN AND KIDNEY FUNCTION AND DISEASER01DK054724 · NIDDK · KAROLINSKA INSTITUTE · PI TRYGGVASON, KARL · 1999 to 2001
$368k
NIDDK NIH HHS DK-54724
6 · The paper itself

Abstract

Nephrin is a type-1 transmembrane protein and a key component of the podocyte slit diaphragm, the ultimate glomerular plasma filter. Genetic and acquired diseases affecting expression or function of nephrin lead to severe proteinuria and distortion or absence of the slit diaphragm. Here, we showed by using a surface plasmon resonance biosensor that soluble recombinant variants of nephrin, containing the extracellular part of the protein, interact with each other in a specific and concentration-dependent manner. This molecular interaction was increased by twofold in the presence of physiological Ca(2+)concentration, indicating that the binding is not dependent on, but rather promoted by Ca(2+). Furthermore, transfected HEK293 cells and an immortalized mouse podocyte cell line overexpressing full-length human nephrin formed cellular aggregates, with cell-cell contacts staining strongly for nephrin. The distance between plasma membranes at the nephrin-containing contact sites was shown by electron microscopy to be 40 to 50 nm, similar to the width of glomerular slit diaphragm. The cell contacts could be dissociated with antibodies reacting with the first two extracellular Ig-like domains of nephrin. Wild-type HEK293 cells were shown to express slit diaphragm components CD2AP, P-cadherin, FAT, and NEPH1. The results show that nephrin molecules exhibit homophilic interactions that could promote cellular contacts through direct nephrin-nephrin interactions, and that the other slit diaphragm components expressed could contribute to that interaction.

Indexed as

AnimalsCell AdhesionCell CommunicationCell LineGenetic VariationHumansKidneyMembrane ProteinsMiceProteinsProtein Structure, TertiaryRecombination, GeneticSolubilityMembrane ProteinsnephrinProteins

Identifiers

PMID14633607
PMCPMC1892394
OpenAlexW2091474389

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.