Evidence map›Paper›PMID 9700172›Full record

ArticleThe Journal of cell biology1998

Interactions of the cytoplasmic domain of P-selectin with clathrin-coated pits enhance leukocyte adhesion under flow.

H Setiadi, G Sedgewick, S L Erlandsen, R P McEver

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Adhesion molecules in CNS disorders: biomarker and therapeutic targets.CNS & neurological disorders drug targets · 2013
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Rolling cell adhesion.Annual review of cell and developmental biology · 2010
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

4 authors at 3 institutions in 1 country.

H SetiadiDepartment of Medicine, University of Oklahoma Health Sciences Center, and Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104, USA.
G Sedgewick
S L Erlandsen
R P McEver
University of Oklahoma Health Sciences Center · USOklahoma Medical Research Foundation · USUniversity of Minnesota · US

Funding

Signal-dependent neutrophil adhesion to vascular surfacesR01HL034363 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI MCEVER, RODGER PAUL · 1985 to 2017
$3.9M
CYTOPLASMIC REGULATION OF P-SELECTIN/PSGL-1 INTERACTIONSR37HL034363 · NHLBI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI MCEVER, RODGER PAUL · 1998 to 2007
$3.3M
NHLBI NIH HHS HL 34363NHLBI NIH HHS R01 HL034363NHLBI NIH HHS R37 HL034363
6 · The paper itself

Abstract

Flowing leukocytes tether to and roll on P-selectin, a receptor on endothelial cells that is rapidly internalized in clathrin-coated pits. We asked whether the association of P-selectin with clathrin-coated pits contributes to its adhesive function. Under flow, rolling neutrophils accumulated efficiently on CHO cells expressing wild-type P-selectin or a P-selectin construct with a substitution in the cytoplasmic domain that caused even faster internalization than that of the wild-type protein. By contrast, far fewer rolling neutrophils accumulated on CHO cells expressing P-selectin constructs with a deletion or a substitution in the cytoplasmic domain that impaired internalization. Neutrophils rolled on the internalization-competent constructs with greater adhesive strength, slower velocity, and more uniform motion. Flowing neutrophils tethered equivalently to internalization-competent or internalization-defective P-selectin, but after tethering, they rolled further on internalization-competent P-selectin. Confocal microscopy demonstrated colocalization of alpha-adaptin, a component of clathrin-coated pits, with wild-type P-selectin, but not with P-selectin lacking the cytoplasmic domain. Treatment of CHO cells or endothelial cells with hypertonic medium reversibly impaired the clathrin-mediated internalization of P-selectin and its ability to support neutrophil rolling. Interactions of the cytoplasmic domain of P-selectin with clathrin-coated pits provide a novel mechanism to enhance leukocyte adhesion under flow.

Indexed as

Adaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAnimalsCell AdhesionCells, CulturedCHO CellsClathrinCoated Pits, Cell-MembraneCricetinaeEndocytosisEndothelium, VascularHumansMembrane ProteinsNeutrophilsP-SelectinRheologyAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportClathrinMembrane ProteinsP-Selectin

Identifiers

PMID9700172
PMCPMC2148165
OpenAlexW2088900101

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.