Evidence map›Paper›PMID 10510329›Full record

ArticleThe Journal of clinical investigation1999

Heparin-binding protein targeted to mitochondrial compartments protects endothelial cells from apoptosis.

A M Olofsson, M Vestberg, H Herwald, J Rygaard, G David, K E Arfors, V Linde, H Flodgaard, J Dedio, W Müller-Esterl and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Heparin-binding protein is important for vascular leak in sepsis.Intensive care medicine experimental · 2016
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Paracrine control of endothelial cell survival.The Journal of clinical investigation · 1999
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 5 institutions in 4 countries.

A M OlofssonDepartment of Cell and Molecular Biology, Lund University, S-22100 Lund, Sweden.
M Vestberg
H Herwald
J Rygaard
G David
K E Arfors
V Linde
H Flodgaard
J Dedio
W Müller-Esterl
E Lundgren-Akerlund
Lund University · SEJohannes Gutenberg University Mainz · DENovo Nordisk (Denmark) · DKKommunedata (Denmark) · DKKU Leuven · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neutrophil-borne heparin-binding protein (HBP) is a multifunctional protein involved in the progression of inflammation. HBP is stored in neutrophil granules and released upon stimulation of the cells in proximity to endothelial cells. HBP affects endothelial cells in multiple ways; however, the molecular and cellular mechanisms underlying the interaction of HBP with these cells are unknown. Affinity isolation and enzymatic degradation demonstrated that HBP released from human neutrophils binds to endothelial cell-surface proteoglycans, such as syndecans and glypican. Flow cytometry indicated that a significant fraction of proteoglycan-bound HBP is taken up by the endothelial cells, and we used radiolabeled HBP to determine the internalization rate of surface-bound HBP. Confocal and electron microscopy revealed that internalized HBP is targeted to perinuclear compartments of endothelial cells, where it colocalizes with mitochondria. Western blotting of isolated mitochondria from HBP-treated endothelial cells showed that HBP is present in 2 forms - 28 and 22 kDa. Internalized HBP markedly reduced growth factor deprivation-induced caspase-3 activation and protected endothelial cells from apoptosis, suggesting that uptake and intracellular routing of exogenous HBP to mitochondria contributes to the sustained viability of endothelial cells in the context of locally activated neutrophils.

Indexed as

Antimicrobial Cationic PeptidesApoptosisBiological TransportBlood ProteinsCarrier ProteinsCells, CulturedChromatography, AffinityEndothelium, VascularHeparinHumansKineticsLeukotriene B4MitochondriaNeutrophilsN-Formylmethionine Leucyl-PhenylalanineProteoglycansAntimicrobial Cationic PeptidesAZU1 protein, humanBlood ProteinsCarrier ProteinsHeparinLeukotriene B4N-Formylmethionine Leucyl-PhenylalanineProteoglycansRecombinant ProteinsTetradecanoylphorbol Acetate

Identifiers

PMID10510329
PMCPMC408551
OpenAlexW2114986223

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.