Evidence map›Paper›PMID 21075844›Full record

ArticleThe Journal of biological chemistry2011

Serglycin is a major proteoglycan in polarized human endothelial cells and is implicated in the secretion of the chemokine GROalpha/CXCL1.

Astri J Meen, Inger Øynebråten, Trine M Reine, Annette Duelli, Katja Svennevig, Gunnar Pejler, Trond Jenssen, Svein O Kolset

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

35 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Matrix proteoglycans in tumor inflammation and immunity.American journal of physiology. Cell physiology · 2022
    Review
  6. International journal of molecular sciences · 2022
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
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  18. Syndecan-4 is a major syndecan in primary human endothelial cells in vitro, modulated by inflammatory stimuli and involved in wound healing.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2015
    Article
  19. 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

8 authors at 3 institutions in 4 countries.

Astri J MeenDepartment of Nutrition, University of Oslo, Box 1046, Blindern, 0316 Oslo, Norway.
Inger Øynebråten
Trine M Reine
Annette Duelli
Katja Svennevig
Gunnar Pejler
Trond Jenssen
Svein O Kolset
University of Oslo · NOSwedish University of Agricultural Sciences · SEKidney Associates · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteoglycan (PG) expression was studied in primary human umbilical vein endothelial cells (HUVEC). RT-PCR analyses showed that the expression of the PG serglycin core protein was much higher than that of the extracellular matrix PG decorin and the cell surface PG syndecan-1. PG biosynthesis was further studied by biosynthetic [(35)S]sulfate labeling of polarized HUVEC. Interestingly, a major part of (35)S-PGs was secreted to the apical medium. A large portion of these PGs was trypsin-resistant, a typical feature of serglycin. The trypsin-resistant PGs were mainly of the chondroitin/dermatan sulfate type but also contained a minor heparan sulfate component. Secreted serglycin was identified by immunoprecipitation as a PG with a core protein of ∼30 kDa. Serglycin was furthermore shown to be present in perinuclear regions and in two distinct types of vesicles throughout the cytoplasm using immunocytochemistry. To search for possible serglycin partner molecules, HUVEC were stained for the chemokine growth-related oncogene α (GROα/CXCL1). Co-localization with serglycin could be demonstrated, although not in all vesicles. Serglycin did not show overt co-localization with tissue-type plasminogen activator-positive vesicles. When PG biosynthesis was abrogated using benzyl-β-D-xyloside, serglycin secretion was decreased, and the number of vesicles with co-localized serglycin and GROα was reduced. The level of GROα in the apical medium was also reduced after xyloside treatment. Together, these findings indicate that serglycin is a major PG in human endothelial cells, mainly secreted to the apical medium and implicated in chemokine secretion.

Indexed as

Cell PolarityChemokine CXCL1DecorinEndothelial CellsGene Expression RegulationGlycosidesHumansPlasminogen ActivatorsProteoglycansSecretory VesiclesUmbilical VeinsVesicular Transport Proteinsbenzyl-beta-D-xylosideChemokine CXCL1CXCL1 protein, humanDCN protein, humanDecorinGlycosidesPlasminogen ActivatorsProteoglycansserglycinVesicular Transport Proteins

Identifiers

PMID21075844
PMCPMC3024759
OpenAlexW2046617409

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.