Evidence map›Paper›PMID 26515055›Full record

ArticleHistochemistry and cell biology2016

Hyaluronidase 2 (HYAL2) is expressed in endothelial cells, as well as some specialized epithelial cells, and is required for normal hyaluronan catabolism.

Biswajit Chowdhury, Richard Hemming, Sana Faiyaz, Barbara Triggs-Raine

Abstract read
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In one paragraph

Article in Histochemistry and cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Elucidating the clinical spectrum and molecular basis of HYAL2 deficiency.Genetics in medicine : official journal of the American College of Medical Genetics · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Hyaluronan in inflammatory bowel disease: Cross-linking inflammation and coagulation.Matrix biology : journal of the International Society for Matrix Biology · 2019
    Review
  13. Article
  14. Review
  15. Article
  16. Oncotarget · 2017
    Article
  17. Article
  18. 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 2 institutions in 1 country.

Biswajit ChowdhuryDepartments of Biochemistry and Medical Genetics, University of Manitoba, 745 Bannatyne Ave, Winnipeg, MB, R3E 0J9, Canada.
Richard HemmingDepartments of Biochemistry and Medical Genetics, University of Manitoba, 745 Bannatyne Ave, Winnipeg, MB, R3E 0J9, Canada.
Sana FaiyazDepartments of Biochemistry and Medical Genetics, University of Manitoba, 745 Bannatyne Ave, Winnipeg, MB, R3E 0J9, Canada.
Barbara Triggs-RaineDepartments of Biochemistry and Medical Genetics, University of Manitoba, 745 Bannatyne Ave, Winnipeg, MB, R3E 0J9, Canada. Barbara.Triggs-Raine@umanitoba.ca.ORCID http://orcid.org/0000-0003-4719-6779
University of Manitoba · CAManitoba Health · CA

Funding

Canadian Institutes of Health Research MP-89873
6 · The paper itself

Abstract

Hyaluronidase 2 (HYAL2) is a membrane-anchored protein that is proposed to initiate the degradation of hyaluronan (HA) in the extracellular matrix. The distribution of HYAL2 in tissues, and of HA in tissues lacking HYAL2, is largely unexplored despite the importance of HA metabolism in several disease processes. Herein, we use immunoblot and histochemical analyses to detect HYAL2 and HA in mouse tissues, as well as agarose gel electrophoresis to examine the size of HA. HYAL2 was detected in all tissues that were examined, including the brain. It was localized to the surface and cytoplasm of endothelial cells, as well as specialized epithelial cells in several tissues, including the skin. Accumulated HA, often of higher molecular mass than that in control tissues, was detected in tissues from Hyal2 (-/-) mice. The accumulating HA was located near to where HYAL2 is normally found, although in some tissues, it was distant from the site of HYAL2 localization. Overall, HYAL2 was highest in tissues that remove HA from the circulation (liver, lymph node and spleen), but the levels of HA accumulation in Hyal2 (-/-) mice were highest in tissues that catabolize locally synthesized HA. Our results support HYAL2's role as an extracellular enzyme that initiates HA breakdown in somatic tissues. However, our findings also suggest that HYAL2 contributes to HA degradation through other routes, perhaps as a soluble or secreted form.

Indexed as

AnimalsElectrophoresis, Agar GelEndothelial CellsEpithelial CellsExtracellular MatrixGPI-Linked ProteinsHyaluronic AcidHyaluronoglucosaminidaseImmunoblottingImmunohistochemistryMiceMice, KnockoutGPI-Linked ProteinsHyal2 protein, mouseHyaluronic AcidHyaluronoglucosaminidaseGlycosaminoglycanHyaluronanHyaluronidase 2Matrix degradationMouse model

Identifiers

PMID26515055
OpenAlexW1857570296

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.