Evidence map›Paper›PMID 19536613›Full record

ArticleMedical molecular morphology2009

Cell-surface arylsulfatase A and B on sinusoidal endothelial cells, hepatocytes, and Kupffer cells in mammalian livers.

Keiko Mitsunaga-Nakatsubo, Shinichiro Kusunoki, Hayato Kawakami, Koji Akasaka, Yoshihiro Akimoto

Abstract read
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Article in Medical molecular morphology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Arylsulfatase B is reduced in prostate cancer recurrences.Cancer biomarkers : section A of Disease markers · 2017
    Article
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  14. Extra-lysosomal localization of arylsulfatase B in human colonic epithelium.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2011
    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

5 authors at 4 institutions in 1 country.

Keiko Mitsunaga-NakatsuboDepartment of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Hiroshima, Japan.
Shinichiro Kusunoki
Hayato Kawakami
Koji Akasaka
Yoshihiro Akimoto
Kyorin University · JPHiroshima University · JPSony Computer Science Laboratories · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arylsulfatase A (ARSA) and B (ARSB) have been regarded as lysosomal enzymes because of their hydrolytic activity on synthetic aromatic substrates and the lysosomal localization of their enzymatic activity. Using sea urchin embryos, we previously demonstrated that the bulk of ARS is located on the cell surface of the epithelium, colocalizing with sulfated polysaccharides, and that it does not exhibit enzymatic activity. To examine whether ARSA and ARSB exist on the cell surface in mammalian tissues, we raised antibodies against ARSA and ARSB and examined immunohistochemically their localization in the liver using light and electron microscopy. Here we show that mammalian ARSA and ARSB exist on the cell surface of sinusoidal endothelial cells, hepatocytes, and sinusoidal macrophages (Kupffer cells), as well as in the lysosome. They are also colocalized with heparan sulfate proteoglycan. These results suggest that ARSA and ARSB also may function in the cell surface of mammals. This is the first report to show cell-surface localization of ARS in mammalian somatic cells. The extracellular localization of ARS will provide new insight for human ARS deficiency disorders, such as metachromatic leukodystrophy and mucopolysaccharidosis VI.

Indexed as

AnimalsAntibodiesBlotting, WesternCerebroside-SulfataseEndothelial CellsHepatocytesKupffer CellsLiverMaleMembrane ProteinsMiceMice, Inbred ICRMicroscopy, FluorescenceMicroscopy, ImmunoelectronN-Acetylgalactosamine-4-SulfataseRatsAntibodiesCerebroside-SulfataseMembrane ProteinsN-Acetylgalactosamine-4-Sulfatase

Identifiers

PMID19536613
OpenAlexW2056395141

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.