Evidence map›Paper›PMID 28055182›Full record

ArticleACS chemical biology2017

Arylsulfatase K is the Lysosomal 2-Sulfoglucuronate Sulfatase.

Omkar P Dhamale, Roger Lawrence, Elena M Wiegmann, Bhahwal A Shah, Kanar Al-Mafraji, William C Lamanna, Torben Lübke, Thomas Dierks, Geert-Jan Boons, Jeffrey D Esko

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PubMed Full text at PMC Publisher
In one paragraph

Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

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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

10 authors at 3 institutions in 5 countries.

Omkar P DhamaleComplex Carbohydrate Research Center, University of Georgia , Athens, Georgia, United States.
Roger LawrenceDepartment of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego , La Jolla, California, United States.
Elena M WiegmannDepartment of Chemistry, Biochemistry I, Bielefeld University , Bielefeld, Germany.
Bhahwal A ShahComplex Carbohydrate Research Center, University of Georgia , Athens, Georgia, United States.
Kanar Al-MafrajiComplex Carbohydrate Research Center, University of Georgia , Athens, Georgia, United States.
William C LamannaDepartment of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego , La Jolla, California, United States.
Torben LübkeDepartment of Chemistry, Biochemistry I, Bielefeld University , Bielefeld, Germany.
Thomas DierksDepartment of Chemistry, Biochemistry I, Bielefeld University , Bielefeld, Germany.
Geert-Jan BoonsComplex Carbohydrate Research Center, University of Georgia , Athens, Georgia, United States.ORCID 0000-0003-3111-5954
Jeffrey D EskoDepartment of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego , La Jolla, California, United States.ORCID 0000-0001-8322-1834
University of Georgia · USBielefeld University · DEUniversity of California San Diego · US

Funding

Siglec Modulation of Inflammatory ResponsesP01HL107150 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LE, DZUNG T · 2011 to 2017
$18.0M
NHLBI NIH HHS P01 HL107150
6 · The paper itself

Abstract

The degradation of glycosaminoglycans (GAGs) involves a series of exolytic glycosidases and sulfatases that act sequentially on the nonreducing end of the polysaccharide chain. Enzymes have been cloned that catalyze all of the known linkages with the exception of the removal of the 2-O-sulfate group from 2-sulfoglucuronate, which is found in heparan sulfate and dermatan sulfate. Here, we show using synthetic disaccharide substrates that arylsulfatase K is the glucuronate-2-sulfatase. Arylsulfatase K acts selectively on 2-sulfoglucuronate and lacks activity against 2-sulfoiduronate, whereas iduronate-2-sulfatase (IDS) desulfates synthetic disaccharides containing 2-sulfoiduronate but not 2-sulfoglucuronate. As arylsulfatase K has all of the properties expected of a lysosomal enzyme, we conclude that arylsulfatase K is the long sought lysosomal glucuronate-2-sulfatase, which we designate GDS.

Indexed as

ArylsulfatasesChromatography, LiquidGlycosaminoglycansHumansLysosomesMass SpectrometrySubstrate SpecificityARSK protein, humanArylsulfatasesGlycosaminoglycans

Identifiers

PMID28055182
PMCPMC6031138
OpenAlexW2568696345

What OpenQuestion holds

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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.