Arylsulfatase G, a novel lysosomal sulfatase

Frese M-A, Schulz S, Dierks T (2008)

Zeitschriftenaufsatz | Veröffentlicht | Englisch
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
Frese, Marc-Andre; Schulz, Stefanie; Dierks, ThomasUniBi
Abstract / Bemerkung
The sulfatases constitute a conserved family of enzymes that specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. By modifying the sulfation state of their substrates, sulfatases play a key role in the control of physiological processes, including cellular degradation, cell signaling, and hormone regulation. The loss of sulfatase activity has been linked with various severe pathophysiological conditions such as lysosomal storage disorders, developmental abnormalities, or cancer. A novel member of this family, arylsulfatase G (ASG), was initially described as an enzyme lacking in vitro arylsulfatase activity and localizing to the endoplasmic reticulum. Contrary to these results, we demonstrate here that ASG does indeed have arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. The activity of ASG depends on the Cys-84 residue that is predicted to be post-translationally converted to the critical active site C-alpha-formylglycine. Phosphate acts as a strong, competitive ASG inhibitor. ASG is active as an unprocessed 63-kDa monomer and shows an acidic pH optimum as typically seen for lysosomal sulfatases. In transfected cells, ASG accumulates within lysosomes as indicated by indirect immunofluorescence microscopy. Furthermore, ASG is a glycoprotein that binds specifically to mannose 6-phosphate receptors, corroborating its lysosomal localization. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ASG that might be associated with a so far non-classified lysosomal storage disorder.
Page URI


Frese M-A, Schulz S, Dierks T. Arylsulfatase G, a novel lysosomal sulfatase. JOURNAL OF BIOLOGICAL CHEMISTRY. 2008;283(17):11388-11395.
Frese, M. - A., Schulz, S., & Dierks, T. (2008). Arylsulfatase G, a novel lysosomal sulfatase. JOURNAL OF BIOLOGICAL CHEMISTRY, 283(17), 11388-11395.
Frese, Marc-Andre, Schulz, Stefanie, and Dierks, Thomas. 2008. “Arylsulfatase G, a novel lysosomal sulfatase”. JOURNAL OF BIOLOGICAL CHEMISTRY 283 (17): 11388-11395.
Frese, M. - A., Schulz, S., and Dierks, T. (2008). Arylsulfatase G, a novel lysosomal sulfatase. JOURNAL OF BIOLOGICAL CHEMISTRY 283, 11388-11395.
Frese, M.-A., Schulz, S., & Dierks, T., 2008. Arylsulfatase G, a novel lysosomal sulfatase. JOURNAL OF BIOLOGICAL CHEMISTRY, 283(17), p 11388-11395.
M.-A. Frese, S. Schulz, and T. Dierks, “Arylsulfatase G, a novel lysosomal sulfatase”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 283, 2008, pp. 11388-11395.
Frese, M.-A., Schulz, S., Dierks, T.: Arylsulfatase G, a novel lysosomal sulfatase. JOURNAL OF BIOLOGICAL CHEMISTRY. 283, 11388-11395 (2008).
Frese, Marc-Andre, Schulz, Stefanie, and Dierks, Thomas. “Arylsulfatase G, a novel lysosomal sulfatase”. JOURNAL OF BIOLOGICAL CHEMISTRY 283.17 (2008): 11388-11395.

19 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Expression, activity and localization of lysosomal sulfatases in Chronic Obstructive Pulmonary Disease.
Weidner J, Jogdand P, Jarenbäck L, Åberg I, Helihel D, Ankerst J, Westergren-Thorsson G, Bjermer L, Erjefält JS, Tufvesson E., Sci Rep 9(1), 2019
PMID: 30760748
A homozygous founder missense variant in arylsulfatase G abolishes its enzymatic activity causing atypical Usher syndrome in humans.
Khateb S, Kowalewski B, Bedoni N, Damme M, Pollack N, Saada A, Obolensky A, Ben-Yosef T, Gross M, Dierks T, Banin E, Rivolta C, Sharon D., Genet Med 20(9), 2018
PMID: 29300381
Arylsulfatase K is the Lysosomal 2-Sulfoglucuronate Sulfatase.
Dhamale OP, Lawrence R, Wiegmann EM, Shah BA, Al-Mafraji K, Lamanna WC, Lübke T, Dierks T, Boons GJ, Esko JD., ACS Chem Biol 12(2), 2017
PMID: 28055182
Homologous expression and biochemical characterization of the arylsulfatase from Kluyveromyces lactis and its relevance in milk processing.
Stressler T, Leisibach D, Lutz-Wahl S, Kuhn A, Fischer L., Appl Microbiol Biotechnol 100(12), 2016
PMID: 26875879
Matching the Diversity of Sulfated Biomolecules: Creation of a Classification Database for Sulfatases Reflecting Their Substrate Specificity.
Barbeyron T, Brillet-Guéguen L, Carré W, Carrière C, Caron C, Czjzek M, Hoebeke M, Michel G., PLoS One 11(10), 2016
PMID: 27749924
Sanfilippo syndrome: causes, consequences, and treatments.
Fedele AO., Appl Clin Genet 8(), 2015
PMID: 26648750
Molecular characterization of arylsulfatase G: expression, processing, glycosylation, transport, and activity.
Kowalewski B, Lübke T, Kollmann K, Braulke T, Reinheckel T, Dierks T, Damme M., J Biol Chem 289(40), 2014
PMID: 25135642
Discovery of a novel iota carrageenan sulfatase isolated from the marine bacterium Pseudoalteromonas carrageenovora.
Genicot SM, Groisillier A, Rogniaux H, Meslet-Cladière L, Barbeyron T, Helbert W., Front Chem 2(), 2014
PMID: 25207269
Arylsulfatase K, a novel lysosomal sulfatase.
Wiegmann EM, Westendorf E, Kalus I, Pringle TH, Lübke T, Dierks T., J Biol Chem 288(42), 2013
PMID: 23986440
The prevalence of nine genetic disorders in a dog population from Belgium, the Netherlands and Germany.
Broeckx BJ, Coopman F, Verhoeven GE, Van Haeringen W, van de Goor L, Bosmans T, Gielen I, Saunders JH, Soetaert SS, Van Bree H, Van Neste C, Van Nieuwerburgh F, Van Ryssen B, Verelst E, Van Steendam K, Deforce D., PLoS One 8(9), 2013
PMID: 24069350
Evaluation of sulfatase-directed quinone methide traps for proteomics.
Lenger J, Schröder M, Ennemann EC, Müller B, Wong CH, Noll T, Dierks T, Hanson SR, Sewald N., Bioorg Med Chem 20(2), 2012
PMID: 21570853
Arylsulfatase G inactivation causes loss of heparan sulfate 3-O-sulfatase activity and mucopolysaccharidosis in mice.
Kowalewski B, Lamanna WC, Lawrence R, Damme M, Stroobants S, Padva M, Kalus I, Frese MA, Lübke T, Lüllmann-Rauch R, D'Hooge R, Esko JD, Dierks T., Proc Natl Acad Sci U S A 109(26), 2012
PMID: 22689975
Action of polystyrene nanoparticles of different sizes on lysosomal function and integrity.
Fröhlich E, Meindl C, Roblegg E, Ebner B, Absenger M, Pieber TR., Part Fibre Toxicol 9(), 2012
PMID: 22789069
Complex actions of estradiol-3-sulfate in late gestation fetal brain.
Winikor J, Schlaerth C, Rabaglino MB, Cousins R, Sutherland M, Wood CE., Reprod Sci 18(7), 2011
PMID: 21273638
Genetic variations in ATP2B1, CSK, ARSG and CSMD1 loci are related to blood pressure and/or hypertension in two Korean cohorts.
Hong KW, Go MJ, Jin HS, Lim JE, Lee JY, Han BG, Hwang SY, Lee SH, Park HK, Cho YS, Oh B., J Hum Hypertens 24(6), 2010
PMID: 19960030
A canine Arylsulfatase G (ARSG) mutation leading to a sulfatase deficiency is associated with neuronal ceroid lipofuscinosis.
Abitbol M, Thibaud JL, Olby NJ, Hitte C, Puech JP, Maurer M, Pilot-Storck F, Hédan B, Dréano S, Brahimi S, Delattre D, André C, Gray F, Delisle F, Caillaud C, Bernex F, Panthier JJ, Aubin-Houzelstein G, Blot S, Tiret L., Proc Natl Acad Sci U S A 107(33), 2010
PMID: 20679209
Proteomics of the lysosome.
Lübke T, Lobel P, Sleat DE., Biochim Biophys Acta 1793(4), 2009
PMID: 18977398
Cell-surface arylsulfatase A and B on sinusoidal endothelial cells, hepatocytes, and Kupffer cells in mammalian livers.
Mitsunaga-Nakatsubo K, Kusunoki S, Kawakami H, Akasaka K, Akimoto Y., Med Mol Morphol 42(2), 2009
PMID: 19536613
Characterization of the human sulfatase Sulf1 and its high affinity heparin/heparan sulfate interaction domain.
Frese MA, Milz F, Dick M, Lamanna WC, Dierks T., J Biol Chem 284(41), 2009
PMID: 19666466

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

PMID: 18283100
PubMed | Europe PMC

Suchen in

Google Scholar