Arylsulfatase K, a Novel Lysosomal Sulfatase
Wiegmann E, Westendorf E, Kalus I, Pringle TH, Lübke T, Dierks T (2013)
Journal of Biological Chemistry 288(42): 30019-30028.
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Autor*in
Wiegmann, ElenaUniBi;
Westendorf, EvaUniBi;
Kalus, InaUniBi;
Pringle, Thomas H.;
Lübke, TorbenUniBi ;
Dierks, ThomasUniBi
Einrichtung
Abstract / Bemerkung
The human sulfatase family has 17 members, 13 of which have been characterized biochemically. These enzymes specifically hydrolyze sulfate esters in glycosaminoglycans, sulfolipids, or steroid sulfates, thereby playing key roles in cellular degradation, cell signaling, and hormone regulation. The loss of sulfatase activity has been linked to severe pathophysiological conditions such as lysosomal storage disorders, developmental abnormalities, or cancer. A novel member of this family, arylsulfatase K (ARSK), was identified bioinformatically through its conserved sulfatase signature sequence directing posttranslational generation of the catalytic formylglycine residue in sulfatases. However, overall sequence identity of ARSK with other human sulfatases is low (18-22%). Here we demonstrate that ARSK indeed shows desulfation activity toward arylsulfate pseudosubstrates. When expressed in human cells, ARSK was detected as a 68-kDa glycoprotein carrying at least four N-glycans of both the complex and high-mannose type. Purified ARSK turned over p-nitrocatechol and p-nitrophenyl sulfate. This activity was dependent on cysteine 80, which was verified to undergo conversion to formylglycine. Kinetic parameters were similar to those of several lysosomal sulfatases involved in degradation of sulfated glycosaminoglycans. An acidic pH optimum (4.6) and colocalization with LAMP1 verified lysosomal functioning of ARSK. Further, it carries mannose 6-phosphate, indicating lysosomal sorting via mannose 6-phosphate receptors. ARSK mRNA expression was found in all tissues tested, suggesting a ubiquitous physiological substrate and a so far non-classified lysosomal storage disorder in the case of ARSK deficiency, as shown before for all other lysosomal sulfatases.
Erscheinungsjahr
2013
Zeitschriftentitel
Journal of Biological Chemistry
Band
288
Ausgabe
42
Seite(n)
30019-30028
ISSN
0021-9258
eISSN
1083-351X
Page URI
https://pub.uni-bielefeld.de/record/2623550
Zitieren
Wiegmann E, Westendorf E, Kalus I, Pringle TH, Lübke T, Dierks T. Arylsulfatase K, a Novel Lysosomal Sulfatase. Journal of Biological Chemistry. 2013;288(42):30019-30028.
Wiegmann, E., Westendorf, E., Kalus, I., Pringle, T. H., Lübke, T., & Dierks, T. (2013). Arylsulfatase K, a Novel Lysosomal Sulfatase. Journal of Biological Chemistry, 288(42), 30019-30028. doi:10.1074/jbc.M113.499541
Wiegmann, Elena, Westendorf, Eva, Kalus, Ina, Pringle, Thomas H., Lübke, Torben, and Dierks, Thomas. 2013. “Arylsulfatase K, a Novel Lysosomal Sulfatase”. Journal of Biological Chemistry 288 (42): 30019-30028.
Wiegmann, E., Westendorf, E., Kalus, I., Pringle, T. H., Lübke, T., and Dierks, T. (2013). Arylsulfatase K, a Novel Lysosomal Sulfatase. Journal of Biological Chemistry 288, 30019-30028.
Wiegmann, E., et al., 2013. Arylsulfatase K, a Novel Lysosomal Sulfatase. Journal of Biological Chemistry, 288(42), p 30019-30028.
E. Wiegmann, et al., “Arylsulfatase K, a Novel Lysosomal Sulfatase”, Journal of Biological Chemistry, vol. 288, 2013, pp. 30019-30028.
Wiegmann, E., Westendorf, E., Kalus, I., Pringle, T.H., Lübke, T., Dierks, T.: Arylsulfatase K, a Novel Lysosomal Sulfatase. Journal of Biological Chemistry. 288, 30019-30028 (2013).
Wiegmann, Elena, Westendorf, Eva, Kalus, Ina, Pringle, Thomas H., Lübke, Torben, and Dierks, Thomas. “Arylsulfatase K, a Novel Lysosomal Sulfatase”. Journal of Biological Chemistry 288.42 (2013): 30019-30028.
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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
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
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
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
Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications.
Appel MJ, Bertozzi CR., ACS Chem Biol 10(1), 2015
PMID: 25514000
Appel MJ, Bertozzi CR., ACS Chem Biol 10(1), 2015
PMID: 25514000
Critical issues for the proper diagnosis of Metachromatic Leukodystrophy.
Lorioli L, Cesani M, Regis S, Morena F, Grossi S, Fumagalli F, Acquati S, Redaelli D, Pini A, Sessa M, Martino S, Filocamo M, Biffi A., Gene 537(2), 2014
PMID: 24334127
Lorioli L, Cesani M, Regis S, Morena F, Grossi S, Fumagalli F, Acquati S, Redaelli D, Pini A, Sessa M, Martino S, Filocamo M, Biffi A., Gene 537(2), 2014
PMID: 24334127
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
Kowalewski B, Lübke T, Kollmann K, Braulke T, Reinheckel T, Dierks T, Damme M., J Biol Chem 289(40), 2014
PMID: 25135642
37 References
Daten bereitgestellt von Europe PubMed Central.
Hopwood J., Ballabio A.., 2001
Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship.
Sardiello M, Annunziata I, Roma G, Ballabio A., Hum. Mol. Genet. 14(21), 2005
PMID: 16174644
Sardiello M, Annunziata I, Roma G, Ballabio A., Hum. Mol. Genet. 14(21), 2005
PMID: 16174644
Sulfatases: structure, mechanism, biological activity, inhibition, and synthetic utility.
Hanson SR, Best MD, Wong CH., Angew. Chem. Int. Ed. Engl. 43(43), 2004
PMID: 15493058
Hanson SR, Best MD, Wong CH., Angew. Chem. Int. Ed. Engl. 43(43), 2004
PMID: 15493058
Sulfatases and human disease.
Diez-Roux G, Ballabio A., Annu Rev Genomics Hum Genet 6(), 2005
PMID: 16124866
Diez-Roux G, Ballabio A., Annu Rev Genomics Hum Genet 6(), 2005
PMID: 16124866
Regulation of Wnt signaling and embryo patterning by an extracellular sulfatase.
Dhoot GK, Gustafsson MK, Ai X, Sun W, Standiford DM, Emerson CP Jr., Science 293(5535), 2001
PMID: 11533491
Dhoot GK, Gustafsson MK, Ai X, Sun W, Standiford DM, Emerson CP Jr., Science 293(5535), 2001
PMID: 11533491
Heparan sulfate 6-O-endosulfatases: discrete in vivo activities and functional co-operativity.
Lamanna WC, Baldwin RJ, Padva M, Kalus I, Ten Dam G, van Kuppevelt TH, Gallagher JT, von Figura K, Dierks T, Merry CL., Biochem. J. 400(1), 2006
PMID: 16901266
Lamanna WC, Baldwin RJ, Padva M, Kalus I, Ten Dam G, van Kuppevelt TH, Gallagher JT, von Figura K, Dierks T, Merry CL., Biochem. J. 400(1), 2006
PMID: 16901266
Cloning and characterization of two extracellular heparin-degrading endosulfatases in mice and humans.
Morimoto-Tomita M, Uchimura K, Werb Z, Hemmerich S, Rosen SD., J. Biol. Chem. 277(51), 2002
PMID: 12368295
Morimoto-Tomita M, Uchimura K, Werb Z, Hemmerich S, Rosen SD., J. Biol. Chem. 277(51), 2002
PMID: 12368295
The heparanome--the enigma of encoding and decoding heparan sulfate sulfation.
Lamanna WC, Kalus I, Padva M, Baldwin RJ, Merry CL, Dierks T., J. Biotechnol. 129(2), 2007
PMID: 17337080
Lamanna WC, Kalus I, Padva M, Baldwin RJ, Merry CL, Dierks T., J. Biotechnol. 129(2), 2007
PMID: 17337080
A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency.
Schmidt B, Selmer T, Ingendoh A, von Figura K., Cell 82(2), 1995
PMID: 7628016
Schmidt B, Selmer T, Ingendoh A, von Figura K., Cell 82(2), 1995
PMID: 7628016
Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis.
von Bulow R, Schmidt B, Dierks T, von Figura K, Uson I., J. Mol. Biol. 305(2), 2001
PMID: 11124905
von Bulow R, Schmidt B, Dierks T, von Figura K, Uson I., J. Mol. Biol. 305(2), 2001
PMID: 11124905
Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases.
Dierks T, Lecca MR, Schlotterhose P, Schmidt B, von Figura K., EMBO J. 18(8), 1999
PMID: 10205163
Dierks T, Lecca MR, Schlotterhose P, Schmidt B, von Figura K., EMBO J. 18(8), 1999
PMID: 10205163
Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum.
Dierks T, Schmidt B, von Figura K., Proc. Natl. Acad. Sci. U.S.A. 94(22), 1997
PMID: 9342345
Dierks T, Schmidt B, von Figura K., Proc. Natl. Acad. Sci. U.S.A. 94(22), 1997
PMID: 9342345
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme.
Dierks T, Dickmanns A, Preusser-Kunze A, Schmidt B, Mariappan M, von Figura K, Ficner R, Rudolph MG., Cell 121(4), 2005
PMID: 15907468
Dierks T, Dickmanns A, Preusser-Kunze A, Schmidt B, Mariappan M, von Figura K, Ficner R, Rudolph MG., Cell 121(4), 2005
PMID: 15907468
Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme.
Dierks T, Schmidt B, Borissenko LV, Peng J, Preusser A, Mariappan M, von Figura K., Cell 113(4), 2003
PMID: 12757705
Dierks T, Schmidt B, Borissenko LV, Peng J, Preusser A, Mariappan M, von Figura K., Cell 113(4), 2003
PMID: 12757705
Molecular basis of multiple sulfatase deficiency, mucolipidosis II/III and Niemann-Pick C1 disease - Lysosomal storage disorders caused by defects of non-lysosomal proteins.
Dierks T, Schlotawa L, Frese MA, Radhakrishnan K, von Figura K, Schmidt B., Biochim. Biophys. Acta 1793(4), 2008
PMID: 19124046
Dierks T, Schlotawa L, Frese MA, Radhakrishnan K, von Figura K, Schmidt B., Biochim. Biophys. Acta 1793(4), 2008
PMID: 19124046
The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases.
Cosma MP, Pepe S, Annunziata I, Newbold RF, Grompe M, Parenti G, Ballabio A., Cell 113(4), 2003
PMID: 12757706
Cosma MP, Pepe S, Annunziata I, Newbold RF, Grompe M, Parenti G, Ballabio A., Cell 113(4), 2003
PMID: 12757706
Arylsulfatase G, a novel lysosomal sulfatase.
Frese MA, Schulz S, Dierks T., J. Biol. Chem. 283(17), 2008
PMID: 18283100
Frese MA, Schulz S, Dierks T., J. Biol. Chem. 283(17), 2008
PMID: 18283100
X-linked icthyosis. A sulphatase deficiency.
Koppe G, Marinkovic-Ilsen A, Rijken Y, De Groot WP, Jobsis AC., Arch. Dis. Child. 53(10), 1978
PMID: 727794
Koppe G, Marinkovic-Ilsen A, Rijken Y, De Groot WP, Jobsis AC., Arch. Dis. Child. 53(10), 1978
PMID: 727794
A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy.
Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, Andria G, Petit C, Ballabio A., Cell 81(1), 1995
PMID: 7720070
Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, Andria G, Petit C, Ballabio A., Cell 81(1), 1995
PMID: 7720070
Lysosomal disorders: from storage to cellular damage.
Ballabio A, Gieselmann V., Biochim. Biophys. Acta 1793(4), 2008
PMID: 19111581
Ballabio A, Gieselmann V., Biochim. Biophys. Acta 1793(4), 2008
PMID: 19111581
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, Lubke T, Lullmann-Rauch R, D'Hooge R, Esko JD, Dierks T., Proc. Natl. Acad. Sci. U.S.A. 109(26), 2012
PMID: 22689975
Kowalewski B, Lamanna WC, Lawrence R, Damme M, Stroobants S, Padva M, Kalus I, Frese MA, Lubke T, Lullmann-Rauch R, D'Hooge R, Esko JD, Dierks T., Proc. Natl. Acad. Sci. U.S.A. 109(26), 2012
PMID: 22689975
Molecular cloning and initial characterization of three novel human sulfatases.
Obaya AJ., Gene 372(), 2006
PMID: 16500042
Obaya AJ., Gene 372(), 2006
PMID: 16500042
Proteomics of the lysosome.
Lubke T, Lobel P, Sleat DE., Biochim. Biophys. Acta 1793(4), 2008
PMID: 18977398
Lubke T, Lobel P, Sleat DE., Biochim. Biophys. Acta 1793(4), 2008
PMID: 18977398
Molecular characterization of the human Calpha-formylglycine-generating enzyme.
Preusser-Kunze A, Mariappan M, Schmidt B, Gande SL, Mutenda K, Wenzel D, von Figura K, Dierks T., J. Biol. Chem. 280(15), 2005
PMID: 15657036
Preusser-Kunze A, Mariappan M, Schmidt B, Gande SL, Mutenda K, Wenzel D, von Figura K, Dierks T., J. Biol. Chem. 280(15), 2005
PMID: 15657036
A novel single-chain antibody fragment for detection of mannose 6-phosphate-containing proteins: application in mucolipidosis type II patients and mice.
Muller-Loennies S, Galliciotti G, Kollmann K, Glatzel M, Braulke T., Am. J. Pathol. 177(1), 2010
PMID: 20472886
Muller-Loennies S, Galliciotti G, Kollmann K, Glatzel M, Braulke T., Am. J. Pathol. 177(1), 2010
PMID: 20472886
Molecular characterization and gene disruption of mouse lysosomal putative serine carboxypeptidase 1.
Kollmann K, Damme M, Deuschl F, Kahle J, D'Hooge R, Lullmann-Rauch R, Lubke T., FEBS J. 276(5), 2009
PMID: 19187242
Kollmann K, Damme M, Deuschl F, Kahle J, D'Hooge R, Lullmann-Rauch R, Lubke T., FEBS J. 276(5), 2009
PMID: 19187242
Identification of novel lysosomal matrix proteins by proteome analysis.
Kollmann K, Mutenda KE, Balleininger M, Eckermann E, von Figura K, Schmidt B, Lubke T., Proteomics 5(15), 2005
PMID: 16145712
Kollmann K, Mutenda KE, Balleininger M, Eckermann E, von Figura K, Schmidt B, Lubke T., Proteomics 5(15), 2005
PMID: 16145712
Biosynthesis and transport of cathepsin D in cultured human fibroblasts.
Gieselmann V, Pohlmann R, Hasilik A, Von Figura K., J. Cell Biol. 97(1), 1983
PMID: 6863385
Gieselmann V, Pohlmann R, Hasilik A, Von Figura K., J. Cell Biol. 97(1), 1983
PMID: 6863385
Crystal structure of a covalent intermediate of endogenous human arylsulfatase A.
Chruszcz M, Laidler P, Monkiewicz M, Ortlund E, Lebioda L, Lewinski K., J. Inorg. Biochem. 96(2-3), 2003
PMID: 12888274
Chruszcz M, Laidler P, Monkiewicz M, Ortlund E, Lebioda L, Lewinski K., J. Inorg. Biochem. 96(2-3), 2003
PMID: 12888274
Amino acid residues forming the active site of arylsulfatase A. Role in catalytic activity and substrate binding.
Waldow A, Schmidt B, Dierks T, von Bulow R, von Figura K., J. Biol. Chem. 274(18), 1999
PMID: 10212197
Waldow A, Schmidt B, Dierks T, von Bulow R, von Figura K., J. Biol. Chem. 274(18), 1999
PMID: 10212197
Sorting of lysosomal proteins.
Braulke T, Bonifacino JS., Biochim. Biophys. Acta 1793(4), 2008
PMID: 19046998
Braulke T, Bonifacino JS., Biochim. Biophys. Acta 1793(4), 2008
PMID: 19046998
Proteomics analysis of serum from mutant mice reveals lysosomal proteins selectively transported by each of the two mannose 6-phosphate receptors.
Qian M, Sleat DE, Zheng H, Moore D, Lobel P., Mol. Cell Proteomics 7(1), 2007
PMID: 17848585
Qian M, Sleat DE, Zheng H, Moore D, Lobel P., Mol. Cell Proteomics 7(1), 2007
PMID: 17848585
The mannose 6-phosphate glycoprotein proteome.
Sleat DE, Della Valle MC, Zheng H, Moore DF, Lobel P., J. Proteome Res. 7(7), 2008
PMID: 18507433
Sleat DE, Della Valle MC, Zheng H, Moore DF, Lobel P., J. Proteome Res. 7(7), 2008
PMID: 18507433
Identification of sites of mannose 6-phosphorylation on lysosomal proteins.
Sleat DE, Zheng H, Qian M, Lobel P., Mol. Cell Proteomics 5(4), 2006
PMID: 16399764
Sleat DE, Zheng H, Qian M, Lobel P., Mol. Cell Proteomics 5(4), 2006
PMID: 16399764
The early and late processing of lysosomal enzymes: proteolysis and compartmentation.
Hasilik A., Experientia 48(2), 1992
PMID: 1740186
Hasilik A., Experientia 48(2), 1992
PMID: 1740186
Components and proteolytic processing sites of arylsulfatase B from human placenta.
Kobayashi T, Honke K, Jin T, Gasa S, Miyazaki T, Makita A., Biochim. Biophys. Acta 1159(3), 1992
PMID: 1390929
Kobayashi T, Honke K, Jin T, Gasa S, Miyazaki T, Makita A., Biochim. Biophys. Acta 1159(3), 1992
PMID: 1390929
Structure of a human lysosomal sulfatase.
Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM., Structure 5(2), 1997
PMID: 9032078
Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM., Structure 5(2), 1997
PMID: 9032078
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