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 (2014)
The Journal of biological chemistry 289(40): 27992-28005.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ; ;
Abstract
Arylsulfatase G (ARSG) is a recently identified lysosomal sulfatase that was shown to be responsible for the degradation of 3-O-sulfated N-sulfoglucosamine residues of heparan sulfate glycosaminoglycans. Deficiency of ARSG leads to a new type of mucopolysaccharidosis, as described in a mouse model. Here, we provide a detailed molecular characterization of the endogenous murine enzyme. ARSG is expressed and proteolytically processed in a tissue-specific manner. The 63-kDa single-chain precursor protein localizes to pre-lysosomal compartments and tightly associates with organelle membranes, most likely the endoplasmic reticulum. In contrast, proteolytically processed ARSG fragments of 34-, 18-, and 10-kDa were found in lysosomal fractions and lost their membrane association. The processing sites and a disulfide bridge between the 18- and 10-kDa chains could be roughly mapped. Proteases participating in the processing were identified as cathepsins B and L. Proteolytic processing is dispensable for hydrolytic sulfatase activity in vitro. Lysosomal transport of ARSG in the liver is independent of mannose 6-phosphate, sortilin, and Limp2. However, mutation of glycosylation site N-497 abrogates transport of ARSG to lysosomes in human fibrosarcoma cells, due to impaired mannose 6-phosphate modification.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

Kowalewski B, Lübke T, Kollmann K, et al. Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY. The Journal of biological chemistry. 2014;289(40):27992-28005.
Kowalewski, B., Lübke, T., Kollmann, K., Braulke, T., Reinheckel, T., Dierks, T., & Damme, M. (2014). Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY. The Journal of biological chemistry, 289(40), 27992-28005.
Kowalewski, B., Lübke, T., Kollmann, K., Braulke, T., Reinheckel, T., Dierks, T., and Damme, M. (2014). Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY. The Journal of biological chemistry 289, 27992-28005.
Kowalewski, B., et al., 2014. Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY. The Journal of biological chemistry, 289(40), p 27992-28005.
B. Kowalewski, et al., “Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY”, The Journal of biological chemistry, vol. 289, 2014, pp. 27992-28005.
Kowalewski, B., Lübke, T., Kollmann, K., Braulke, T., Reinheckel, T., Dierks, T., Damme, M.: Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY. The Journal of biological chemistry. 289, 27992-28005 (2014).
Kowalewski, Björn, Lübke, Torben, Kollmann, Katrin, Braulke, Thomas, Reinheckel, Thomas, Dierks, Thomas, and Damme, Markus. “Molecular Characterization of Arylsulfatase G: EXPRESSION, PROCESSING, GLYCOSYLATION, TRANSPORT, AND ACTIVITY”. The Journal of biological chemistry 289.40 (2014): 27992-28005.
This data publication is cited in the following publications:
This publication cites the following data publications:

2 Citations in Europe PMC

Data provided by Europe PubMed Central.

Sanfilippo syndrome: causes, consequences, and treatments.
Fedele AO., Appl Clin Genet 8(), 2015
PMID: 26648750
Mannose 6-phosphate-independent Lysosomal Sorting of LIMP-2.
Blanz J, Zunke F, Markmann S, Damme M, Braulke T, Saftig P, Schwake M., Traffic 16(10), 2015
PMID: 26219725

60 References

Data provided by Europe PubMed Central.

I-cell disease-like phenotype in mice deficient in mannose 6-phosphate receptors.
Dittmer F, Hafner A, Ulbrich EJ, Moritz JD, Schmidt P, Schmahl W, Pohlmann R, Figura KV., Transgenic Res. 7(6), 1998
PMID: 10341453
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
Proteolytic excision of a repressive loop domain in tartrate-resistant acid phosphatase by cathepsin K in osteoclasts.
Ljusberg J, Wang Y, Lang P, Norgard M, Dodds R, Hultenby K, Ek-Rylander B, Andersson G., J. Biol. Chem. 280(31), 2005
PMID: 15929988
Heparanase processing by lysosomal/endosomal protein preparation.
Cohen E, Atzmon R, Vlodavsky I, Ilan N., FEBS Lett. 579(11), 2005
PMID: 15848168
Maturation of human tripeptidyl-peptidase I in vitro.
Golabek AA, Wujek P, Walus M, Bieler S, Soto C, Wisniewski KE, Kida E., J. Biol. Chem. 279(30), 2004
PMID: 15143070
Activation and oligomerization of aspartylglucosaminidase.
Saarela J, Laine M, Tikkanen R, Oinonen C, Jalanko A, Rouvinen J, Peltonen L., J. Biol. Chem. 273(39), 1998
PMID: 9737998

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 25135642
PubMed | Europe PMC

Search this title in

Google Scholar