The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases
- PMID: 12757706
- DOI: 10.1016/s0092-8674(03)00348-9
The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases
Abstract
In multiple sulfatase deficiency (MSD), a human inherited disorder, the activities of all sulfatases are impaired due to a defect in posttranslational modification. Here we report the identification, by functional complementation using microcell-mediated chromosome transfer, of a gene that is mutated in MSD and is able to rescue the enzymatic deficiency in patients' cell lines. Functional conservation of this gene was observed among distantly related species, suggesting a critical biological role. Coexpression of SUMF1 with sulfatases results in a strikingly synergistic increase of enzymatic activity, indicating that SUMF1 is both an essential and a limiting factor for sulfatases. These data have profound implications on the feasibility of enzyme replacement therapy for eight distinct inborn errors of metabolism.
Comment in
-
A major step on the road to understanding a unique posttranslational modification and its role in a genetic disease.Cell. 2003 May 16;113(4):421-2. doi: 10.1016/s0092-8674(03)00354-4. Cell. 2003. PMID: 12757700 Review.
Similar articles
-
Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme.Cell. 2003 May 16;113(4):435-44. doi: 10.1016/s0092-8674(03)00347-7. Cell. 2003. PMID: 12757705
-
Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency.Hum Mutat. 2004 Jun;23(6):576-81. doi: 10.1002/humu.20040. Hum Mutat. 2004. PMID: 15146462
-
A major step on the road to understanding a unique posttranslational modification and its role in a genetic disease.Cell. 2003 May 16;113(4):421-2. doi: 10.1016/s0092-8674(03)00354-4. Cell. 2003. PMID: 12757700 Review.
-
Multiple Sulfatase Deficiency: A Disease Comprising Mucopolysaccharidosis, Sphingolipidosis, and More Caused by a Defect in Posttranslational Modification.Int J Mol Sci. 2020 May 13;21(10):3448. doi: 10.3390/ijms21103448. Int J Mol Sci. 2020. PMID: 32414121 Free PMC article. Review.
-
Sulfatases and human disease.Annu Rev Genomics Hum Genet. 2005;6:355-79. doi: 10.1146/annurev.genom.6.080604.162334. Annu Rev Genomics Hum Genet. 2005. PMID: 16124866 Review.
Cited by
-
Neonatal gene therapy with a gamma retroviral vector in mucopolysaccharidosis VI cats.Mol Ther. 2012 May;20(5):898-907. doi: 10.1038/mt.2012.9. Epub 2012 Mar 6. Mol Ther. 2012. PMID: 22395531 Free PMC article.
-
Characterization of the human sulfatase Sulf1 and its high affinity heparin/heparan sulfate interaction domain.J Biol Chem. 2009 Oct 9;284(41):28033-28044. doi: 10.1074/jbc.M109.035808. Epub 2009 Aug 7. J Biol Chem. 2009. PMID: 19666466 Free PMC article.
-
Overexpression of inactive arylsulphatase mutants and in vitro activation by light-dependent oxidation with vanadate.Biochem J. 2004 Sep 1;382(Pt 2):581-7. doi: 10.1042/BJ20040447. Biochem J. 2004. PMID: 15175008 Free PMC article.
-
Past, present, and future perspectives of transcription factor EB (TFEB): mechanisms of regulation and association with disease.Cell Death Differ. 2022 Aug;29(8):1433-1449. doi: 10.1038/s41418-022-01028-6. Epub 2022 Jun 23. Cell Death Differ. 2022. PMID: 35739255 Free PMC article. Review.
-
Functional consequences of the subdomain organization of the sulfs.J Biol Chem. 2009 Aug 7;284(32):21505-14. doi: 10.1074/jbc.M109.028472. Epub 2009 Jun 11. J Biol Chem. 2009. PMID: 19520866 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
- Actions
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical
Molecular Biology Databases
Research Materials
