Normal Function
The ARSL gene provides instructions for making an enzyme called arylsulfatase L. This enzyme is part of a group known as sulfatases, which are enzymes that help process molecules that contain chemical groups known as sulfates. Sulfatases play important roles in cartilage and bone development.
Within cells, arylsulfatase L is located in the Golgi apparatus, a structure that modifies newly produced enzymes and other proteins. The function of this enzyme is unknown, although researchers believe it participates in a chemical pathway involving vitamin K. Evidence suggests that vitamin K normally plays a role in bone growth and maintenance of bone density.
Health Conditions Related to Genetic Changes
X-linked chondrodysplasia punctata 1
Genetic changes involving the ARSL gene are responsible for X-linked chondrodysplasia punctata 1, a disorder of bone and cartilage development that occurs almost exclusively in males. Between 60 and 75 percent of males with the characteristic features of this condition have a mutation within the ARSL gene. At least 18 mutations have been found in affected individuals; these genetic changes reduce or eliminate the function of arylsulfatase L. Another 25 percent of affected males have a small deletion of genetic material from the region of the X chromosome that contains the ARSL gene. These individuals are missing the entire gene, so their cells produce no functional arylsulfatase L.
It is unclear how a shortage of arylsulfatase L disrupts the development of bones and cartilage and leads to the characteristic features of X-linked chondrodysplasia punctata 1.
More About This Health ConditionOther Names for This Gene
- ARSE
- ARSE_HUMAN
- arylsulfatase E
- CDPX
- CDPX1
- CDPXR
- MGC163310
Additional Information & Resources
Tests Listed in the Genetic Testing Registry
Scientific Articles on PubMed
Catalog of Genes and Diseases from OMIM
References
- Braverman NE, Bober MB, Brunetti-Pierri N, Suchy SF. Chondrodysplasia Punctata 1, X-Linked. 2008 Apr 22 [updated 2020 Oct 15]. In: Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE, Amemiya A, editors. GeneReviews(R) [Internet]. Seattle (WA): University of Washington, Seattle; 1993-2024. Available from http://www.ncbi.nlm.nih.gov/books/NBK1544/ Citation on PubMed
- Brunetti-Pierri N, Andreucci MV, Tuzzi R, Vega GR, Gray G, McKeown C, Ballabio A, Andria G, Meroni G, Parenti G. X-linked recessive chondrodysplasia punctata: spectrum of arylsulfatase E gene mutations and expanded clinical variability. Am J Med Genet A. 2003 Mar 1;117A(2):164-8. doi: 10.1002/ajmg.a.10950. Citation on PubMed
- Daniele A, Parenti G, d'Addio M, Andria G, Ballabio A, Meroni G. Biochemical characterization of arylsulfatase E and functional analysis of mutations found in patients with X-linked chondrodysplasia punctata. Am J Hum Genet. 1998 Mar;62(3):562-72. doi: 10.1086/301746. Citation on PubMed or Free article on PubMed Central
- Nino M, Matos-Miranda C, Maeda M, Chen L, Allanson J, Armour C, Greene C, Kamaluddeen M, Rita D, Medne L, Zackai E, Mansour S, Superti-Furga A, Lewanda A, Bober M, Rosenbaum K, Braverman N. Clinical and molecular analysis of arylsulfatase E in patients with brachytelephalangic chondrodysplasia punctata. Am J Med Genet A. 2008 Apr 15;146A(8):997-1008. doi: 10.1002/ajmg.a.32159. Citation on PubMed
- Parenti G, Buttitta P, Meroni G, Franco B, Bernard L, Rizzolo MG, Brunetti-Pierri N, Ballabio A, Andria G. X-linked recessive chondrodysplasia punctata due to a new point mutation of the ARSE gene. Am J Med Genet. 1997 Dec 12;73(2):139-43. doi: 10.1002/(sici)1096-8628(19971212)73:23.0.co;2-p. Citation on PubMed
- Sheffield LJ, Osborn AH, Hutchison WM, Sillence DO, Forrest SM, White SJ, Dahl HH. Segregation of mutations in arylsulphatase E and correlation with the clinical presentation of chondrodysplasia punctata. J Med Genet. 1998 Dec;35(12):1004-8. doi: 10.1136/jmg.35.12.1004. Citation on PubMed or Free article on PubMed Central
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