HGNC Approved Gene Symbol: ARSB
SNOMEDCT: 52677002, 69463008;
Cytogenetic location: 5q14.1 Genomic coordinates (GRCh38): 5:78,777,209-78,985,958 (from NCBI)
Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
---|---|---|---|---|
5q14.1 | Mucopolysaccharidosis type VI (Maroteaux-Lamy) | 253200 | Autosomal recessive | 3 |
The ARSB gene encodes arylsulfatase B (N-acetylgalactosamine 4-sulfatase; EC 3.1.6.12), a lysosomal enzyme that removes the C4 sulfate ester group from the N-acetylgalactosamine sugar residue at the nonreducing terminus of the glycosaminoglycans (GAGs) dermatan sulfate and chondroitin sulfate during lysosomal degradation (Karageorgos et al., 2007).
Schuchman et al. (1990) cloned a full-length ARSB cDNA from a human testes cDNA library. The deduced 533-residue protein has 6 potential N-glycosylation sites. Comparison of the predicted amino acid sequences of arylsulfatases A (ARSA; 607574), B, and C (ARSC; 300747) demonstrated regions of identity, particularly in their N termini.
Kunieda et al. (1995) isolated the rat Arsb gene.
The ARSB gene contains 8 exons and spans about 206 kb (Karageorgos et al., 2007).
Hellkuhl and Grzeschik (1978) assigned a gene for arylsulfatase B to chromosome 5 by human-mouse somatic cell hybrids. By somatic cell hybridization methods, DeLuca et al. (1979) assigned arylsulfatases A and B to chromosomes 22 and 5, respectively. By study of an interstitial deletion of 5q12, Dudin et al. (1984) excluded ARSB and HEXB from this segment.
Fidzianska et al. (1984) assigned the ARSB locus to 5p11-qter by analysis of somatic cell hybrids isolated from 2 separate fusions of human fibroblasts carrying a translocation involving chromosome 5 with a Chinese hamster cell line. By study of rearranged chromosomes in human/hamster hybrids, using a tritium-labeled human genomic DNA fragment for in situ hybridization, Fidzianska et al. (1986) narrowed the assignment of ARSB to 5q11-q13.
Litjens et al. (1989) localized the ARSB gene to 5q13-q14.
By rat/mouse somatic cell hybridization, Kunieda et al. (1995) localized the rat Arsb gene to chromosome 2.
In a patient with mucopolysaccharidosis type VI (253200), Wicker et al. (1991) identified a homozygous mutation in the ARSB gene (611542.0001).
In patients with MPS VI, Jin et al. (1992) identified homozygous or compound heterozygous mutations in the ARSB gene (611532.0002-611542.0004).
In 9 patients with MPS VI, Litjens et al. (1996) identified several mutations in the ARSB gene (see, e.g., 611542.0008-611542.0010). All patients were compound heterozygotes and showed variable phenotypes ranging from mild to severe. For each patient, the combined biochemical phenotypes of the 2 mutant sulfatase alleles demonstrated a good correspondence with the observed clinical phenotype.
Litjens and Hopwood (2001) stated that a total of 45 clinically relevant mutations had been identified in the ARSB gene in patients with mucopolysaccharidosis type VI. Missense mutations represented the largest group, with 31 identified. No common mutations had been described, making screening of the general population difficult.
Karageorgos et al. (2007) identified 83 different ARSB mutations among 105 patients with MPS VI. The most frequent mutation was Y210C (611542.0009), which was identified in 18% of patients and associated with an attenuated phenotype.
Among 12 Spanish and 4 Argentinian patients with MPS VI, Garrido et al. (2007) identified 19 different mutations, including 9 novel mutations, in the ARSB gene. The most common mutant alleles were splice site mutations, 611542.0011 and 611542.0012, which accounted for 21.9% and 12.5% of mutant alleles, respectively.
Tomanin et al. (2018) reviewed all variants in the ARSB gene in patients with MPS VI reported in the literature and in public databases and identified 908 alleles with 198 distinct nonpolymorphic variants from 478 patients. They also identified 3 benign variants that had previously been incorrectly reported as pathogenic. Most (59.5%) unique variants were missense, followed by small deletions (13.5%), nonsense (12.0%), splice site or intronic (5.0%), small duplications (3.0%), and large deletions (3.0%). Of the unique alleles, 31.7% appeared only once, with an additional 28.5% appearing twice. Of the identified patients, 54.8% were homozygous for pathogenic ARSB variants, 35.6% were heterozygous, 9.2% had only one allele reported, and 0.4% had both alleles unidentified. Pathogenic variants in ARSB did not appear to be concentrated in any particular region of the protein. Analysis of the genotype-phenotype correlation based on homozygotes was poorly informative for most variants, although some variants did appear to be associated with a more rapidly progressive phenotype. The authors emphasized the importance of submitting variants to public databases.
Yoshida et al. (1993) reported the clinical, morphologic, and biochemical features of a rat model of MPS VI. Affected rats had facial dysmorphia, dysostosis multiplex, and increased urinary excretion of glucosaminoglycans. Ultrastructural studies revealed storage of GAGs throughout the reticuloendothelial cells, cartilage, and other connective tissues, but no deposition was observed in the nervous system. Biochemical analyses demonstrated that the excreted GAG was dermatan sulfate and the activity of hepatic arylsulfatase B was less than 5% of the normal mean value. Pedigree analysis showed that the phenotype was inherited as an autosomal recessive single trait. Yoshida et al. (1994) demonstrated that the responsible gene lies on rat chromosome 2. It had been known that some loci on rat chromosome 2 correspond to those on human chromosome 5 and mouse chromosome 13. Kunieda et al. (1995) demonstrated furthermore MPS VI in rats was due to a homozygous 1-bp insertion (507insC) in the Arsb gene, resulting in a frameshift and premature termination at codon 258.
Evers et al. (1996) produced a targeted disruption of the Arsb gene in mice and found that homozygous mutant animals exhibited arylsulfatase B enzyme deficiency and elevated urinary secretion of dermatan sulfate. They developed progressive symptoms resembling those of MPS VI in humans. Around 4 weeks of age, facial dysmorphism became overt, long bones were shortened, and pelvic and costal abnormalities were observed. Major alterations in bone formation with perturbed cartilaginous tissues in newborns and widened, perturbed, and persisting growth plates in adult animals were seen. All major parenchymal organs showed storage of glycosaminoglycans preferentially in interstitial cells and macrophages. Affected mice were fertile and mortality was not elevated up to 15 months of age.
McGovern et al. (1985) studied the mutant arylsulfatase B enzymes in homozygotes for separately ascertained cat lines with MPS VI. They showed that the enzymes were distinguishable in physicokinetic and immunologic properties as well as in ability to dimerize with normal enzyme in heterozygotes.
Yogalingam et al. (1996) studied the Arsb (feline f4S) gene in MPS VI Siamese cats. They cloned the gene from a normal feline heart cDNA library, sequenced it, and identified a missense mutation (leu476pro; L476P) in the gene in MPS VI cats. Expression of the normal f4S gene, accompanied by mannose-6-phosphate (M6P), corrected the lysosomal storage of undegraded sulfated glycosaminoglycans in these cells. The observation suggested that expression of the normal f4S gene in MPS VI myoblasts is predominantly mediated by an M6P receptor (154540).
Crawley et al. (1996) used a feline model of MPS VI to investigate enzyme replacement therapy. They evaluated tissue distribution and clinical efficacy of 3 forms of recombinant human N-acetylgalactosamine-4-sulfatase. Intravenously administered enzyme was rapidly cleared from the circulation. The majority of the enzyme was distributed to the liver but was also detected in most other tissues. Tissue half-life was approximately 2-4 days. In 3 MPS VI cats, regular intravenous infusions of recombinant enzyme for up to 20 months showed variable reduction of storage vacuoles in Kupffer cells and connective tissues; however, cartilage chondrocytes remained vacuolated. Vertebral bone mineral volume was improved in 2 MPS VI cats in which therapy was initiated before skeletal maturity, and increased bone volume appeared to correlate with earlier age of onset of therapy. One cat showed greater mobility in response to therapy. Crawley et al. (1996) suggested that, given their results, significant reduction in disease progression and tissue pathology might be expected in patients with this disorder.
Crawley et al. (1997) reported a dose-related response effect of enzyme replacement therapy in MPS VI cats treated from birth. The evidence came from clinical, biochemical, and histopathologic observations.
Crawley et al. (1998) stated that the family of cats with MPS VI used for testing the efficacy of enzyme replacement therapy were homozygous for the L476P substitution in the Arsb gene. An additional mutation, asp520asn (D520N), inherited independently from L476P and identified in the same family of cats, resulted in 3 clinical phenotypes: L476P homozygotes exhibited dwarfism and facial dysmorphia due to epiphyseal dysplasia, abnormal low leukocyte 4S/beta-hexosaminidase ratios, dermatan sulfaturia, lysosomal inclusions in most tissues (including chondrocytes), corneal clouding, degenerative joint disease, and abnormal leukocyte inclusions. Similarly, D520N/D520N and L476P/D520N cats had abnormally low leukocyte 4S/beta-hexosaminidase ratios, mild dermatan sulfaturia, lysosomal inclusions in some chondrocytes, and abnormal leukocyte inclusions; however, both had normal growth and appearance. In addition, L476P/D520N cats had a high incidence of degenerative joint disease. Crawley et al. (1998) concluded that L476P/D520N cats have a very mild MPS VI phenotype not previously described in MPS VI humans. Yogalingam et al. (1998), from the same group, also reported biochemical and clinical assessment of L476P homozygous, D520N/L476P compound heterozygous, and D520N homozygous cats. They showed that the entire range of clinical phenotypes, from severe MPS VI, to mild MPS VI, to normal were clustered within a narrow range of residual 4S activity from 0.5 to 4.6% of normal levels. The results suggested that the D520N mutation causes a rapid degradation of 4S protein. The effect of this is partially ameliorated as a result of a significant elevation in the specific activity of mutant D520N 4S reaching the lysosomes.
In a patient with mucopolysaccharidosis type VI (MPS6; 253200), born of consanguineous parents, Wicker et al. (1991) identified a homozygous 410G-T transversion in the ARSB gene, resulting in a gly137-to-val (G137V) substitution. The mutation did not affect protein synthesis, but severely reduced protein stability. The phenotype was of intermediate severity.
In a patient with severe mucopolysaccharidosis type VI (MPS6; 253200), Jin et al. (1992) identified a homozygous 349T-C transition in the ARSB gene, resulting in a cys117-to-arg (C117R) substitution. The patient's cultured fibroblasts showed about 2% of normal arylsulfatase B activity compared to a value of about 7% in cultured fibroblasts from a patient with mild MPS6 (L236P; 611542.0003).
In a patient with mild mucopolysaccharidosis type VI (MPS6; 253200), Jin et al. (1992) identified compound heterozygosity for 2 mutations in the ARSB gene: a 707T-C transition resulting in a leu236-to-pro (L236P) substitution, and a 1214G-A transition resulting in a cys405-to-tyr (C405Y; 611542.0004) substitution. The patient's cultured fibroblasts showed about 7% of normal arylsulfatase B activity compared to a value of about 2% in cultured fibroblasts from a patient with severe MPS6 (C117R; 611542.0002).
For discussion of the cys405-to-tyr (C405Y) mutation in the ARSB gene that was found in compound heterozygous state in a patient with mild mucopolysaccharidosis type VI (MPS6; 253200) by Jin et al. (1992), see 611542.0003.
In an 11-year-old boy with severe mucopolysaccharidosis type VI (MPS6; 253200), Litjens et al. (1992) identified a homozygous 1-bp deletion (238delG), resulting in a frameshift and premature termination at codon 113. As an infant, he had coarse dysmorphic features, advanced bone age, dysostosis multiplex, and corneal clouding. Hydrocephalus required shunting at 4 years, and cervical cord compression resulting from upper cervical instability required surgical stabilization at 6 years of age.
In a child with a severe form of Maroteaux-Lamy syndrome (MPS6; 253200), Isbrandt et al. (1996) identified compound heterozygosity for 2 deletions in the ARSB gene. One allele carried a 1-bp deletion (743delC) in exon 4 resulting in a frameshift and premature termination. The protein was predicted to be 221 amino acids, which is less than 42% of the 533 amino acid wildtype enzyme. The second allele carried an 11-bp deletion in exon 1 and a leu72-to-gln substitution (611542.0007). The patient presented at 2.5 years with facial dysmorphism, scoliosis and dysostosis multiplex, corneal clouding, hepatomegaly, and umbilical hernia. At age 7 years, he had short stature, severe kyphoscoliosis, restriction of joint movement, and pyramidal symptoms.
In a child with severe Maroteaux-Lamy syndrome (MPS6; 253200), Isbrandt et al. (1996) found a 1-bp deletion in the ARSB gene (611542.0006) and an 11-bp deletion which resulted in premature termination and a shortened protein predicted to be less than 23% of the length of the wildtype enzyme. In addition to the 11-bp deletion, they observed a 215T-A transversion resulting in a leu72-to-gln (L72Q) substitution on the same allele.
In a patient with a severe form of mucopolysaccharidosis type VI (MPS6; 253200), Litjens et al. (1996) identified compound heterozygosity for 2 mutations in the ARSB gene: a 284G-A transition resulting in an arg95-to-gln (R95Q) substitution, and H393P (611542.0010). She presented at age 13 months with mild developmental delay, thoracolumbar kyphosis, hepatosplenomegaly, and skeletal changes characteristic of the disorder. In another family, 2 sibs with a mild form of MPS6 were compound heterozygous for R95Q and Y210C (611542.0009). Functional expression studies in CHO cells showed that the R95Q mutant retained about 0.02% residual activity.
In 2 sibs with a mild form of mucopolysaccharidosis type VI (MPS6; 253200), Litjens et al. (1996) identified compound heterozygosity for 2 mutations in the ARSB gene: a 629A-G transition resulting in a tyr210-to-cys (Y210C) substitution, and R95Q (611542.0008). An additional unrelated patient with an intermediate phenotype was compound heterozygous for Y210C and H393P (611542.0010). Functional expression studies in CHO cells showed that the Y210C mutant retained about 2% residual activity.
In a patient with a severe form of mucopolysaccharidosis type VI (MPS6; 253200), Litjens et al. (1996) identified compound heterozygosity for 2 mutations in the ARSB gene: a 1178A-C transversion resulting in a his393-to-pro (H393P) substitution, and R95Q (611542.0008) Functional expression studies in CHO cells showed that the H393P mutant expressed no ARSB protein and thus had no residual activity.
Garrido et al. (2007) identified a G-to-C transversion in intron 5 of the ARSB gene (1143-1G-C) in 21.9% of mutant alleles from 16 Spanish and Argentinian patients with mucopolysaccharidosis type VI (MPS6; 253200). RT-PCR analysis showed that the mutation resulted in the skipping of exon 6 and premature termination. Haplotype analysis indicated a founder effect.
Garrido et al. (2007) identified a T-to-G transversion in intron 5 of the ARSB gene (1143-8T-G) in 12.5% of mutant alleles from 16 Spanish and Argentinian patients with mucopolysaccharidosis type VI (MPS6; 253200). RT-PCR analysis showed that the mutation resulted in the skipping of exon 6 and premature termination. Haplotype analysis indicated a founder effect.
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