Alternative titles; symbols
Other entities represented in this entry:
HGNC Approved Gene Symbol: ASS1
SNOMEDCT: 1149103000;
Cytogenetic location: 9q34.11 Genomic coordinates (GRCh38) : 9:130,444,707-130,501,274 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 9q34.11 | Citrullinemia | 215700 | Autosomal recessive | 3 |
The ASS1 gene encodes argininosuccinate synthetase-1 (EC 6.3.4.5), a cytosolic urea cycle enzyme mainly expressed in periportal hepatocytes, but also in most other body tissues. The enzyme is a homotetrameric protein composed of 45-kD monomers and is involved in the synthesis of arginine and catalyzes that condensation of citrulline and aspartate to argininosuccinate using ATP (summary by Engel et al., 2009).
Bock et al. (1983) isolated clones corresponding to the ASS1 gene from a human cDNA library. The deduced 412-residue protein has a molecular mass of 46 kD. Haberle et al. (2002) provided a revised sequence for the ASS1 gene. Engel et al. (2009) noted that the enzyme is usually described as having 3 domains: a nucleotide-binding domain, the synthetase domain, and a C-terminal oligomerization domain.
Dennis et al. (1989) cloned and sequenced bovine cDNA for argininosuccinate synthetase and found 96% identity with the deduced human sequence at the amino acid level.
Haberle et al. (2002) determined that the ASS1 gene contains 16 exons. The start codon is in exon 3 and the stop codon in exon 16.
Rabinovich et al. (2015) demonstrated that decreased activity of ASS1 in cancers supports proliferation by facilitating pyrimidine synthesis via CAD (carbamoyl-phosphate synthase 2, aspartate transcarbamylase, and dihydroorotase complex; 114010) activation. The studies were initiated by delineating the consequences of loss of ASS1 activity in humans with 2 types of citrullinemia. Rabinovich et al. (2015) found that in citrullinemia type I (CTLN1; 215700), which is caused by deficiency of ASS1, there is increased pyrimidine synthesis and proliferation compared with citrullinemia type II (CTLN2; see 603471), in which there is decreased substrate availability for ASS1 caused by deficiency of the aspartate transporter citrin (SLC25A13; 603859). Building on these results, Rabinovich et al. (2015) demonstrated that ASS1 deficiency in cancer increases cytosolic aspartate levels, which increases CAD activation by upregulating its substrate availability and by increasing its phosphorylation by S6K1 (608938) through the mammalian target of rapamycin (mTOR; 601231) pathway. Decreasing CAD activity by blocking citrin, the mTOR signaling, or pyrimidine synthesis decreases proliferation and thus may serve as a therapeutic strategy in multiple cancers where ASS1 is downregulated. Rabinovich et al. (2015) concluded that their results demonstrated that ASS1 downregulation is a novel mechanism supporting cancerous proliferation, and their results provided a metabolic link between the urea cycle enzymes and pyrimidine synthesis.
From study of human-hamster cell hybrids, Carritt et al. (1977) concluded that a gene for argininosuccinate synthetase (ASS) is carried by chromosome 9. In a study of 10 citrullinemic cell lines, no complementation was observed (Cathelineau et al., 1981).
Northrup et al. (1989) identified 3 RFLPs within the ASS gene. They found that the ASS gene is located about 0.04 cM from the ABO blood group locus (110300) and is probably centromeric to ABO, between ABO and ABL (189980).
Engel et al. (2009) stated that the functional human ASS1 gene maps to chromosome 9q34.11-q34.12.
Jackson et al. (1990) assigned the murine equivalent to the proximal portion of mouse chromosome 2 by study of recombinant inbred strains.
PSEUDOGENES
Engel et al. (2009) noted that the ASS1 gene has 10 to 14 homologous copies scattered across the human genome. However, only the sequence on chromosome 9q34 seems to encode a functional protein.
Using a cDNA probe for argininosuccinate synthetase, Beaudet et al. (1982) identified 10 or more distinct DNA sequences bearing homology. The only functional sequence is presumably that on chromosome 9, which is mutant in classic citrullinemia. Pseudogenes are situated on several autosomes (including ASSP2 on chromosome 6), on the X chromosome (ASSP4 and ASSP5), and perhaps on the Y chromosome (ASSP6).
Su et al. (1984) mapped pseudogenes for ASS to 2cen-p25, 3qter-q12, 4qter-q21, 5 (2 loci), 6, 7, 9p13-q11, 9q11-q22, 11q, 12, Xpter-p22, Xq22-q26, and Ycen-q11. They emphasized the usefulness of cloned probes in cytogenetic analysis. Such dispersion may have been mediated by a transposable element. McCarrey and Riggs (1986) proposed that determinator-inhibitor pairs are a mechanism for threshold setting in development, and that pseudogenes may serve as the source of intracellular inhibitors. They suggested that the system could function at the RNA level by the pairs taking the form of sense-antisense RNAs or at the protein level via a competitive inhibition mechanism. By PCR amplification of specific sequences in somatic cell hybrids, Todd and Naylor (1992) demonstrated that an ASS pseudogene, which they referred to as ASSP1, maps to 6p23-p12.
Engel et al. (2009) provided a review of mutations in the ASS1 gene. They listed 87 mutations, including 27 novel mutations, in patients with citrullinemia (215700). Mutations are distributed throughout the gene, and it is usually difficult to predict the phenotype based on genotype. However, the G390R mutation (603470.0009) in exon 15 was found to be the single most common mutation in patients with the classic phenotype. Engel et al. (2009) also provided a map of the geographic distribution of ASS1 mutations worldwide.
Type I, or classic, citrullinemia is caused by deficiency of argininosuccinate synthetase. Kinetically abnormal ASS is demonstrable in the liver, kidney, and cultured fibroblasts. Kobayashi et al. (1989) found that since most patients with citrullinemia express stable mRNA in fibroblasts, the disorder is ideally suited for gene amplification with PCR and sequence analysis of mutant cDNA. They sequenced cDNA from 11 independent chromosomes and identified 9 different mutations: 3 showed absence of exon 5, 6 or 7, and 6 showed point mutations. Five of the 6 involved C:G-to-T:A transitions in CpG dinucleotides, and 3 of these resulted in loss of MspI sites. Kobayashi et al. (1990) further demonstrated the marked heterogeneity of mutations causing citrullinemia: among 13 unrelated patients with the neonatal form of the disease, they found 10 different mutations. Seven were single missense mutations. Two had deletions of single exons (exon 7 and exon 13) and one had a G-to-C substitution in the last position of intron 15 resulting in splicing to a cryptic splice site within exon 16.
In the course of studying the molecular nature of mutations in Japanese patients with classic citrullinemia, Kobayashi et al. (1994) found that 10 of 23 affected alleles had the same mutation, deletion of exon 7 (603470.0003). This differed from the situation in the United States, where far greater heterogeneity of mutations had been found. Kobayashi et al. (1995) reported that 20 mutations had been identified in ASS mRNA in classic citrullinemia, including 14 single base changes causing missense mutations, 4 mutations associated with an absence of exons 5, 6, 7, or 13 in mRNA, 1 mutation with a deletion of the first 7 bases in exon 16 (caused by abnormal splicing), and 1 mutation with an insertion of 37 bases between the exon 15 and 16 regions of mRNA. In an extension of their previous studies, Kobayashi et al. (1995) reported that 19 of 33 Japanese ASS alleles had the IVS6AS-2 (603470.0003) mutation.
Most reported patients with citrullinemia have presented with the classic form of the disease. There are also patients with a mild form of citrullinemia in whom the exact molecular basis and clinical relevance are uncertain. Mutations in the ASS gene had not been described in mildly affected or asymptomatic patients with citrullinemia until the work of Haberle et al. (2002), who described the entire genomic DNA sequence and mutations in the ASS gene of patients with both the classic and the mild form of the disease. The mutations gly390 to arg (G390R; 603470.0009), IVS13+5G-A (603470.0017), and arg108 to leu (R108L; 603470.0014) were associated with classic citrullinemia, whereas the mutations trp179 to arg (W179R; 603470.0015) and gly362 to val (G362V; 603470.0016) were detected on alleles of mildly affected patients. These were cases of asymptomatic children with biochemical abnormalities. The authors concluded that the elucidation of the structure of the human ASS gene made it possible to use intronic primers for molecular analysis of patients with mild disease and the classic form, and provided another option for prenatal diagnostics in affected families with the severe type.
In a study of 38 patients with classic citrullinemia, Gao et al. (2003) identified 16 novel mutations in the ASS gene. Previously, 34 different mutations had been described in 50 families worldwide. Three mutations are particularly frequent: G390R (603470.0009) in 18 families, IVS6-2A-G (603470.0003) in 23 families (20 from Japan and 3 from Korea), and R304W (603470.0010) in 10 families (9 from Japan and 1 from Turkey). The clinical course of the patients with truncating mutations or the G390R mutation seemed to be early-onset/severe. The phenotype of patients with certain missense mutations, G362V (603470.0016) or W179R (603470.0015), was late-onset/mild. Eight patients with R86H, A118T, R265H, or K310R showed an adult/onset phenotype and 4 of them showed severe symptoms during pregnancy or postpartum.
In Friesian cattle in Australia, Harper et al. (1986, 1989) reported that citrullinemia-affected calves had a clinical disease similar to the acute neonatal form of citrullinemia in humans. Dennis et al. (1989) cloned and sequenced bovine cDNA for argininosuccinate synthetase and found 96% identity with the deduced human sequence at the amino acid level. Dennis et al. (1989) found, furthermore, a C-to-T transition converting arginine-86 (CGA) to a nonsense codon (TGA). The loss of an AvaII site could be used for rapid, economical, nonradioactive detection of heterozygotes for bovine citrullinemia.
Seidl et al. (2024) generated a morpholino knockdown in zebrafish for ass1. The mutant fish had disorganized midbrain structures in the larval phase and reduced brain size. Neurod1 (601724) and elavl3 (603458) expression were reduced in mutant larvae, consistent with abnormal differentiation of neural progenitor cells. The mutant zebrafish had elevated citrulline and reduced arginine compared to wildtype fish, but ammonia was not elevated. Treating wildtype larvae with L-citrulline did not induce the brain defects observed in the ass1 knockdown fish. Seidl et al. (2024) hypothesized that ASS1 may have a moonlighting effect in brain development distinct from its role in the urea cycle.
Kobayashi et al. (1989) demonstrated deletion of exon 5 in a case of citrullinemia (215700). Kobayashi et al. (1995) stated that this represented deletion of 3 to 4 kb, including the 189-bp exon 5.
Kobayashi et al. (1989) demonstrated deletion of exon 6 in the ASS gene in a case of citrullinemia (215700). Kobayashi et al. (1995) stated that this is a deletion of 2-3 kb, including the 57-bp exon 6.
Kobayashi et al. (1989) demonstrated deletion of exon 7 in the ASS gene in a case of citrullinemia (215700). Kobayashi et al. (1995) found that among Japanese patients with classic citrullinemia, the deletion of exon 7 accounted for 19 of 33 mutant alleles. The mutation is an A-to-G transition at the second nucleotide upstream for the acceptor splice-cleavage site within the 3-prime splice site of intron 6 and creates a new cleavage site for MspI, allowing detection by a combination of PCR and MspI RFLP analysis. Kobayashi et al. (1995) confirmed that 9 patients with type III citrullinemia were homozygotes or compound heterozygotes for the exon 7 deletion. Although undetectable ASS protein is the criterion of type III citrullinemia, a very low amount of ASS crossreacting material was detected in the liver of a patient with this form of the disease.
Kobayashi et al. (1989) demonstrated a change in codon 14 of the ASS gene, GGC (gly) to AGC (ser), in a case of citrullinemia (215700).
Kobayashi et al. (1989) demonstrated a change in codon 157 of the ASS gene, CGC (arg) to CAC (his), in a case of citrullinemia (215700).
Kobayashi et al. (1989) demonstrated a change in codon 180 in the ASS gene, AGC (ser) to AAC (asn), in a case of citrullinemia (215700).
Kobayashi et al. (1989) demonstrated change in codon 324 in the ASS gene, GGT (gly) to AGT (ser), in a case of citrullinemia (215700).
Kobayashi et al. (1989) demonstrated a change in codon 363 in the ASS gene, CGG (arg) to TGG (trp), in a case of citrullinemia (215700).
Kobayashi et al. (1989) demonstrated a change in codon 390 in the ASS gene, GGC (gly) to AGG (arg), in a case of citrullinemia (215700). Five of the 6 single base mutations involved C:G to T:A transitions in CpG dinucleotides.
In a review, Engel et al. (2009) stated that the G390R mutation is the most common mutation in patients with the classic phenotype of citrullinemia.
Kobayashi et al. (1990) demonstrated a change in codon 304 in the ASS gene, CGG (arg) to TGG (trp), in a case of citrullinemia (215700).
Kobayashi et al. (1991) demonstrated an S18L mutation due to a C-to-T transition in a CpG dinucleotide of the ASS gene in a case of citrullinemia (215700).
Kobayashi et al. (1991) described an R86C mutation resulting from a C-to-T transition in a CpG dinucleotide of the ASS gene in a case of citrullinemia (215700). They stated that 8 of 9 missense mutations causing citrullinemia involved similar transitions in CpG dinucleotides. Six of 9 missense mutations in humans occur in amino acid positions that are completely conserved in 4 mammalian species, yeast, and 3 bacterial species. Mutations causing human citrullinemia are extremely heterogeneous; all nonconsanguineous persons studied to 1991 had been found to be compound heterozygotes.
In a citrullinemia (215700) patient carrying an RNA-negative allele, Li et al. (2001) described a C-to-T transition at nucleotide 835 in the cDNA of the ASS gene, converting the CGA arginine codon to a TGA termination codon within exon 12 (R279X). The patient was compound heterozygous for the R279X mutation and the IVS6-2A-G mutation (603470.0003). There was no indication of the R279X mutation leading to altered splicing, and the most likely defect responsible for the mRNA reduction appeared to be nonsense-mediated mRNA decay affecting the abundance of nucleus-associated mRNA. It was estimated that mRNA from the R279X allele was less than 2% of the normal level.
In a patient with classic citrullinemia (215700), Haberle et al. (2002) identified compound heterozygosity for a G-to-T transversion at nucleotide 323 of the ASS gene, resulting in an arg108-to-leu substitution, and a G-to-A transition at the +5 position downstream of the intron 13 donor site (603470.0017).
In 2 sibs of each of 2 families, Haberle et al. (2002) identified a T-to-C transition at nucleotide 535 of the ASS gene, resulting in a trp179-to-arg substitution, associated with mild citrullinemia (see 215700). Both families were of Turkish extraction and the parents were consanguineous. Three of the affected children were asymptomatic. The fourth had mild mental retardation. There was no hyperammonemia in any of the 4. Enzyme assays showed levels of activity varying from 7 to 26%. The plasma levels of citrulline were considerably lower than in classic citrullinemia.
In a Turkish family with consanguineous parents, Haberle et al. (2002) found that asymptomatic citrullinemia (see 215700) was caused by a G-to-T transversion at nucleotide 1085 of the ASS gene, resulting in a gly362-to-val substitution.
See 603470.0014 and Haberle et al. (2002).
In a patient with neonatal citrullinemia (215700), Kobayashi et al. (1990) found a G-to-C transversion in the last nucleotide of intron 15 of the ASS gene. The mutation resulted in a 7-base deletion in exon 16 of ASS mRNA.
Potter et al. (2004) found this mutation in compound heterozygosity with a novel missense mutation (603470.0019) in an adult female patient, diagnosed through newborn screening, who underwent 2 successful pregnancies.
Gucer et al. (2004) identified this homozygous splice site mutation in a girl with severe neonatal citrullinemia who died at age 17 months of early liver cirrhosis and hepatic encephalopathy.
In an adult female with citrullinemia (215700) who had been diagnosed through newborn screening and had been described by Whelan et al. (1976), Potter et al. (2004) found compound heterozygosity for mutations in the ASS gene. A previously described splice site mutation was found in intron 15 (603470.0018); on the other allele a novel missense mutation, a 928A-C transversion in exon 13 resulting in glutamine substituting lysine at codon 310 (K310Q), was found. When described as a child her lack of symptoms despite high citrulline levels was novel. She underwent 2 successful pregnancies.
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Seidl, M. J., Scharre, S., Posset, R., Druck, A. C., Epp, F., Okun, J. G., Dimitrov, B., Hoffmann, G. F., Kolker, S., Zielonka, M. ASS1 deficiency is associated with impaired neuronal differentiation in zebrafish larvae. Molec. Genet. Metab. 141: 108097, 2024. [PubMed: 38113552] [Full Text: https://doi.org/10.1016/j.ymgme.2023.108097]
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