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Fibroblasts did not exhibit aspartoacylase activity. Paper-7751869.
Aspartoacylase activity in skin fibroblasts was deficient. Paper-7840922.
Canavan disease: molecular basis of aspartoacylase deficiency. Paper-8229603.
In the absence of leupeptin, 90% of aspartoacylase activity is lost. Paper-7392510.
Aspartoacylase deficiency and Canavan disease in Saudi Arabia. Paper-6612200.
Mutational analysis of aspartoacylase: implications for Canavan disease. Paper-13198530.
The smoothest surface for Aspa was obtained with a silicon carbide disk. Paper-3074833.
Fibroblasts from the patient are deficient in aspartoacylase activity. Paper-5735662.
Human aspartoacylase is coded by six exons intervened by five introns. Paper-132782.
Cranial ultrasound findings in aspartoacylase deficiency ( Canavan disease). Paper-7622005.
SSIEM Award. Aspartoacylase deficiency: the enzyme defect in Canavan disease. Paper-6180500.
Cultured skin fibroblasts from the patient showed no aspartoacylase activity. Paper-10103690.
Structure of aspartoacylase, the brain enzyme impaired in Canavan disease. Paper-12401238.
Prenatal detection of Canavan disease ( aspartoacylase deficiency) by DNA analysis. Paper-8123434.
Mutation analysis of the aspartoacylase gene in non-Jewish patients with Canavan disease. Paper-12051587.
Aspartoacylase ( ASPA) synthesizing cells, oligodendrocytes, are lost in CD. Paper-10895175.
Finished surface texture, abrasion resistance, and porosity of Aspa glass-ionomer cement. Paper-3074833.
Characterization of human aspartoacylase: the brain enzyme responsible for canavan disease. Paper-11834248.
Novel splice site mutation of aspartoacylase gene in a Turkish patient with Canavan disease. Paper-2144819.
A knockout mouse for CD which was engineered, also has ASPA deficiency and elevated NAA. Paper-12051582.
Aspartoacylase deficiency and N-acetylaspartic aciduria in patients with Canavan disease. Paper-6210595.
Aspartoacylase deficiency and N-acetylaspartic aciduria in patients with Canavan disease. Paper-6101789.
The aspartoacylase assay affords a new tool for determining the diagnosis of Canavan disease. Paper-6101789.
Variable course of Canavan disease in two boys with early infantile aspartoacylase deficiency. Paper-7179077.
Upregulation of aspartoacylase seen in diabetes is due to advanced glycation end-products. Paper-12442235.
Deficiency of ASPA leads to elevation of N-acetyl-L-aspartic acid (NAA) in the brain and urine. Paper-10021075.
The spectrum of mutations of the aspartoacylase gene in Canavan disease in non-Jewish patients. Paper-1981611.
N-acetylaspartic acid (NAA) is converted into aspartate and acetate by aspartoacylase. Paper-13489163.
The molecular basis of canavan (aspartoacylase deficiency) disease in European non-Jewish patients. Paper-347478.
All nine mutations identified in non-Jewish patients reside in exons 4-6 of the aspartoacylase gene. Paper-347478.
A partial deletion of the aspartoacylase gene is the cause of Canavan disease in a family from Mexico. Paper-8763181.
Effects of AAV-2-mediated aspartoacylase gene transfer in the tremor rat model of Canavan disease. Paper-11107475.
Aspartoacylase metabolizes N-acetylaspartic acid to produce L-aspartate and acetate. Paper-10163917.
Canavan, an autosomal-recessive neurodegenerative disease, is caused by a deficiency of aspartoacylase. Paper-1448367.
The release of fluoride from a glass ionomer cement ( ASPA) was compared with that from a silicate cement. Paper-2841165.
Ultrasound findings in follow-up investigations in a case of aspartoacylase deficiency ( canavan disease). Paper-9723456.
Both patients were found to be compound heterozygotes for C914A (A305E) and G212A (R71H) mutations in ASPA. Paper-11402444.
Canavan disease is an infantile neurodegenerative disease that is due to aspartoacylase deficiency. Paper-347478.
Consistent with its role in supplying acetate for myelin lipid synthesis, ASPA is thought to be cytoplasmic. Paper-12248186.
Aspartoacylase activity in this latter group is protected to the same extent by the presence of leupeptin. Paper-7392510.
Mild-onset presentation of Canavan's disease associated with novel G212A point mutation in aspartoacylase gene. Paper-11402444.
As a result of aspartoacylase deficiency, NAA builds up in extracellular fluids (ECF) and is excreted in urine. Paper-1271695.
In conclusion, the effect of hASP on fatty acid esterification is not influenced by feed restriction. Paper-9400205.
Canavan disease, an inherited leukodystrophy, is caused by mutations in the aspartoacylase ( ASPA) gene. Paper-9625006.
INTRODUCTION: Canavan disease is a megalencephalic leukodystrophy due to deficiency of the enzyme aspartoacylase. Paper-13142641.
Deficient aspartoacylase activity in cultured fibroblasts or brain biopsy confirmed the diagnosis in all patients. Paper-6634385.
A description is give of the effect on the ASPA cement reaction of tartaric acid incorporated in the cement liquid. Paper-2447131.
The bovine aspa gene has also been cloned, and its exon/ intron organization is identical to that of the human gene. Paper-132782.
Canavan disease is an autosomal recessive leukodystrophy caused by the deficiency of aspartoacylase ( ASPA). Paper-8064945.
Human acylation-stimulating protein ( hASP) up-regulates triacylglycerol synthesis in human adipocytes. Paper-9400205.
Rapid detection of three large novel deletions of the aspartoacylase gene in non-Jewish patients with Canavan disease. Paper-12181655.
Prenatal diagnosis has been undertaken in 17 pregnancies in 15 families at risk for aspartoacylase deficiency. Paper-7762424.
The aspartoacylase assay is a new tool for determining both the prenatal and antenatal diagnosis of Canavan disease. Paper-6656794.
The deficiency of aspartoacylase leads to increased concentration of N-acetylaspartic acid in brain and body fluids. Paper-10141040.
A radiometric assay for aspartoacylase activity in human fibroblasts: application for the diagnosis of Canavan's disease. Paper-6854856.
Canavan disease (CD) is an autosomal recessive leukodystrophy caused by deficiency of aspartoacylase ( ASPA). Paper-10021075.
Adeno-associated virus-mediated aspartoacylase gene transfer to the brain of knockout mouse for canavan disease. Paper-10021075.
Here we describe the occurrence of ASPA within nuclei of rat brain and kidney, and in cultured rodent oligodendrocytes. Paper-12248186.
Coincident neuraminidase and aspartoacylase deficiency associated with chromosome 9Q paracentric inversion in a Saudi family. Paper-7354916.
Identification and characterization of novel mutations of the aspartoacylase gene in non-Jewish patients with Canavan disease. Paper-9625006.
We have developed a PCR assay named ASPA (allele-specific primer amplification) to determine the HPA-5a and -5b genotypes. Paper-8168173.
Canavan disease is inherited as an autosomal recessive trait that is caused by the deficiency of aspartoacylase ( ASPA). Paper-575250.
An aspartoacylase deficiency in humans is responsible for Canavan disease, a lethal autosomal recessive leukodystrophy. Paper-10163917.
Reliable prenatal diagnosis of Canavan disease ( aspartoacylase deficiency): comparison of enzymatic and metabolite analysis. Paper-7762424.
Two novel aspartoacylase gene ( ASPA) missense mutations specific to Norwegian and Swedish patients with Canavan disease. Paper-9308270.
The altered NAA metabolism has been traced to mutations in the gene encoding ASPA, located on chromosome 17 (17p13-ter). Paper-11488906.
The biochemical marker for this disease is increased levels of N-acetylaspartic acid, due to the defective enzyme, aspartoacylase. Paper-1988645.
Mutation detection in the aspartoacylase gene in 17 patients with Canavan disease: four new mutations in the non-Jewish population. Paper-8663324.
Aspartoacylase catalyzes hydrolysis of N-acetyl-l-aspartate to aspartate and acetate in the vertebrate brain. Paper-12401238.
Aspartoacylase gene transfer to the mammalian central nervous system with therapeutic implications for Canavan disease. Paper-8404449.
The patients with sialidosis had normal aspartoacylase activity, while neuraminidase activity in the patients with ICNSSD was reduced. Paper-7354916.
Mutations in the gene for ASPA result in the fatal leukodystrophy Canavan disease, for which there is currently no effective treatment. Paper-13125373.
A glutamate at position 273 is located central to the strongly conserved INEAAY motif and corresponds to a glutamate-285 in human ASPA. Paper-1135075.
On the cellular level, aspartoacylase immunoreactivity is restricted to oligodendrocyte somata in both white and gray matter. Paper-10163917.
The disease is caused by deficiency of aspartoacylase, the enzyme responsible for the hydrolysis of NAA into acetate and l-aspartate. Paper-13424582.
Aspartoacylase catalyzes the deacetylation of N-acetylaspartic acid ( NAA) in the brain to produce acetate and L-aspartate. Paper-9670582.
PURPOSE: Canavan disease, caused by a deficiency of aspartoacylase, is one of the most common cerebral degenerative diseases of infancy. Paper-13066897.
Are astrocytes the missing link between lack of brain aspartoacylase activity and the spongiform leukodystrophy in canavan disease? Paper-13895884.
A new sensitive method for measuring aspartoacylase activity in human skin fibroblasts using [3H]N-acetyl-L-aspartic acid (NAA) is described. Paper-6854856.
To examine the mechanism of this enzyme the genes encoding murine and human aspartoacylase were cloned and expressed in Escherichia coli. Paper-9670582.
Canavan disease is an infantile neurodegenerative disease that is caused by mutations in the gene encoding the enzyme aspartoacylase. Paper-1981611.
The tremor rat is a spontaneous epilepsy model with a seizure phenotype caused by a deletion in the aspartoacylase ( ASPA) gene. Paper-11107475.
Aspartoacylase was assayed in cultured skin fibroblasts from one patient of each family and a profound deficiency of this enzyme was found. Paper-6101789.
Canavan disease (CD), an autosomal recessive neurodegenerative disorder, is caused by mutations in the aspartoacylase ( ASPA) gene. Paper-12181655.
Canavan disease, or spongy degeneration of the brain, is a severe leukodystrophy caused by the deficiency of aspartoacylase ( ASPA). Paper-132782.
In the present study, the ASPA gene was analysed in 22 unrelated non-Jewish patients with Canavan disease, and 24 different mutations were found. Paper-9625006.
Canavan disease (CD) is a genetic degenerative brain disorder associated with mutations of the gene encoding aspartoacylase ( ASPA). Paper-13895884.
Since both TAC and TAT code for tyrosine, this sequence polymorphism has no effect on the amino acid sequence of the ASPA protein. Paper-1751181.
Deglycosylation of aspartoacylase or mutation at the glycosylation site causes decreased enzyme stability and diminished catalytic activity. Paper-11834248.
ASPA releases acetate by deacetylation of N-acetylaspartate (NAA), a highly abundant amino acid derivative in the central nervous system. Paper-12049651.
Unreliable verification of prenatal diagnosis of Canavan disease: aspartoacylase activity in deficient and normal fetal skin fibroblasts. Paper-8123438.
Canavan disease occurs more frequently among Ashkenazi Jewish individuals with two predominant mutations in the aspartoacylase ( ASPA) gene. Paper-2144819.
Canavan disease is a severe, progressive leukodystrophy with an autosomal recessive inheritance, caused by aspartoacylase ( ASPA) deficiency. Paper-11488906.
An aspartoacylase deficiency, with concomitant accumulation of NAA, is responsible for Canavan disease, a lethal autosomal recessive disorder. Paper-9670582.
NAA is transported from neurons to the cytoplasm of oligodendrocytes, where ASPA cleaves the acetate moiety for use in fatty acid and steroid synthesis. Paper-13125373.
Does ASPA gene mutation in Canavan disease alter oligodendrocyte development? A tissue culture study of ASPA KO mice brain. Paper-12051588.
Recently the disease has been related to N-acetylaspartic aciduria and deficiency of aspartoacylase, an enzyme possibly involved in the myelin synthesis. Paper-7206757.
A second mutation was found in exon 6, 863 A-->G in aspartoacylase complementary DNA, causing a tyrosine-to-cysteine (Y288C) amino acid substitution. Paper-10103690.
Glass ionomer cement ( ASPA) was inserted in unconditioned class V cavities or in contact with polished ground surfaces of enamel and dentine in twelve teeth. Paper-3615270.
Canavan disease is caused by mutations in aspartoacylase, the enzyme that degrades N-acetylaspartate ( NAA) into acetate and aspartate. Paper-8361580.
The structures also provide a structural framework necessary for understanding the deleterious effects of many missense mutations of human aspartoacylase. Paper-12401238.
Clinical protocol. Gene therapy of Canavan disease: AAV-2 vector for neurosurgical delivery of aspartoacylase gene ( ASPA) to the human brain. Paper-9290996.
We compared phenotypes identified by serological testing and genotypes identified by RHD Multiplex PCR and D(VII) specific ASPA PCR. Paper-8546596.
The results would enable accurate genetic counseling in the families of 13 (68.4%) of 19 patients, in whom two mutations were identified in the aspartoacylase cDNA. Paper-347478.
Diagnosis was based on elevated N-acetylaspartate in urine, reduced aspartoacylase activity in fibroblasts, and marked white matter changes on cerebral imaging. Paper-11286101.
Prenatal diagnosis has been difficult using the enzyme assay owing to the low activity of aspartoacylase in cultured chorionic villus samples or amniocytes. Paper-7554841.
It is characterized by developmental delay, severe hypotonia and early death, and is caused by a deficiency of aspartoacylase which is encoded by the ASPA gene. Paper-11769426.
The 12.13kb deletion involves deletion of the ASPA gene from intron 3 to intron 5 including exons 4 and 5 (I3 to E4E5I5) in a compound heterozygous patient. Paper-12181655.
In vitro expression of mutant cDNA clones demonstrated that all of these mutations led to a deficiency of ASPA and should therefore result in Canavan disease. Paper-575250.
The catalytic site of aspartoacylase shows close structural similarity to those of carboxypeptidases despite only 10-13% sequence identity between these proteins. Paper-12401238.
The gene for aspartoacylase has been cloned and two mutations have been found to be responsible for Canavan disease among Ashkenazi Jewish patients in 98% of the cases. Paper-1988645.
N-acetylaspartic acid (NAA) is the biochemical hallmark of Canavan Disease, an inherited metabolic disease caused by deficiency of aspartoacylase activity. Paper-13770266.
Aspartoacylase deficiency is a neurodegenerative disease which typically starts in the first months of life with muscular hypotonia and developmental standstill. Paper-9723456.
Massive excretion in the urine of N-acetylaspartic acid is the biochemical marker for Canavan disease, which is caused by deficiency of the enzyme aspartoacylase. Paper-2200564.
Toxicity and expression testing was first carried out in human 293 cells, which demonstrated effective transduction of cells and high levels of functional ASPA activity. Paper-8404449.
It has been demonstrated that urinary N-acetylaspartate levels are increased because of a deficiency of aspartoacylase (N-acyl-L-aspartate aminohydrolase) in these patients. Paper-1789650.
The demonstration of the selective localization of ASPA in oligodendrocytes in the central nervous system (CNS) is consistent with the acetate deficiency hypothesis of CD. Paper-12049651.
The significance of aspartoacylase deficiency in Canavan disease for differential diagnosis, genetic counselling and prenatal diagnosis of leucodystrophy is discussed. Paper-7179077.
One is Canavan disease (CD), in which there is a buildup of NAA (hyperacetylaspartia) and associated spongiform leukodystrophy, caused by a lack of aspartoacylase activity. Paper-9721421.
After it was confirmed that AxASPA-infected HeLa cells expressed ASPA in vitro, AxASPA or AxLacZ was administered into the left lateral ventricle of 11-week-old SER. Paper-10212091.
Adeno-associated virus, serotype 2 (AAV2), mediated intraparenchymal delivery of the human aspartoacylase cDNA at a maximum dose of 1 x 10(12) vector genomes per subject. Paper-11829705.
The viscosities of the liquid components of these systems have been found to be Newtonian up to a shear rate of 140 s-1 with values of 0.80 N m-2 s for ASPA and 1.8 N m-2 for Fuji. Paper-3880356.
Frequency of a DNA polymorphism at position Y231 in the aspartoacylase gene and its impact on DNA-based carrier testing for Canavan disease in the Ashkenazi Jewish Population. Paper-1882502.
Canavan disease (CD) is an inherited leukodystrophy, caused by aspartoacylase ( ASPA) deficiency, and accumulation of N-acetylaspartic acid ( NAA) in the brain. Paper-10186690.
Canavan disease (CD) is an autosomal-recessive neurodegenerative disorder caused by inactivation of the enzyme aspartoacylase ( ASPA, EC 3.5.1.15) due to mutations. Paper-12049651.
Canavan disease, also known as Van Bogaert-Bertrand disease, is a monogeneic, autosomal recessive disease in which the gene coding for the enzyme aspartoacylase ( ASPA) is defective. Paper-9290996.
This study reports, for the first time, the carrier frequency of Canavan disease in the Ashkenazi Jewish population in Australia, and the identification of a novel mutation in the ASPA gene. Paper-10450768.
ASPA acts to hydrolyze N-acetylaspartate (NAA) into l-aspartate and acetate, but the connection between ASPA deficiency and the failure of proper CNS development is unclear. Paper-11205819.
More interestingly, the product of N-acetylasparagine was aspartate but not asparagine, indicating that ASPA catalyzed deacetylation as well as hydrolysis of the beta acid amide. Paper-8361580.
Therefore, the tremor rat may be regarded as a suitable animal model of human Canavan disease, characterized by spongy leukodystrophy that is caused by aspartoacylase deficiency. Paper-2206909.
Five other genes encode enzymes involved in the synthesis of myelin constituents ( ASPA, UGT8), or are essential in regulation of myelin formation ( ENPP2, EDG2, TF, KLK6). Paper-11141149.
Deficiency of the enzyme aspartoacylase and the accumulation of N-acetylaspartic acid lead to a severe leukodystrophy and spongy degeneration of the brain, Canavan disease (McKusick 271900). Paper-7554841.
This set of reactions starts when aspartoacylase converts the six carbons of NAA to aspartate and acetate, which are subsequently converted to oxaloacetate and acetyl CoA, respectively. Paper-12056346.
The gene for aspartoacylase has been cloned and two mutations predominate among Ashkenazi Jewish individuals with Canavan disease and account for more than 98% of the Ashkenazi Jewish patients. Paper-2200564.
These results show that aspartoacylase is a member of the caboxypeptidase A family and offer novel explanations for most loss-of-function aspartoacylase mutations associated with Canavan Disease. Paper-13198530.
Since aspartoacylase activity was present in cultured amniotic cells and chorionic villi, it is likely that the assay for this enzyme can be used for the prenatal diagnosis of Canavan disease. Paper-6101789.
The retentive capacity of the Whaledent Parapost system utilizing ASPA cement was compared at two lengths, three diameters, and with respect to the effect of both medication and citric acid pretreatment. Paper-3439338.
Our success in preparing the recombinant ASPA in high purity should permit multiple lines of investigations to understand the pathogenic mechanisms of Canavan disease and the functional roles of NAA. Paper-8361580.
Whereas two recent reports have indicated that ASPA exists as a dimer, size-exclusion chromatography of subcellular fractions showed ASPA is an active monomer in both subcellular fractions. Paper-12248186.
Our hypothesis is that ASPA actively participates in myelin synthesis by providing NAA-derived acetate for acetyl CoA synthesis, which in turn is used for synthesis of the lipid portion of myelin. Paper-12049651.
Aspartoacylase catalyzes the deacetylation of N-acetylaspartic acid ( NAA) to produce acetate and l-aspartate and is the only brain enzyme that has been shown to effectively metabolize NAA. Paper-11834248.
Finally, we performed the first in vivo gene transfer study for a human neurodegenerative disease in 2 children with Canavan disease to assess the in vivo toxicity and efficacy of ASPA gene delivery. Paper-8404449.
Patients with CD have aspartoacylase ( ASPA) deficiency, which results accumulation of N-acetylaspartic acid ( NAA) in the brain and elevated excretion of urinary NAA. Paper-12051582.
Mutations in ASPA that lead to loss of enzymatic activity have been identified, and E285A and Y231X are the two predominant mutations that account for 97% of the mutant chromosomes in Ashkenazi Jewish patients. Paper-575250.
It is an osmotic disease that affects both gray and white matter and is caused by the inability of oligodendrocytes to hydrolyze N-acetyl-L-aspartate (NAA) because of a lack of aspartoacylase activity. Paper-9569425.
A single case with amniotic fluid NAA in the normal range (1.56 mumol/L, measured in one laboratory only) resulted in an aborted fetus in whom aspartoacylase was deficient in cultured skin fibroblasts. Paper-7762424.
We have tested this hypothesis by determining acetate levels and studying myelin lipid synthesis in the ASPA gene knockout model of CD, and the results provided the first direct evidence in support of this hypothesis. Paper-12049651.
In support of human gene therapy for CD, recombinant adeno-associated viral vector (AAV-2) expressing ASPA was stereotactically delivered to the tremor rat brain and effects on the mutant phenotype were measured. Paper-11107475.
We found defective aspartoacylase activity in fibroblasts cultured from 12 patients with leukodystrophy clinically diagnosed as spongy degeneration of the brain ( Canavan disease), three confirmed by brain biopsy. Paper-6612200.
Alanine substitutions of Cys124 and Cys152, residues indicated by homology modeling to be in close proximity and in the proper orientation for disulfide bonding, yielded reduced ASPA protein and activity levels. Paper-13198530.
Mutations in the gene for aspartoacylase ( ASPA), which catalyzes deacetylation of N-acetyl-L-aspartate in the central nervous system (CNS), result in Canavan Disease, a fatal dysmyelinating disease. Paper-12248186.
However, finding the links between the lacks of ASPA activity in oligodendrocytes, the buildup of NAA in white matter (WM) and the mechanisms underlying the edematous spongiform leukodystrophy have remained elusive. Paper-13895884.
The cause of the altered NAA metabolism has been traced to several mutations in the gene for the production of aspartoacylase, located on chromosome 17, which is the primary enzyme involved in the catabolic metabolism of NAA. Paper-8558535.
On the other hand, macrophages in peripheral blood, Kupffer cells in the liver and certain cells of the thymus-medulla were stained with ASPA, but not with ATOS, even after intensively absorbing ASPS with thymocytes. Paper-2895244.
Canavan disease (CD) has only been diagnosed on autopsy or brain biopsy, however, specific biochemical markers, such as N-acetylaspartic acid ( NAA) and aspartoacylase activity, have recently been described in CD. Paper-7751869.
Acetate incorporation into lipids increased 15 to 30%, and palmitate or oleate incorporation increased 10 to 25%, when explants were exposed to hASP, although this response was not significant in every experiment. Paper-9400205.
Amniocentesis was at 14-18 weeks gestation followed by measurement of amniotic fluid N-acetyl-L-aspartate (NAA) levels in all pregnancies and amniocyte aspartoacylase activity in most pregnancies. Paper-7762424.
Canavan disease is a childhood leukodystrophy caused by mutations in the gene for human aspartoacylase ( ASPA), which leads to an abnormal accumulation of the substrate molecule N-acetyl-aspartate (NAA) in the brain. Paper-12360665.
[1988] in a totally different ethnic group and provides independent verification that aspartoacylase activity is the first documented specific biochemical marker in Canavan disease and plays an important role in pathogenesis. Paper-6612200.
OBJECTIVE: Prenatal diagnosis of Canavan disease by measuring N-acetylaspartic acid (NAA) in amniotic fluid is reliable and preferred over aspartoacylase enzyme assay especially in populations with unknown mutations. Paper-13737984.
Mutations that result in near undetectable activity of aspartoacylase, which catalyzes the deacetylation of N-acetyl-l-aspartate, correlate with Canavan Disease, a neurodegenerative disorder usually fatal during childhood. Paper-13198530.
The results of transient expression of the mutant ASPA cDNA containing these mutations in COS-7 cells and assays for ASPA activity of patient fibroblasts indicated that these mutations were responsible for the enzyme deficiency. Paper-9625006.
Sequence alignments show that, in particular, the regions previously suggested to form the catalytic core of human ASPA are evolutionarily conserved and nearly identical to that found in the Prochlorococcus putative ASPA. Paper-1135075.
This study provides evidence that AAV-2-mediated aspartoacylase gene transfer to the brain improves biochemical and behavioral deficits in tremor rat mutants (tm/tm) and supports the rationale of human gene transfer for Canavan disease. Paper-11107475.
Here, we describe the pathophysiological parameters of Canavan disease (CD), caused by genetic mutations of the aspartoacylase ( ASPA) gene, a metabolic enzyme restricted in the central nervous system (CNS) to oligodendrocytes. Paper-12137444.
Accordingly, no aspartoacylase expression was detected in any of the tissues examined, and abnormal accumulation of N-acetyl-L-aspartate (NAA) was shown in the mutant brain, in correlation with the severity of the vacuole formation. Paper-2206909.
During early postnatal central nervous system (CNS) development, the expression of lipogenic enzymes in oligodendrocytes, including the NAA-degrading enzyme aspartoacylase ( ASPA), is increased along with increased NAA production in neurons. Paper-13125373.
A biochemical defect associated with this disease results in reduced activity of the enzyme N-acetyl-L-aspartate amidohydrolase ( aspartoacylase) and affected individuals have less ability to hydrolyze N-acetyl-L-asparate (NAA) in brain and other tissues. Paper-1271695.
The absence of ASPA expression in these animals results in undetectable levels of enzyme activity and the accumulation of the substrate N-acetyl-aspartate (NAA) in brain, leading to generalized myelin vacuolation and severe motor and cognitive impairment. Paper-11107475.
We present here a patient with a mild form of Canavan disease confirmed with the absent ASPA activity, atypical MRI findings, related to compound heterozygosity for a missense mutation, p.Tyr288Cys, and the known pan-European mutation, the p.Ala305Glu. Paper-11488906.
This hypothesis ascribes for the first time a possible key role played by astrocytes in CD, linking the lack of ASPA activity in myelinating oligodendrocytes, the pathological buildup of NAA in WM ECF, and the spongiform demyelination process. Paper-13895884.
Acetate incorporation (P < 0.32) was 0.99, 1.03, 1.04, and 1.10 nmol x mg(-1) h(-1) (SE = 0.13) and oleate incorporation (P < 0.01) was 0.347, 0.357, 0.353, and 0.420 nmol x mg(-1)h(-1) (SE = 0.022) for 0, 0.01, 0.1, and 1 microM hASP, respectively. Paper-9400205.
The octapeptide angiotensin II mediates the physiological actions of the renin-angiotensin system through activation of several angiotensin II receptor (AT) subtypes, in particular AT1 ( AT1a and AT1b in the case of rodents). Paper-8315149.
Because ASPA is small enough to passively diffuse into the nucleus, we constructed, expressed, and detected in COS-7 cells a green fluorescent protein-human ASPA (GFP- hASPA) fusion protein larger than the permissible size for the nuclear pore complex. Paper-12248186.
Surface cleaning and conditioning with 5% sodium hypochlorite solution showed an improvement in the bonds of the cements to dentine and they were significantly stronger than the bonds formed after the use of 50% citric acid solution ( ASPA conditioner.) Paper-4233238.
Fresh s.c. adipose tissue was sectioned into 20- to 30-mg explants and incubated for 1 to 6 h in M199 media containing 3% BSA and either 0.75 mM [1-14C]palmitate, 0.75 mM [9, 10-3H]oleate, or 2.5 mM [1-14C] acetate, as well as hASP and(or) insulin. Paper-9400205.
The objectives of this research were 1) to determine the effect of hASP on triacylglycerol synthesis in bovine adipose explants and 2) to determine whether nutritional status influences the sensitivity of adipose tissue to hASP. Paper-9400205.
An open reading frame encoding a polypeptide with significant homology (about 28% identity and 16% similarity) to human aspartoacylase ( ASPA) was identified in the genome of Prochlorococcus marinus CCMP 1375, an oxyphototrophic bacterium. Paper-1135075.
Aspartoacylase, the enzyme whose activity is deficient in infantile central nervous system spongy degeneration ( Canavan-Van Bogaert-Bertrand disease), is detected as an approximately 59-kD protein in the Sephadex G-200 filtration of normal fibroblast extracts. Paper-7392510.
Before the establishment of N-acetylaspartic aciduria due to aspartoacylase deficiency as the cause of Canavan disease, diagnosis was based on the characteristic clinical features and spongiform encephalopathy, a pathological response shared by a number of other unrelated conditions. Paper-7725432.
This review summarizes recent knowledge on pathomechanisms involved in phenylketonuria, glutaric aciduria type I, succinic semialdehyde dehydrogenase deficiency and aspartoacylase deficiency with examples, highlighting general as well as disease-specific concepts and their putative impact on treatment. Paper-13073566.
Finally, expression of several previously tested (E24G, D68A, C152W, E214X, D249V, E285A, and A305E) and untested (H21P, A57T, I143T, P183H, M195R, K213E/G274R, G274R, and F295S) Canavan Disease mutations resulted in undetectable enzyme activity, and only E285A and P183H showed wild-type aspartoacylase protein levels. Paper-13198530.
This procedure involves neurosurgical administration of approximately 900 billion genomic particles (approximately 10 billion infectious particles) of recombinant adeno-associated virus (AAV) containing the aspartoacylase gene ( ASPA) directly to affected regions of the brain in each of 21 patients with Canavan disease. Paper-9290996.
We evaluated the functional effects of rAAV-hASPA-GFP-mediated ASPA expression by standard histological methods, magnetic resonance spectroscopy (MRS) for in vivo NAA levels, and magnetic resonance imaging of CD mice. rAAV- hASPA-injected animals displayed a remarkable lack of spongiform degeneration in the thalamus. Paper-10021075.
The enzyme was found to have maximal activity at pH 8.5, and the Michaelis constant for the substrate N-acetylaspartate was 1.8-2.0 mmol/l. Aspartoacylase activity in control cultured human fibroblasts was 9.2 +/- 1.8 nmol/h per mg protein, compared with 1.1 +/- 0.2 in seven Canavan patients and 3.5 +/- 0.9 in four patients' parents. Paper-6854856.
These synonyms are used for gene ASPA (aspartoacylase (Canavan disease)): Aspartoacylase, ASP, Aminoacylase-2, ACY-2, ACY2.
These accession numbers are used for gene ASPA: Q6FH48 (UNIPROT__AC), AAH29128 (NCBI_GENBANK__AC), AAB29190 (NCBI_GENBANK__AC).
ASPA is a homologue of zgc:171507 (zgc:171507) from Danio rerio.
ASPA is a homologue of ASPA (aspartoacylase (Canavan disease)) from Bos taurus.
ASPA is a homologue of ASPA (aspartoacylase (Canavan disease)) from Pan troglodytes.
ASPA is a homologue of ASPA (aspartoacylase (Canavan disease)) from Gallus gallus.
ASPA is a homologue of ASPA (aspartoacylase (Canavan disease)) from Canis lupus familiaris.
ASPA is a homologue of Aspa (aspartoacylase) from Mus musculus.
ASPA is a homologue of Aspa (aspartoacylase) from Rattus norvegicus.
Important links !
iHOP - Information Hyperlinked over Proteins .
Concept & Implementation by Robert Hoffmann.