A radiochemical assay for N-acetyl-L-aspartate amidohydrolase (EC 3.5.1.15) and its occurrence in the tissues of the chicken

D’Adamo, Amedeo F.; Wertman, Elon; Foster, Faye; Schneider, Howard A.

doi:10.1016/0024-3205(78)90513-1

Cited by 4 publications

(4 citation statements)

References 11 publications

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“…5 A ) from kidney and brain of WT and ASPA –/– mutant Tremor rats (28). As described previously, there was ~10‐fold higher activity in kidney than in brain (6, 17, 30). This activity was due to the ASPA gene as it was not present in Tremor rat tissue extracts.…”

Section: Resultssupporting

confidence: 73%

“…Subsequently, antibodies against recombinant human ASPA (8) and recombinant murine ASPA (16) demonstrated ASPA expression primarily in oligodendrocytes in rat brain by immunohistochemistry. These and earlier studies showing ASPA activity restricted to the cytoplasm (6,7) and in membrane fractions (11,17,18) have implied a specific subcellular localization for ASPA, but this remains to be established definitively. Immunohistochemistry of rat brain sections identified oligodendrocytes expressing ASPA protein and provided initial indications that ASPA is present in the nucleus as well (16).…”

mentioning

confidence: 58%

“…For many years ASPA has been assumed to be a soluble, cytoplasmic enzyme with some partial membrane association (6, 11, 17, 18). However, our recent immunohistochemical localization study raised the possibility that ASPA may also be found in the nucleus of oligodendrocytes (16).…”

Section: Discussionmentioning

confidence: 99%

“…Overall acetate levels and lipid synthesis have recently been shown to be deficient in brains of CD knockout mice (14), providing strong support for the hypothesis that NAA in the CNS supplies acetyl groups for lipid synthesis during myelination (3, 7, 14). The functions served by ASPA in other tissues such as kidney (17) are currently unknown.…”

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confidence: 99%

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Aspartoacylase is a regulated nuclear‐cytoplasmic enzyme

et al. 2006

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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. Consistent with its role in supplying acetate for myelin lipid synthesis, ASPA is thought to be cytoplasmic. Here we describe the occurrence of ASPA within nuclei of rat brain and kidney, and in cultured rodent oligodendrocytes. Immunohistochemistry showed cytoplasmic and nuclear ASPA staining, the specificity of which was demonstrated by its absence from tissues of the Tremor rat, an ASPA-null mutant. Subcellular fractionation analysis revealed low enzyme activity against NAA in nuclear fractions from normal rats. 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. Western blotting detected ASPA as a single 38 kD band. 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. GFP-hASPA was enzymatically active and showed mixed nuclear-cytoplasmic distribution. We conclude that ASPA is a regulated nuclear-cytoplasmic protein that may have distinct functional roles in the two cellular compartments.

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