aspartylglycosaminuria


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as·par·tyl·gly·cos·a·mi·nu·ri·a

(as-par'til-glī-kō'să-min-yū'rē-ă), [MIM*208400]
A lysosomal disorder caused by deficiency of aspartoglucosaminidase, resulting in accumulation of aspartylglycosamine in the urine and spinal fluid; characterized by symptoms usually in the first few months of life, with recurrent infections and diarrhea; mental retardation, seizures, coarse facial features, and skeletal abnormalities become evident by adolescence. Autosomal recessive inheritance, caused by mutation in the aspartoglucosaminidase gene (AGA) on 4q.

aspartylglycosaminuria

A disease due to deficiency of the enzyme aspartylglycosaminidase which splits acetylglucosamine from the polypeptide chain of glycoproteins. Aspartylglucosamine is excreted in large quantities in the urine. Affected children are short, with coarse features, cataracts, over-mobile joints and mental retardation. Most of the reported cases have been in Finland.

as·par·tyl·gly·cos·a·mi·nu·ri·a

(as-par'til-glī-kō'să-min-yū'rē-ă) [MIM*208400]
A lysosomal disorder caused by deficiency of aspartoglucosaminidase; involves recurrent infections and diarrhea; mental retardation, seizures, coarse facial features, and skeletal abnormalities that become evident by adolescence.
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References in periodicals archive ?
High prevalence of aspartylglycosaminuria among school-age children in eastern Finland.
This is higher than the carrier frequency of the major mutations that cause aspartylglycosaminuria or infantile neuronal ceroid lipofuscinosis in the Finnish population (1:94-1:83 and 1:95, respectively) (13-15).
Fin]) (25), which is responsible for Finnish-type aspartylglycosaminuria (AGU; McKusick 208400).
Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.
Deficient enzyme activity leads to the lysosomal storage disease aspartylglycosaminuria (McKusick 208400).
Considerable residual GA activity in I-cell disease fibroblasts compared with that in GA-deficient aspartylglycosaminuria fibroblasts (12) indicates that the autoproteolytic cleavage of the precursor polypeptide of the enzyme into subunits and association of at least one of each subunit to form the active enzyme in humans (4,15) takes place inside the cells before leakage into extracellular fluids.
These findings also suggest that newborn babies affected by I-cell disease could be detected on the basis of high GA values in neonatal screening of aspartylglycosaminuria (16).
Recombinant glycosylasparaginase and in vitro correction of aspartylglycosaminuria.
A fluorometric assay for glycosylasparaginase activity and detection of aspartylglycosaminuria.
A PCR-OLA method was also used for the detection of the major mutation causing aspartylglycosaminuria (AGU; McKusick 20840) in a pilot population-screening study in eastern Finland (6, 7).