Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0025362 (mental retardation)
 15,878 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Aspartylglycosaminuria is an autosomal recessive disorder of glycoprotein catabolism, characterized by presence of aspartyglycosamine in the urine, progressive mental retardation, coarse face, impaired speech and motor functions, and signs of involvement of connective tissue and skeleton. In infancy, clinical symptoms are mild or absent. Vacuolized lymphocytes are often found in the blood and bone marrow. The disease appears unusually common in Finland.
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PMID:Aspartylglycosaminuria: a gargoyle-like syndrome with autosomal recessive inheritance. 422 85

Aspartylglycosaminuria (AGU, McKusick 20840) is a metabolic disorder affecting the catabolism of glycoproteins. It was first described in 1967, by Jenner and Pollitt, in two mentally retarded English siblings. Subsequently several cases were reported from Finland (Palo and Mattsson, 1970; Autio, 1972; Autio et al., 1973). Today the number of known cases is about 140, most of them Finnish or of Finnish origin (Aula et al., 1980). The incidence of AGU in Finland has been estimated to be approximately 1:26000 and the disease is inherited as an autosomal recessive trait (Autio et al., 1973). Clinical manifestations include progressive mental retardation, coarse gargoyle-like facial features, skeletal abnormalities and recurrent infections. Early development of the patients is usually normal, but by the age of 5-15 years they are already severely retarded (Autio, 1972; Autio et al., 1973). Morphologically AGU is a generalized storage disease (Haltia et al., 1975). Affected tissues show enlarged lysosomes. Vacuolization is a prominent feature of liver and nerve cells (Haltia et al., 1975) and of peripheral lymphocytes (Aula et al., 1975).
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PMID:Aspartylglycosaminuria: an inborn error of glycoprotein catabolism. 682 Apr 40

Aspartylglycosaminuria (AGU) is a lysosomal storage disease caused by deficient activity of glycosylasparaginase (AGA), and characterized by motor and mental retardation. Enzyme replacement therapy (ERT) in adult AGU mice with AGA removes the accumulating substance aspartylglucosamine from and reverses pathology in many somatic tissues, but has only limited efficacy in the brain tissue of the animals. In the current work, ERT of AGU mice was initiated at the age of 1 week with three different dosage schedules of recombinant glycosylasparaginase. The animals received either 3.4 U of AGA/kg every second day for 2 weeks (Group 1), 1.7 U/kg every second day for 9 days followed by an enzyme injection once a week for 4 weeks (Group 2) or 17 U/kg at the age of 7 and 9 days (Group 3). In the Group 1 and Group 3 mice, ERT reduced the amount of aspartylglucosamine by 34 and 41% in the brain tissue, respectively. No therapeutic effect was observed in the brain tissue of Group 2 mice. As in the case of adult AGU mice, the AGA therapy was much more effective in the somatic tissues than in the brain tissue of the newborn AGU mice. The combined evidence demonstrates that a high dose ERT with AGA in newborn AGU mice is up to twofold more effective in reducing the amount of the accumulated storage material from the brain tissue than ERT in adult AGU animals, indicating the importance of early detection and treatment of the disease.
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PMID:Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice. 2060 10