Monitoring the CNS pathology in aspartylglucosaminuria mice

Journal of Neuropathology and Experimental Neurology

Volumn 57, Issue 12, 1998, Pages 1154-1163

  Tenhunen, Kai ^a   Uusitalo, Annukka ^a   Autti, Taina ^b   Joensuu, Raimo ^b   Kettunen, Mikko ^c   Kauppinen, Risto A ^c   Ikonen, Sami ^c   LaMarca, Mary E ^d   Haltia, Matti ^b   Ginns, Edward I ^d   Jalanko, Anu ^a   Peltonen, Leena ^a  

^a NATIONAL PUBLIC HEALTH INSTITUTE   (Finland)

^b UNIVERSITY OF HELSINKI   (Finland)

^c UNIVERSITY OF EASTERN FINLAND   (Finland)

^d NATIONAL INSTITUTE OF MENTAL HEALTH   (United States)

Author keywords

Aspartylglucosaminuria; Knock out mouse; Lysosomal storage disease

Indexed keywords

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; ASPARTYLGLYCOSAMINURIA; BRAIN DISEASE; CENTRAL NERVOUS SYSTEM DISEASE; CONTROLLED STUDY; ELECTRON MICROSCOPY; GENE MUTATION; HETEROZYGOSITY; HOMOZYGOSITY; HUMAN; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; MOUSE; NEUROPATHOLOGY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE IMAGING; PRIORITY JOURNAL; QUANTITATIVE DIAGNOSIS;

EID: 0031797006     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1097/00005072-199812000-00007     Document Type: Article

References (29)

1. Pollit RJ, Jenner FA, Merskey H. Aspartylglucosaminuria: An inborn error of metabolism associated with mental defect. Lancet 1968;2:253-55
2. Palo J, Mattsson K. Eleven new cases of aspartylglucosaminuria. J Ment Defic Res 1970;14(2):168-73
3. Haltia M, Palo J, Autio S. Aspartylglucosaminuria: A generalized storage disease. Acta Neuropath 1975;31:243-55
4. Makino M, Kojima T, Ohgushi T, et al. Studies on enzymes acting on glycopeptides. J Biochem 1968;63:186-92
5. Ikonen E, Julkunen I, Tollersrud O-K, et al. Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease. EMBO J 1991;10:51-58
6. Riikonen A, Tikkanen R, Jalanko A, et al. Immediate interaction between the nascent subunits and two conserved amino acids Trp 34 and Thr 206 are needed for the catalytic activity of aspartylglucosaminidase. J Biol Chem 1995;270:4903-7
7. Tikkanen R, Enomaa N, Riikonen A, et al. Intracellular sorting of aspartylglucosaminidase: The role of N-linked oligosaccharides and evidence of Man-6-independent lysosomal targeting. DNA Cell Biol 1995;14:305-12
8. Oinonen C, Tikkanen R, Rouvinen J, et al. Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nat Struct Biol 1995;2:1102-8
9. Riikonen A, Rouvinen J, Tikkanen R, et al. Primary folding of aspartylglucosaminidase: Significance of disulfide bridges and evidence of early multimerization. J Biol Chem 1996;271:21340-44
10. Tikkanen R, Riikonen A, Oinonen C, et al. Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: Implications for catalytic mechamism and autocatalytic activation. EMBO J 1996;12:2954-60
11. Tikkanen R, Peltola M, Oinonen C, et al. Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase. EMBO J 1997;16:22:6684-93
12. Arvio M. Life with aspartylglucosaminuria. Monograph, Lammi-Paino 1993
13. Aula P, Autio S, Raivio K, et al. Aspartylglucosaminuria in genetic errors of glycoprotein metabolism. Springer-Verlag, Berlin 1982; 123-52
14. Autti T, Raininko R, Haltia M, et al. Aspartylglucosaminuria: Radiologic course of the disease with histopathologic correlation. J Child Neurol 1997;12:369-75
15. Autti T, Santavuori P, Raininko R, et al. Bone-marrow transplantation in aspartylglucosaminuria. Lancet 1997;349:1366-67
16. Jalanko A, Tenhunen K, McKinney CE, et al. Mice with aspartylglucosaminuria mutation similar to humans replicate the pathophysiology in patients. Hum Mol Genet 1998;7:265-72
17. Kaartinen V, Mononen I, Voncken J-V, et al. A mouse model for the human lysosomal disease aspartylglucosaminuria. Nat Med 1996;2:1375-78
18. Fisher KJ, Aronson NN, Jr. Deletion of exon 8 causes glycosylasparaginase deficiency in an African American aspartylglucosaminuria (AGU) patient. FEBS Lett 1991;288:173-78
19. Jalanko A, Manninen T, Peltonen L. Deletion of the C-terminal end of aspartylglucosaminidase resulting in a lysosomal accumulation disease: Evidence for a unique genomic rearrangement. Hum Mol Genet 1995;4:435-41
20. Laemmli UK. Clevage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1979;227:680-85
21. Sambrook J, Fritch EF, Maniatis T. Molecular cloning: a laboratory manual. Cold Spring Harbor, NY: Cold Spring Harbor Press, 1989
22. Halila R, Baumann M, Ikonen E, et al. Human leucocyte aspartylglucosaminidase. Evidence for two different subunits in a more complex native structure. Biochem J 1991;271:251-56
23. Lister RG. The use of a plus maze to measure anxiety in the mouse. Psychopharmacology 1987;92:180-85
24. Kelley A E. Locomotor activity and exploration. In: Sahgal A, ed. Behavioural Neuroscience. A practical approach. Oxford, UK: Oxford University Press, 1993:1-21
25. Evers M, Saftig P, Schmidt P. et al. Targeted disruption of the arylsulfatase B gene results in mice resembling the phenotype of mucopolysaccharidosis VI Proc Nat Acad. Sci. USA 1996;93: 8214-19
26. Hess B, Saftig P, Hartmann D, et al. Phenotype of arylsulfatase A-deficient mice: Relationship to human metachromatic leukodystrophy. Proc Natl Acad Sci USA 1996;93:14821-26
27. Clarke L, Russell C, Pownall S. et al. Murine mucopolysaccharidosis type I: Targeted disruption of the murine α - iduronidase gene. Hum Mol Genet 1997;6:4:503-11
28. Riikonen A, Ikonen E, Sormunen R, et al. Dissection of the molecular consequences of a double mutation causing a human lysosomal disease. DNA Cell Biol 1994;13:3:257-64
29. Enomaa N, Lukinmaa P, Ikonen E, et al. Expression of aspartylgucosaminidase in human tissues from normal individuals and aspartylglucosaminuria patients. J Histoch Cytoch 1993;41:981-89