Literature DB >> 8830180

Single base deletion in exon 7 of the glycosylasparaginase gene causes a mild form of aspartylglycosaminuria in a patient of Mauritian origin.

H Park1, M Rossiter, A H Fensom, B Winchester, N N Aronson.   

Abstract

Aspartylglycosaminuria (AGU) is a lysosomal storage disorder of glycoprotein degradation caused by deficiency of glycosylasparaginase (GA). A deletion mutation was found in a mildly affected AGU patient whose parents are first-cousins of Mauritian origin. One bp deletion at position 787 or 788 (delta T788) in exon 7 of the GA gene resulted in a frameshift and produced an immediate stop codon. The resulting truncated polypeptide was defective in its post-translational proteolytic processing and remained as a single chain (36 kDa) with no GA activity.

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Year:  1996        PMID: 8830180     DOI: 10.1007/bf01799351

Source DB:  PubMed          Journal:  J Inherit Metab Dis        ISSN: 0141-8955            Impact factor:   4.982


  27 in total

1.  Gene deletions causing human genetic disease: mechanisms of mutagenesis and the role of the local DNA sequence environment.

Authors:  M Krawczak; D N Cooper
Journal:  Hum Genet       Date:  1991-03       Impact factor: 4.132

Review 2.  Aspartylglycosaminuria. Analysis of thirty-four patients.

Authors:  S Autio
Journal:  J Ment Defic Res       Date:  1972

3.  Comparison of liver glycosylasparaginases from six vertebrates.

Authors:  O K Tollersrud; N N Aronson
Journal:  Biochem J       Date:  1992-03-15       Impact factor: 3.857

4.  Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.

Authors:  I Mononen; N Heisterkamp; V Kaartinen; J C Williams; J R Yates; P R Griffin; L E Hood; J Groffen
Journal:  Proc Natl Acad Sci U S A       Date:  1991-04-01       Impact factor: 11.205

5.  Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits.

Authors:  K J Fisher; N N Aronson
Journal:  J Biol Chem       Date:  1991-06-25       Impact factor: 5.157

6.  Improved vectors for stable expression of foreign genes in mammalian cells by use of the untranslated leader sequence from EMC virus.

Authors:  R J Kaufman; M V Davies; L C Wasley; D Michnick
Journal:  Nucleic Acids Res       Date:  1991-08-25       Impact factor: 16.971

7.  Deletion of exon 8 causes glycosylasparaginase deficiency in an African American aspartylglucosaminuria (AGU) patient.

Authors:  K J Fisher; N N Aronson
Journal:  FEBS Lett       Date:  1991-08-19       Impact factor: 4.124

8.  Deletion of the C-terminal end of aspartylglucosaminidase resulting in a lysosomal accumulation disease: evidence for a unique genomic rearrangement.

Authors:  A Jalanko; T Manninen; L Peltonen
Journal:  Hum Mol Genet       Date:  1995-03       Impact factor: 6.150

9.  Post-translational processing and Thr-206 are required for glycosylasparaginase activity.

Authors:  K J Fisher; M Klein; H Park; M B Vettese; N N Aronson
Journal:  FEBS Lett       Date:  1993-06-01       Impact factor: 4.124

10.  Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum.

Authors:  E Ikonen; I Julkunen; O K Tollersrud; N Kalkkinen; L Peltonen
Journal:  EMBO J       Date:  1993-01       Impact factor: 11.598

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  3 in total

1.  Sleep disturbances in aspartylglucosaminuria (AGU): a questionnaire study.

Authors:  Niki Lindblom; Satu Kivinen; Hannu Heiskala; Maija-Liisa Laakso; Markus Kaski
Journal:  J Inherit Metab Dis       Date:  2006-08-30       Impact factor: 4.982

2.  Overgrowth of oral mucosa and facial skin, a novel feature of aspartylglucosaminuria.

Authors:  P Arvio; M Arvio; M Kero; S Pirinen; P L Lukinmaa
Journal:  J Med Genet       Date:  1999-05       Impact factor: 6.318

3.  Structural constraints on autoprocessing of the human nucleoporin Nup98.

Authors:  Yixin Sun; Hwai-Chen Guo
Journal:  Protein Sci       Date:  2008-03       Impact factor: 6.725

  3 in total

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