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A variant of mucolipidosis

II. Clinical, biochemical and pathological investigations

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Abstract

We present in this paper a patient with a clinically intermediate form of mucolipidosis (ML). Lysosomal hydrolase activity in fibroblasts was normal and levels of these enzymes in culture media were not elevated. There was a striking elevation of several hydrolases in serum and a deficiency (15% of normal) of N-acetyl-glucosamine phosphotransferase in fibroblasts. Atypical electron microscopic findings were also observed.

There was no evidence of increased synthesis, slower turnover, unbalanced distribution or further changes in lysosomal enzymes. Phosphotransferase deficiency against endogenous β-glucosaminidase and the fact that the electrophoretic mobility of lysosomal enzymes was identical to that of ML II suggest that these enzymes are not phosphorylated. Hypotheses that could explain this atypical pathology are discussed.

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Abbreviations

ML II:

mucolipidosis type II

ML III:

mucolipidosis type III

4 MU:

4-methylum belliferone

Con A:

concanavaline A

Hex A:

hexosaminidase A

HA:

our patient's initials

PT:

N-acetylglucosamine-1-phosphotransferase

Hex:

N-acetyl-β-glucosaminidase

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Authors and Affiliations

  1. Inserm U.129, 24 Rue du Faubourg Saint-Jacques, F-75674, Paris Cedex 14, France

    L. Poenaru & L. Castelnau

  2. Inserum U. 153, 17 Rue du Fer à Moulin, F-75005, Paris, France

    F. Tome

  3. Inserum U. 73, Château de Longchamp, Bois de Boulogne, F-75016, Paris, France

    J. Boue

  4. Inserum U. 12 et CNRS UA. 584, 149 Rue de Sèvres, F-75743, Paris Cedex 15, France

    P. Maroteaux

Authors
  1. L. Poenaru
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  2. L. Castelnau
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  3. F. Tome
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  4. J. Boue
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  5. P. Maroteaux
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Poenaru, L., Castelnau, L., Tome, F. et al. A variant of mucolipidosis. Eur J Pediatr 147, 321–327 (1988). https://doi.org/10.1007/BF00442708

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  • DOI: https://doi.org/10.1007/BF00442708

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