PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 11119053

[Lysosome enzyme pseudodeficiency].

P Bronner·G Rodier·E Cohen·F Derouiche·C Boulay·S Courtois
View original source ↗Export metadata ↓

Abstract

Inherited deficiency of lysosomal hydrolase often displays different clinical features. However, a greatly reduced enzyme activity may be observed in healthy individuals. This pseudo-deficiency concerns at least nine lysosomal hydrolases. When a deficiency has been proved, the presence of mutations known to cause pseudodeficiencies must be searched, above all in Tay-Sachs disease and metachromatic leukodystrophy.

Explore related subjects

Cerebroside-SulfataseDiagnosis, DifferentialGene ExpressionHumansLysosomal Storage DiseasesPoint Mutationbeta-N-AcetylhexosaminidasesEnglish AbstractJournal ArticleReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

P Bronner, G Rodier, E Cohen, F Derouiche, C Boulay, S Courtois. 2000. [Lysosome enzyme pseudodeficiency].. https://pubmed.ncbi.nlm.nih.gov/11119053/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2006

Tyrosine sulfation of arylsulfatase A and its peptide.

Purified human liver arylsulfatase A (ASA) as well as an ASA peptide (residues 28-39) were sulfated by tyrosyl protein sulfotransferase in vitro. The media, but not the cell lysate, of normal human fibroblasts contained a tyrosine sulfated protein (pI = 4.5-5.5). This protein was not present in either media or cell lysate of human fibroblasts lacking ASA protein. These results suggest that tyrosine sulfation facilitates secretion of ASA and that this may have pathophysiological consequences.

Cerebroside-Sulfatase↗
PubMed2005

Prenatal mucolipidosis type II (I-cell disease) can present as Pacman dysplasia.

Pacman dysplasia has been previously reported to be a lethal skeletal dysplasia with epiphyseal stippling and osteoclastic overactivity. We report on a sibling of a fetus previously reported as Pacman dysplasia. This infant has a clinical course consistent with mucolipidosis type II (I-cell disease) along with confirmatory biochemical, cytologic, and radiographic evidence. This case expands the phenotypic spectrum of mucolipidosis type II. Having redefined the diagnosis in one of the original cases of Pacman dysplasia, we suggest that what is called Pacman dysplasia could very well be Mucolipidosis type II (ML-II) in other published reports.

Cerebroside-Sulfatase↗
PubMed2005

Homozygote for mutation c.1204 + 1G > A of the ARSA gene presents with a late-infantile form of metachromatic leukodystrophy and a rare MRI white matter lesion type.

The metachromatic leukodystrophy (MLD)--causing mutation c.1204 + 1G > A damages an intron-exon splice site recognition sequence. This results in a complete loss of enzymatic activity of arylsulfatase A (ARSA) protein molecules. We have found a late-infantile type MLD-patient to be homozygous for this mutation, which was not reported earlier, but is consistent with previous suggestions. Interestingly, the cerebral magnetic resonance imaging (MRI) in this patient displayed linear or punctuate structures radiating in the demyelinated white matter, which resembled the patterns described in Pelizaeus-Merzbacher disease. It should be emphasised that whenever a cerebral MRI demonstrates the "tigroid" or "leopard-skin" demyelination pattern not only Pelizaeus-Merzbacher disease, but also metachromatic leukodystrophy diagnosis should be considered; this suggests the necessity of ARSA activity estimations in patients with such specific MRI patterns.

Cerebroside-Sulfatase↗