Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

[Mucolipidosis. biologic characteristics (author's transl)].

R Gatti, C Borrone, J Torreblanca

    Anales Espanoles De Pediatria
    |August 1, 1979
    PubMed
    Summary

    Mucolipidosis II and III are inherited lysosomal storage diseases with similar enzyme deficiencies. Both conditions show elevated hydrolases in culture medium but not in body fluids, indicating a shared underlying defect in enzyme targeting.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Impact of Vessel Suppressed-CT on Diagnostic Accuracy in Detection of Pulmonary Metastasis and Reading Time.

    Academic radiology·2020
    Same author

    Carbon nanotubes as nanovectors for intracellular delivery of laronidase in Mucopolysaccharidosis type I.

    Nanoscale·2017
    Same author

    Mutation identification of Fabry disease in families with other lysosomal storage disorders.

    Clinical genetics·2012
    Same author

    Krabbe leukodystrophy in a selected population with high rate of late onset forms: longer survival linked to c.121G>A (p.Gly41Ser) mutation.

    Clinical genetics·2010
    Same author

    Origin and spread of a common deletion causing mucolipidosis type II: insights from patterns of haplotypic diversity.

    Clinical genetics·2010
    Same author

    Enhancing cranial nerves and cauda equina: an emerging magnetic resonance imaging pattern in metachromatic leukodystrophy and krabbe disease.

    Neuropediatrics·2010

    Area of Science:

    • Biochemistry
    • Genetics
    • Cell Biology

    Background:

    • Mucolipidosis II (ML II) and Mucolipidosis III (ML III) are rare inherited lysosomal storage diseases.
    • ML II presents with severe psychomotor retardation and skeletal abnormalities, while ML III has a milder course with less severe intellectual disability.
    • Both disorders are characterized by deficient activity of multiple acid hydrolases within cells.

    Purpose of the Study:

    • To investigate the biochemical similarities and differences between Mucolipidosis II and Mucolipidosis III.
    • To explore the enzyme profiles in various biological samples and cultured cells from patients with ML II and ML III.
    • To elucidate the underlying molecular mechanisms contributing to these related lysosomal storage disorders.

    Main Methods:

    Related Experiment Videos

  • Analysis of lysosomal enzyme activities in serum, leukocytes, fibroblast extracts, and culture media.
  • Phase microscopy of cultivated fibroblasts to observe cellular inclusions.
  • Biochemical assays to quantify sialyl-oligosaccharide excretion and sialic acid levels.

    • Main Results:

    • Lysosomal enzyme activities in serum, leukocytes, and fibroblast extracts were similar in both ML II and ML III patients.
    • Cultured fibroblasts from both groups displayed large inclusions and reduced intracellular hydrolase levels.
    • Elevated levels of hydrolases were observed in the culture medium of fibroblasts from affected patients, contrasting with normal levels in body fluids.
    • Excessive excretion of sialyl-oligosaccharides in urine and increased sialic acid compounds in fibroblasts were noted, alongside sialidase deficiency.

    Conclusions:

    • Mucolipidosis II and Mucolipidosis III share significant biochemical similarities, suggesting a common pathogenic pathway.
    • The observed enzyme profile points to a defect in the intracellular targeting or processing of lysosomal enzymes.
    • Further research into sialidase deficiency and sialic acid metabolism may provide insights into the pathogenesis of these related mucolipidoses.