Title: Lysosomal neuraminidase in human genetic diseases
Abstract: textabstractSince the discovery of the lysosome as a distinct subcellular
compartment important for intracellular digestion, by
the group of De Duve in 1955, more than 70 lysosomal hydrolases
have been described. A genetically determined deficiency
of one of these enzymes may result in the intralysosomal
accumulation of cellular constituents or extracellular
products. Depending on the function of the enzyme, the rate of
accumulation and the interference with the cellular metabolism,
a variety of clinical and pathological manifestations
will occur. Up to now more than 30 lysosomal storage disorders
are known, nearly all of which are of autosomal recessive
inheritance.
This thesis deals with the genetic and molecular characterization
of genetic diseases associated with a deficiency
of lysosomal neuraminidase.
Neuraminidases (EC 3.2.1.18, sialidase, N-acetyl-neuraminosyl
glycohydrolase) catalyze the hydrolysis of neuraminic
acid residues (sialic acids) from a variety of neuraminic acid
- containing compounds. These enzymes are widely distributed
in nature and in mammalian cells they form a heterogeneous
group as far as their subcellular localization and substrate
specificity are concerned. Our experimental work has focussed
on the lysosomal neuraminidases which catalyze the cleavage of
N-acetylneurarninic acid residues from glycoproteins, oligosaccharides
and glycopeptides. The availability of an artificial
fluorogenic substrate (4-rnethylumbelliferyl-N-acetyl-neuraminic
acid) permitting a sensitive and reliable enzyme assay,
has greatly facilitated both the diagnostic work and the
research described in this thesis.
Publication Year: 1986
Publication Date: 1986-09-03
Language: en
Type: article
Access and Citation
AI Researcher Chatbot
Get quick answers to your questions about the article from our AI researcher chatbot