Assaying Lysosomal Enzyme Activity in Dictyostelium discoideum.

Autor:	Kim WD; Environmental and Life Sciences Graduate Program, Trent University, Peterborough, ON, Canada., DiGiacinto AF; Department of Biology, Trent University, Peterborough, ON, Canada., Huber RJ; Environmental and Life Sciences Graduate Program, Trent University, Peterborough, ON, Canada. roberthuber@trentu.ca.; Department of Biology, Trent University, Peterborough, ON, Canada. roberthuber@trentu.ca.
Jazyk:	angličtina
Zdroj:	Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2024; Vol. 2814, pp. 55-79.
DOI:	10.1007/978-1-0716-3894-1_4
Abstrakt:	Lysosomes are membrane-enclosed organelles that digest intracellular material. They contain more than 50 different enzymes that can degrade a variety of macromolecules including nucleic acids, proteins, polysaccharides, and lipids. In addition to functioning within lysosomes, lysosomal enzymes are also secreted. Alterations in the levels and activities of lysosomal enzymes dysregulates lysosomes, which can lead to the intralysosomal accumulation of biological material and the development of lysosomal storage diseases (LSDs) in humans. Dictyostelium discoideum has a long history of being used to study the trafficking and functions of lysosomal enzymes. More recently, it has been used as a model system to study several LSDs. In this chapter, we outline the methods for assessing the activity of several lysosomal enzymes in D. discoideum (α-galactosidase, β-galactosidase, α-glucosidase, β-glucosidase, β-N-acetylglucosaminidase, α-mannosidase, cathepsin B, cathepsin D, cathepsin F, palmitoyl protein thioesterase 1, and tripeptidyl peptidase 1). (© 2024. The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)
Databáze:	MEDLINE
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